Sodium chloride-dependent neurotransmitter symporters located primarily on the PLASMA MEMBRANE of noradrenergic neurons. They remove NOREPINEPHRINE from the EXTRACELLULAR SPACE by high affinity reuptake into PRESYNAPTIC TERMINALS. It regulates signal amplitude and duration at noradrenergic synapses and is the target of ADRENERGIC UPTAKE INHIBITORS.
A group of membrane transport proteins that transport biogenic amine derivatives of catechol across the PLASMA MEMBRANE. Catecholamine plasma membrane transporter proteins regulate neural transmission as well as catecholamine metabolism and recycling.
Membrane proteins whose primary function is to facilitate the transport of molecules across a biological membrane. Included in this broad category are proteins involved in active transport (BIOLOGICAL TRANSPORT, ACTIVE), facilitated transport and ION CHANNELS.
The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.
A family of sodium chloride-dependent neurotransmitter symporters that transport the amino acid GLYCINE. They differ from GLYCINE RECEPTORS, which signal cellular responses to GLYCINE. They are located primarily on the PLASMA MEMBRANE of NEURONS; GLIAL CELLS; EPITHELIAL CELLS; and RED BLOOD CELLS where they remove inhibitory neurotransmitter glycine from the EXTRACELLULAR SPACE.
Precursor of epinephrine that is secreted by the adrenal medulla and is a widespread central and autonomic neurotransmitter. Norepinephrine is the principal transmitter of most postganglionic sympathetic fibers and of the diffuse projection system in the brain arising from the locus ceruleus. It is also found in plants and is used pharmacologically as a sympathomimetic.
A family of plasma membrane neurotransmitter transporter proteins that couple the uptake of GLUTAMATE with the import of SODIUM ions and PROTONS and the export of POTASSIUM ions. In the CENTRAL NERVOUS SYSTEM they regulate neurotransmission through synaptic reuptake of the excitatory neurotransmitter glutamate. Outside the central nervous system they function as signal mediators and regulators of glutamate metabolism.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
A family of plasma membrane neurotransmitter transporter proteins that regulates extracellular levels of the inhibitory neurotransmitter GAMMA-AMINOBUTYRIC ACID. They differ from GABA RECEPTORS, which signal cellular responses to GAMMA-AMINOBUTYRIC ACID. They control GABA reuptake into PRESYNAPTIC TERMINALS in the CENTRAL NERVOUS SYSTEM through high-affinity sodium-dependent transport.
Membrane transporters that co-transport two or more dissimilar molecules in the same direction across a membrane. Usually the transport of one ion or molecule is against its electrochemical gradient and is "powered" by the movement of another ion or molecule with its electrochemical gradient.
A large group of membrane transport proteins that shuttle MONOSACCHARIDES across CELL MEMBRANES.
Transport proteins that carry specific substances in the blood or across cell membranes.
Proteins obtained from ESCHERICHIA COLI.
Sodium chloride-dependent neurotransmitter symporters located primarily on the PLASMA MEMBRANE of dopaminergic neurons. They remove DOPAMINE from the EXTRACELLULAR SPACE by high affinity reuptake into PRESYNAPTIC TERMINALS and are the target of DOPAMINE UPTAKE INHIBITORS.
The movement of materials across cell membranes and epithelial layers against an electrochemical gradient, requiring the expenditure of metabolic energy.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
Sodium chloride-dependent neurotransmitter symporters located primarily on the PLASMA MEMBRANE of serotonergic neurons. They are different than SEROTONIN RECEPTORS, which signal cellular responses to SEROTONIN. They remove SEROTONIN from the EXTRACELLULAR SPACE by high affinity reuptake into PRESYNAPTIC TERMINALS. Regulates signal amplitude and duration at serotonergic synapses and is the site of action of the SEROTONIN UPTAKE INHIBITORS.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A broad category of membrane transport proteins that specifically transport FREE FATTY ACIDS across cellular membranes. They play an important role in LIPID METABOLISM in CELLS that utilize free fatty acids as an energy source.
Thin structures that encapsulate subcellular structures or ORGANELLES in EUKARYOTIC CELLS. They include a variety of membranes associated with the CELL NUCLEUS; the MITOCHONDRIA; the GOLGI APPARATUS; the ENDOPLASMIC RETICULUM; LYSOSOMES; PLASTIDS; and VACUOLES.
Thin layers of tissue which cover parts of the body, separate adjacent cavities, or connect adjacent structures.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.
Lipids, predominantly phospholipids, cholesterol and small amounts of glycolipids found in membranes including cellular and intracellular membranes. These lipids may be arranged in bilayers in the membranes with integral proteins between the layers and peripheral proteins attached to the outside. Membrane lipids are required for active transport, several enzymatic activities and membrane formation.
A sequence-related subfamily of ATP-BINDING CASSETTE TRANSPORTERS that actively transport organic substrates. Although considered organic anion transporters, a subset of proteins in this family have also been shown to convey drug resistance to neutral organic drugs. Their cellular function may have clinical significance for CHEMOTHERAPY in that they transport a variety of ANTINEOPLASTIC AGENTS. Overexpression of proteins in this class by NEOPLASMS is considered a possible mechanism in the development of multidrug resistance (DRUG RESISTANCE, MULTIPLE). Although similar in function to P-GLYCOPROTEINS, the proteins in this class share little sequence homology to the p-glycoprotein family of proteins.
A family of MEMBRANE TRANSPORT PROTEINS that require ATP hydrolysis for the transport of substrates across membranes. The protein family derives its name from the ATP-binding domain found on the protein.
The voltage differences across a membrane. For cellular membranes they are computed by subtracting the voltage measured outside the membrane from the voltage measured inside the membrane. They result from differences of inside versus outside concentration of potassium, sodium, chloride, and other ions across cells' or ORGANELLES membranes. For excitable cells, the resting membrane potentials range between -30 and -100 millivolts. Physical, chemical, or electrical stimuli can make a membrane potential more negative (hyperpolarization), or less negative (depolarization).
Proteins found in any species of bacterium.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
The rate dynamics in chemical or physical systems.
The semi-permeable outer structure of a red blood cell. It is known as a red cell 'ghost' after HEMOLYSIS.
The movement of ions across energy-transducing cell membranes. Transport can be active, passive or facilitated. Ions may travel by themselves (uniport), or as a group of two or more ions in the same (symport) or opposite (antiport) directions.
A stack of flattened vesicles that functions in posttranslational processing and sorting of proteins, receiving them from the rough ENDOPLASMIC RETICULUM and directing them to secretory vesicles, LYSOSOMES, or the CELL MEMBRANE. The movement of proteins takes place by transfer vesicles that bud off from the rough endoplasmic reticulum or Golgi apparatus and fuse with the Golgi, lysosomes or cell membrane. (From Glick, Glossary of Biochemistry and Molecular Biology, 1990)
A quality of cell membranes which permits the passage of solvents and solutes into and out of cells.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
Artificially produced membranes, such as semipermeable membranes used in artificial kidney dialysis (RENAL DIALYSIS), monomolecular and bimolecular membranes used as models to simulate biological CELL MEMBRANES. These membranes are also used in the process of GUIDED TISSUE REGENERATION.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
The residual portion of BLOOD that is left after removal of BLOOD CELLS by CENTRIFUGATION without prior BLOOD COAGULATION.
Membrane proteins whose primary function is to facilitate the transport of positively charged molecules (cations) across a biological membrane.
Proteins isolated from the outer membrane of Gram-negative bacteria.
Established cell cultures that have the potential to propagate indefinitely.
Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.
A member of the alkali group of metals. It has the atomic symbol Na, atomic number 11, and atomic weight 23.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Vesicles that are involved in shuttling cargo from the interior of the cell to the cell surface, from the cell surface to the interior, across the cell or around the cell to various locations.
The motion of phospholipid molecules within the lipid bilayer, dependent on the classes of phospholipids present, their fatty acid composition and degree of unsaturation of the acyl chains, the cholesterol concentration, and temperature.
Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.
Membrane proteins whose primary function is to facilitate the transport of negatively charged molecules (anions) across a biological membrane.
Cytoplasmic vesicles formed when COATED VESICLES shed their CLATHRIN coat. Endosomes internalize macromolecules bound by receptors on the cell surface.
A broad category of proteins involved in the formation, transport and dissolution of TRANSPORT VESICLES. They play a role in the intracellular transport of molecules contained within membrane vesicles. Vesicular transport proteins are distinguished from MEMBRANE TRANSPORT PROTEINS, which move molecules across membranes, by the mode in which the molecules are transported.
Glycoproteins found on the membrane or surface of cells.
Elements of limited time intervals, contributing to particular results or situations.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Microscopy of specimens stained with fluorescent dye (usually fluorescein isothiocyanate) or of naturally fluorescent materials, which emit light when exposed to ultraviolet or blue light. Immunofluorescence microscopy utilizes antibodies that are labeled with fluorescent dye.
A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)
An element in the alkali group of metals with an atomic symbol K, atomic number 19, and atomic weight 39.10. It is the chief cation in the intracellular fluid of muscle and other cells. Potassium ion is a strong electrolyte that plays a significant role in the regulation of fluid volume and maintenance of the WATER-ELECTROLYTE BALANCE.

A previously undescribed intron and extensive 5' upstream sequence, but not Phox2a-mediated transactivation, are necessary for high level cell type-specific expression of the human norepinephrine transporter gene. (1/346)

The synaptic action of norepinephrine is terminated by NaCl-dependent uptake into presynaptic noradrenergic nerve endings, mediated by the norepinephrine transporter (NET). NET is expressed only in neuronal tissues that synthesize and secrete norepinephrine and in most cases is co-expressed with the norepinephrine-synthetic enzyme dopamine beta-hydroxylase (DBH). To understand the molecular mechanisms regulating human NET (hNET) gene expression, we isolated and characterized an hNET genomic clone encompassing approximately 9. 5 kilobase pairs of the 5' upstream promoter region. Here we demonstrate that the hNET gene contains an as-yet-unidentified intron of 476 base pairs within the 5'-untranslated region. Furthermore, both primer extension and 5'-rapid amplification of cDNA ends analyses identified multiple transcription start sites from mRNAs expressed only in NET-expressing cell lines. The start sites clustered in two subdomains, each preceded by a TATA-like sequence motif. As expected for mature mRNAs, transcripts from most of these sites each contained an additional G residue at the 5' position. Together, the data strongly support the authenticity of these sites as the transcriptional start sites of hNET. We assembled hNET-chloramphenicol acetyltransferase reporter constructs containing different lengths of hNET 5' sequence in the presence or the absence of the first intron. Transient transfection assays indicated that the combination of the 5' upstream sequence and the first intron supported the highest level of noradrenergic cell-specific transcription. Forced expression of the paired-like homeodomain transcription factor Phox2a did not affect hNET promoter activity in NET-negative cell lines, in marked contrast to its effect on a DBH-chloramphenicol acetyltransferase reporter construct. Together with our previous studies suggesting a critical role of Phox2a for noradrenergic-specific expression of the DBH gene, these data support a model in which distinct, or partially distinct, molecular mechanisms regulate cell-specific expression of the NET and DBH genes.  (+info)

Dominant negative isoform of rat norepinephrine transporter produced by alternative RNA splicing. (2/346)

We have cloned from rat brain a family of alternatively spliced cDNAs from a single gene, which encodes a norepinephrine transporter (NET) having variations at the 3'-region including both coding and noncoding regions. This produces two transporter isoforms, rNETa and rNETb, which differ at their COOH termini. The rNETa isoform reveals a COOH terminus homologous to human NET and transports norepinephrine. In contrast, rNETb revealed no detectable transport function but reduced functional expression of rNETa when both isoforms were expressed in the same cell. Thus, rNETb potentially functions as a dominant negative inhibitor of rNETa activity. Co-expression of rNETb with a gamma-aminobutyric acid transporter (rGAT1), a serotonin transporter (rSERT), and a dopamine transporter (rDAT) reduced their transport activity. No reduction was found with the glutamate/aspartate transporter (rGLAST). Alternative RNA splicing of NET suggests a novel mechanism for the regulation of synaptic transmission.  (+info)

Characteristics of drug interactions with recombinant biogenic amine transporters expressed in the same cell type. (3/346)

We characterized the effects of drugs on the uptake of [3H]neurotransmitter by and the binding of [125I](3beta-(4-iodophenyl)tropane-2beta-carboxylic acid methyl ester ([125I]RTI-55) to the recombinant human dopamine (hDAT), serotonin (hSERT), or norepinephrine (hNET) transporters stably expressed in human embryonic kidney 293 cells. RTI-55 had similar affinity for the hDAT and hSERT and lower affinity for hNET (Kd = 1. 83, 0.98, and 12.1 nM, respectively). Kinetic analysis of [125I]RTI-55 binding indicated that the dissociation rate (k-1) was significantly lower for hSERT and the association rate (k+1) was significantly lower for hNET compared with the hDAT. The potency of drugs at blocking [3H]neurotransmitter uptake was highly correlated with potency at blocking radioligand binding for hDAT and hSERT. Substrates were more potent at the inhibition of [3H]neurotransmitter uptake than radioligand binding. The potency of drugs was highly correlated between displacement of [3H]nisoxetine (Kd = 6.0 nM) and [125I]RTI-55 from the hNET, suggesting that these radioligands recognize similar sites on the transporter protein. The correlation observed between inhibitory potency for uptake and binding of either ligand at the hNET was lower than correlations between uptake and binding for hDAT and hSERT. The present results indicate that the cocaine analog [125I]RTI-55 has unique binding properties at each of the transporters and that the use of recombinant transporters expressed by a single cell type can provide a powerful screening tool for drugs interacting with biogenic amine transporters, such as possible cocaine antagonists.  (+info)

Comparison of the pharmacological properties of cloned rat, human, and bovine norepinephrine transporters. (4/346)

The aims of this study were to characterize the recently cloned rat norepinephrine transporter (NET) in more detail and in particular to study possible species differences in its pharmacological properties compared with the human and bovine NETs. The study was carried out by measuring the uptake of [(3)H]norepinephrine in COS-7 cells expressing the NET after transient transfection with rat, human, or bovine NET cDNA. There were small but significant differences between the rat NET and the human or bovine NETs with respect to the affinities of sodium ions (greater for rat than for bovine) of the substrates norepinephrine, epinephrine, and 1-methyl-4-phenylpyridinium (greater for human than for rat), and of the inhibitor cocaine (greater for human and bovine than for rat), whereas the affinities of dopamine and of most inhibitors, including tricyclic antidepressants, showed no species differences. The fact that the affinities for some substrates, cocaine and sodium ions exhibited small but significant interspecies differences among the rat, human, and bovine NETs suggests that ligand recognition, the translocation process, and sodium ion dependence are influenced differentially by just a few amino acid exchanges in the primary sequences of the transporters. On the other hand, the lack of any major differences in the pharmacological properties of the rat, human, and bovine NETs in this study suggests that data obtained in previous studies on rat tissues and bovine cells can be extrapolated, in all except the most quantitative analyses, to the properties of the human NET.  (+info)

Noradrenaline transporter gene transfer for radiation cell kill by 131I meta-iodobenzylguanidine. (5/346)

Meta-iodobenzylguanidine conjugated to 131I-iodine is an effective agent for the targeted radiotherapy of tumors of neural crest origin which express the noradrenaline transporter (NAT). The therapeutic application of 131I MIBG is presently limited to the treatment of phaeochromocytoma, neuroblastoma, carcinoid and medullary thyroid carcinoma. To determine the feasibility of MIBG targeting for a wider range of tumor types, we employed plasmid-mediated transfer of the NAT gene into a human glioblastoma cell line (UVW) which does not express the NAT gene. This resulted in a 15-fold increase in uptake of MIBG by the host cells. A dose-dependent toxicity of 131I MIBG to the transfectants was demonstrated using three methods: (1) survival of clonogens derived from monolayer culture; (2) survival of clonogens derived from disaggregated multicellular spheroids; and (3) spheroid growth delay. 131I MIBG was twice as toxic to cells in spheroids compared with those in monolayers, consistent with a greater effect of radiation cross-fire (radiological bystander effect) from 131I beta-radiation in the three-dimensional tumor spheroids. The highest concentration of 131I MIBG tested (1 MBq/ml) was nontoxic to UVW control cells or spheroids transfected with the NAT gene in reverse orientation. These findings are encouraging for the development of NAT gene transfer-mediated 131I MIBG therapy.  (+info)

Catechol-O-methyltransferase activity in CHO cells expressing norepinephrine transporter. (6/346)

1. We examined the existence of catecholamine metabolizing enzymes (catechol-O-methyltransferase, COMT, and monoamine oxidase, MAO) in CHO cells transfected with norepinephrine (NE) transporter (NET) cDNA. 2. NET activity was studied by incubating cells with [3H]-NE (0. 5 microCi ml-1, 20 min) in a Na+ containing medium. Incubation with [3H]-NE lead to [3H] accumulation at 47797+/-4864 d.p.m. per well. Specific inhibitors of NET abolished this uptake. 3. During post-uptake incubation, [3H] leaked rapidly from cells and the extracellular phase comprised 89% of total radioactivity within 40 min. Both [3H] retention and [3H] 'leakage' were largely unaffected by inhibitors for MAO. In contrast, COMT inhibitors, U-0521 and Ro 41-0960, dose-dependently increased intracellular [3H]-NE retention with a maximal increase of 4.5 fold. The EC50 for Ro 41-0960 was 139-times lower than that of U-0521. U-0521 largely inhibited [3H] 'leakage' and doubled the apparent Vmax for [3H]-NE uptake. 4. Addition of U-0521 during uptake incubation increased intracellular NE content by 8 fold. Normetanephrine, the COMT-dependent metabolite of NE, was formed in large quantities during post-uptake incubation. U-0521 significantly inhibited the formation of NMN with an equal preservation of intracellular NE. 5. CHO cells expressing NET possess COMT activity, which is responsible for the metabolism of NE to form lipophilic metabolite normetanephrine. The apparent 'properties' of the NET function expressed in CHO cells changed, after inhibition of COMT, in such a way closer to that described in the native neuronal preparations.  (+info)

Ion dependence of carrier-mediated release in dopamine or norepinephrine transporter-transfected cells questions the hypothesis of facilitated exchange diffusion. (7/346)

The mechanism of release mediated by the human dopamine and norepinephrine transporter (DAT and NET, respectively) was studied by a superfusion technique in human embryonic kidney 293 cells stably transfected with the respective transporter cDNA and loaded with the metabolically inert substrate [(3)H]1-methyl-4-phenylpyridinium. Release was induced by amphetamine, dopamine, and norepinephrine or by lowering the sodium or chloride concentration in the superfusion buffer (iso-osmotic replacement by lithium and isethionate, respectively). Efflux of [(3)H]1-methyl-4-phenylpyridinium was analyzed at 30-s time resolution. In both transporters, release induced by the substrates amphetamine, dopamine, and norepinephrine followed the same time course as release induced by the removal of chloride and was faster than that caused by the removal of sodium. In the presence of low sodium (DAT: 10 mM; NET: 5 mM) none of the substrates was able to induce release from either type of cell, but adding back sodium to control conditions promptly restored the releasing action. In the presence of low chloride (DAT: 3 mM; NET: 2 mM), however, amphetamine as well as the catecholamines stimulated release from both types of cell. In contrast with the ion dependence of release observed in superfusion experiments, uptake initial rates of substrates at concentrations used in release experiments were the same or even higher at low sodium than at low chloride. The results indicate a decisive role of extracellular sodium for carrier-mediated release unrelated to the sodium-dependent uptake of the releasing substrate, and suggest a release mechanism different from simple exchange diffusion considering only the amines as substrates.  (+info)

Changes in tyrosine hydroxylase mRNA expression in the rat locus coeruleus following acute or chronic treatment with valproic acid. (8/346)

Valproate has proven effective in treating bipolar disorder. Though some biochemical effects of valproate are rapid, mood-stabilizing effects can take weeks, suggesting that regulatory changes in gene expression in brain neurotransmitter systems may be involved. Given a presumed role for norepinephrine (NE) in bipolar disorder, as well as the actions of mood-stabilizing drugs, we examined changes in mRNA expression for tyrosine hydroxylase (TH), the NE transporter (NET) and alpha 2A autoreceptor in the rat locus coeruleus after valproate treatment. TH mRNA increased slightly (16%) following acute treatment, and more so after chronic valproate treatment (26%), while neither NET nor alpha 2A mRNA expression changed. Further, chronic valproate treatment attenuated the elevation in TH mRNA expression induced in the LC in response to acute restraint stress. Both acute and chronic valproate treatment attenuated restraint stress-induced elevations in plasma ACTH secretion. These observations suggest that the therapeutic effects of valproate may involve regulatory alterations in TH message expression in the brain, and attenuation of stress-reactivity of the central noradrenergic system and the hypothalamic-pituitary-adrenal axis.  (+info)

Norepinephrine plasma membrane transport proteins, also known as norepinephrine transporters (NET), are membrane-bound proteins that play a crucial role in the regulation of neurotransmission. They are responsible for the reuptake of norepinephrine from the synaptic cleft back into the presynaptic neuron, thereby terminating the signal transmission and preventing excessive stimulation of postsynaptic receptors.

The norepinephrine transporter is a member of the sodium-dependent neurotransmitter transporter family and functions as an antiporter, exchanging one intracellular sodium ion for two extracellular sodium ions along with the transport of norepinephrine. This sodium gradient provides the energy required for the active transport process.

Dysregulation of norepinephrine plasma membrane transport proteins has been implicated in various neurological and psychiatric disorders, such as attention deficit hyperactivity disorder (ADHD), depression, and post-traumatic stress disorder (PTSD). Therefore, understanding the function and regulation of these transporters is essential for developing novel therapeutic strategies to treat these conditions.

Catecholamine plasma membrane transport proteins, also known as neurotransmitter transporters or simply transporters, are a type of membrane protein responsible for the reuptake of catecholamines (such as dopamine, norepinephrine, and epinephrine) from the synaptic cleft back into the presynaptic neuron. These proteins play a crucial role in regulating neurotransmitter concentrations in the synapse and terminating neurotransmission. They are targets for various psychoactive drugs, including antidepressants, psychostimulants, and cocaine.

Membrane transport proteins are specialized biological molecules, specifically integral membrane proteins, that facilitate the movement of various substances across the lipid bilayer of cell membranes. They are responsible for the selective and regulated transport of ions, sugars, amino acids, nucleotides, and other molecules into and out of cells, as well as within different cellular compartments. These proteins can be categorized into two main types: channels and carriers (or pumps). Channels provide a passive transport mechanism, allowing ions or small molecules to move down their electrochemical gradient, while carriers actively transport substances against their concentration gradient, requiring energy usually in the form of ATP. Membrane transport proteins play a crucial role in maintaining cell homeostasis, signaling processes, and many other physiological functions.

Biological transport refers to the movement of molecules, ions, or solutes across biological membranes or through cells in living organisms. This process is essential for maintaining homeostasis, regulating cellular functions, and enabling communication between cells. There are two main types of biological transport: passive transport and active transport.

Passive transport does not require the input of energy and includes:

1. Diffusion: The random movement of molecules from an area of high concentration to an area of low concentration until equilibrium is reached.
2. Osmosis: The diffusion of solvent molecules (usually water) across a semi-permeable membrane from an area of lower solute concentration to an area of higher solute concentration.
3. Facilitated diffusion: The assisted passage of polar or charged substances through protein channels or carriers in the cell membrane, which increases the rate of diffusion without consuming energy.

Active transport requires the input of energy (in the form of ATP) and includes:

1. Primary active transport: The direct use of ATP to move molecules against their concentration gradient, often driven by specific transport proteins called pumps.
2. Secondary active transport: The coupling of the movement of one substance down its electrochemical gradient with the uphill transport of another substance, mediated by a shared transport protein. This process is also known as co-transport or counter-transport.

Glycine is an important amino acid that plays a role in various physiological processes in the human body. Plasma membrane transport proteins are specialized molecules found in the cell membrane that facilitate the movement of specific molecules, such as ions or neurotransmitters like glycine, into and out of cells.

Glycine plasma membrane transport proteins specifically regulate the transcellular movement of glycine across the plasma membrane. These transport proteins belong to a family of solute carriers (SLC) known as the glycine transporters (GlyTs). There are two main isoforms, GlyT1 and GlyT2, which differ in their distribution, function, and regulation.

GlyT1 is widely expressed throughout the central nervous system and plays a crucial role in terminating glycinergic neurotransmission by rapidly removing glycine from the synaptic cleft. This isoform is also involved in regulating extracellular glycine concentrations in various tissues, including the brainstem, spinal cord, and retina.

GlyT2, on the other hand, is primarily localized to presynaptic terminals of glycinergic neurons, where it functions as a vesicular glycine transporter (VGT). Its primary role is to transport glycine into synaptic vesicles for subsequent release into the synapse during neurotransmission.

Dysfunction in glycine plasma membrane transport proteins has been implicated in several neurological disorders, such as hyperekplexia (startle disease) and certain forms of epilepsy. In these cases, impaired glycinergic neurotransmission can lead to motor and cognitive deficits, highlighting the importance of proper glycine transport protein function for normal physiological processes.

Norepinephrine, also known as noradrenaline, is a neurotransmitter and a hormone that is primarily produced in the adrenal glands and is released into the bloodstream in response to stress or physical activity. It plays a crucial role in the "fight-or-flight" response by preparing the body for action through increasing heart rate, blood pressure, respiratory rate, and glucose availability.

As a neurotransmitter, norepinephrine is involved in regulating various functions of the nervous system, including attention, perception, motivation, and arousal. It also plays a role in modulating pain perception and responding to stressful or emotional situations.

In medical settings, norepinephrine is used as a vasopressor medication to treat hypotension (low blood pressure) that can occur during septic shock, anesthesia, or other critical illnesses. It works by constricting blood vessels and increasing heart rate, which helps to improve blood pressure and perfusion of vital organs.

Glutamate plasma membrane transport proteins, also known as excitatory amino acid transporters (EAATs), are a type of membrane protein responsible for the uptake of glutamate from the extracellular space into neurons and glial cells in the central nervous system. These transporters play a crucial role in maintaining appropriate levels of glutamate, an important neurotransmitter, in the synaptic cleft to prevent excitotoxicity and ensure normal neurotransmission. There are five subtypes of EAATs (EAAT1-EAAT5) identified in mammals, each with distinct expression patterns and functions.

A cell membrane, also known as the plasma membrane, is a thin semi-permeable phospholipid bilayer that surrounds all cells in animals, plants, and microorganisms. It functions as a barrier to control the movement of substances in and out of the cell, allowing necessary molecules such as nutrients, oxygen, and signaling molecules to enter while keeping out harmful substances and waste products. The cell membrane is composed mainly of phospholipids, which have hydrophilic (water-loving) heads and hydrophobic (water-fearing) tails. This unique structure allows the membrane to be flexible and fluid, yet selectively permeable. Additionally, various proteins are embedded in the membrane that serve as channels, pumps, receptors, and enzymes, contributing to the cell's overall functionality and communication with its environment.

GABA (gamma-aminobutyric acid) is the primary inhibitory neurotransmitter in the mammalian central nervous system. GABA plasma membrane transport proteins, also known as GATs (GABA transporters), are a family of membrane-spanning proteins responsible for the uptake of GABA from the extracellular space into neurons and glial cells.

There are four main subtypes of GATs in mammals, named GAT1, GAT2, GAT3, and Betaine/GABA transporter 1 (BGT1). These transport proteins play a crucial role in terminating the synaptic transmission of GABA and regulating its concentration in the extracellular space. They also help maintain the balance between excitation and inhibition in the central nervous system.

GATs are targets for various pharmacological interventions, as modulation of their activity can affect GABAergic neurotransmission and have therapeutic potential in treating several neurological disorders, such as epilepsy, anxiety, and chronic pain.

A symporter is a type of transmembrane protein that functions to transport two or more molecules or ions across a biological membrane in the same direction, simultaneously. This process is called co-transport and it is driven by the concentration gradient of one of the substrates, which is usually an ion such as sodium (Na+) or proton (H+).

Symporters are classified based on the type of energy that drives the transport process. Primary active transporters, such as symporters, use the energy from ATP hydrolysis or from the electrochemical gradient of ions to move substrates against their concentration gradient. In contrast, secondary active transporters use the energy stored in an existing electrochemical gradient of one substrate to drive the transport of another substrate against its own concentration gradient.

Symporters play important roles in various physiological processes, including nutrient uptake, neurotransmitter reuptake, and ion homeostasis. For example, the sodium-glucose transporter (SGLT) is a symporter that co-transports glucose and sodium ions across the intestinal epithelium and the renal proximal tubule, contributing to glucose absorption and regulation of blood glucose levels. Similarly, the dopamine transporter (DAT) is a symporter that co-transports dopamine and sodium ions back into presynaptic neurons, terminating the action of dopamine in the synapse.

Monosaccharide transport proteins are a type of membrane transport protein that facilitate the passive or active transport of monosaccharides, such as glucose, fructose, and galactose, across cell membranes. These proteins play a crucial role in the absorption, distribution, and metabolism of carbohydrates in the body.

There are two main types of monosaccharide transport proteins: facilitated diffusion transporters and active transporters. Facilitated diffusion transporters, also known as glucose transporters (GLUTs), passively transport monosaccharides down their concentration gradient without the need for energy. In contrast, active transporters, such as the sodium-glucose cotransporter (SGLT), use energy in the form of ATP to actively transport monosaccharides against their concentration gradient.

Monosaccharide transport proteins are found in various tissues throughout the body, including the intestines, kidneys, liver, and brain. They play a critical role in maintaining glucose homeostasis by regulating the uptake and release of glucose into and out of cells. Dysfunction of these transporters has been implicated in several diseases, such as diabetes, cancer, and neurological disorders.

Carrier proteins, also known as transport proteins, are a type of protein that facilitates the movement of molecules across cell membranes. They are responsible for the selective and active transport of ions, sugars, amino acids, and other molecules from one side of the membrane to the other, against their concentration gradient. This process requires energy, usually in the form of ATP (adenosine triphosphate).

Carrier proteins have a specific binding site for the molecule they transport, and undergo conformational changes upon binding, which allows them to move the molecule across the membrane. Once the molecule has been transported, the carrier protein returns to its original conformation, ready to bind and transport another molecule.

Carrier proteins play a crucial role in maintaining the balance of ions and other molecules inside and outside of cells, and are essential for many physiological processes, including nerve impulse transmission, muscle contraction, and nutrient uptake.

'Escherichia coli (E. coli) proteins' refer to the various types of proteins that are produced and expressed by the bacterium Escherichia coli. These proteins play a critical role in the growth, development, and survival of the organism. They are involved in various cellular processes such as metabolism, DNA replication, transcription, translation, repair, and regulation.

E. coli is a gram-negative, facultative anaerobe that is commonly found in the intestines of warm-blooded organisms. It is widely used as a model organism in scientific research due to its well-studied genetics, rapid growth, and ability to be easily manipulated in the laboratory. As a result, many E. coli proteins have been identified, characterized, and studied in great detail.

Some examples of E. coli proteins include enzymes involved in carbohydrate metabolism such as lactase, sucrase, and maltose; proteins involved in DNA replication such as the polymerases, single-stranded binding proteins, and helicases; proteins involved in transcription such as RNA polymerase and sigma factors; proteins involved in translation such as ribosomal proteins, tRNAs, and aminoacyl-tRNA synthetases; and regulatory proteins such as global regulators, two-component systems, and transcription factors.

Understanding the structure, function, and regulation of E. coli proteins is essential for understanding the basic biology of this important organism, as well as for developing new strategies for combating bacterial infections and improving industrial processes involving bacteria.

Dopamine plasma membrane transport proteins, also known as dopamine transporters (DAT), are a type of protein found in the cell membrane that play a crucial role in the regulation of dopamine neurotransmission. They are responsible for the reuptake of dopamine from the synaptic cleft back into the presynaptic neuron, thereby terminating the signal transduction of dopamine and regulating the amount of dopamine available for further release.

Dopamine transporters belong to the family of sodium-dependent neurotransmitter transporters and are encoded by the SLC6A3 gene in humans. Abnormalities in dopamine transporter function have been implicated in several neurological and psychiatric disorders, including Parkinson's disease, attention deficit hyperactivity disorder (ADHD), and substance use disorders.

In summary, dopamine plasma membrane transport proteins are essential for the regulation of dopamine neurotransmission by mediating the reuptake of dopamine from the synaptic cleft back into the presynaptic neuron.

Biological transport, active is the process by which cells use energy to move materials across their membranes from an area of lower concentration to an area of higher concentration. This type of transport is facilitated by specialized proteins called transporters or pumps that are located in the cell membrane. These proteins undergo conformational changes to physically carry the molecules through the lipid bilayer of the membrane, often against their concentration gradient.

Active transport requires energy because it works against the natural tendency of molecules to move from an area of higher concentration to an area of lower concentration, a process known as diffusion. Cells obtain this energy in the form of ATP (adenosine triphosphate), which is produced through cellular respiration.

Examples of active transport include the uptake of glucose and amino acids into cells, as well as the secretion of hormones and neurotransmitters. The sodium-potassium pump, which helps maintain resting membrane potential in nerve and muscle cells, is a classic example of an active transporter.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Membrane proteins are a type of protein that are embedded in the lipid bilayer of biological membranes, such as the plasma membrane of cells or the inner membrane of mitochondria. These proteins play crucial roles in various cellular processes, including:

1. Cell-cell recognition and signaling
2. Transport of molecules across the membrane (selective permeability)
3. Enzymatic reactions at the membrane surface
4. Energy transduction and conversion
5. Mechanosensation and signal transduction

Membrane proteins can be classified into two main categories: integral membrane proteins, which are permanently associated with the lipid bilayer, and peripheral membrane proteins, which are temporarily or loosely attached to the membrane surface. Integral membrane proteins can further be divided into three subcategories based on their topology:

1. Transmembrane proteins, which span the entire width of the lipid bilayer with one or more alpha-helices or beta-barrels.
2. Lipid-anchored proteins, which are covalently attached to lipids in the membrane via a glycosylphosphatidylinositol (GPI) anchor or other lipid modifications.
3. Monotopic proteins, which are partially embedded in the membrane and have one or more domains exposed to either side of the bilayer.

Membrane proteins are essential for maintaining cellular homeostasis and are targets for various therapeutic interventions, including drug development and gene therapy. However, their structural complexity and hydrophobicity make them challenging to study using traditional biochemical methods, requiring specialized techniques such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and single-particle cryo-electron microscopy (cryo-EM).

Serotonin plasma membrane transport proteins, also known as serotonin transporters (SERTs), are membrane-spanning proteins that play a crucial role in the regulation of serotonergic neurotransmission. They are responsible for the reuptake of serotonin (5-hydroxytryptamine or 5-HT) from the synaptic cleft back into the presynaptic neuron, thereby terminating the signal transmission and allowing for its recycling or degradation.

Structurally, SERTs belong to the family of sodium- and chloride-dependent neurotransmitter transporters and contain 12 transmembrane domains with intracellular N- and C-termini. The binding site for serotonin is located within the transmembrane domain, while the substrate-binding site is formed by residues from both the transmembrane and extracellular loops.

Serotonin transporters are important targets for various psychotropic medications, including selective serotonin reuptake inhibitors (SSRIs), tricyclic antidepressants (TCAs), and monoamine oxidase inhibitors (MAOIs). These drugs act by blocking the SERT, increasing synaptic concentrations of serotonin, and enhancing serotonergic neurotransmission. Dysregulation of serotonin transporters has been implicated in several neurological and psychiatric disorders, such as major depressive disorder, anxiety disorders, obsessive-compulsive disorder, and substance abuse.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Fatty acid transport proteins (FATPs) are a group of membrane-bound proteins that play a crucial role in the uptake and transport of long-chain fatty acids across the plasma membrane of cells. They are widely expressed in various tissues, including the heart, muscle, adipose tissue, and liver.

FATPs have several domains that enable them to perform their functions, including a cytoplasmic domain that binds to fatty acids, a transmembrane domain that spans the plasma membrane, and an ATP-binding cassette (ABC) domain that hydrolyzes ATP to provide energy for fatty acid transport.

FATPs also play a role in the regulation of intracellular lipid metabolism by modulating the activity of enzymes involved in fatty acid activation, desaturation, and elongation. Mutations in FATP genes have been associated with various metabolic disorders, including congenital deficiency of long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD), a rare autosomal recessive disorder that affects fatty acid oxidation.

In summary, fatty acid transport proteins are essential for the uptake and metabolism of long-chain fatty acids in cells and have implications in various metabolic disorders.

Intracellular membranes refer to the membrane structures that exist within a eukaryotic cell (excluding bacteria and archaea, which are prokaryotic and do not have intracellular membranes). These membranes compartmentalize the cell, creating distinct organelles or functional regions with specific roles in various cellular processes.

Major types of intracellular membranes include:

1. Nuclear membrane (nuclear envelope): A double-membraned structure that surrounds and protects the genetic material within the nucleus. It consists of an outer and inner membrane, perforated by nuclear pores that regulate the transport of molecules between the nucleus and cytoplasm.
2. Endoplasmic reticulum (ER): An extensive network of interconnected tubules and sacs that serve as a major site for protein folding, modification, and lipid synthesis. The ER has two types: rough ER (with ribosomes on its surface) and smooth ER (without ribosomes).
3. Golgi apparatus/Golgi complex: A series of stacked membrane-bound compartments that process, sort, and modify proteins and lipids before they are transported to their final destinations within the cell or secreted out of the cell.
4. Lysosomes: Membrane-bound organelles containing hydrolytic enzymes for breaking down various biomolecules (proteins, carbohydrates, lipids, and nucleic acids) in the process called autophagy or from outside the cell via endocytosis.
5. Peroxisomes: Single-membrane organelles involved in various metabolic processes, such as fatty acid oxidation and detoxification of harmful substances like hydrogen peroxide.
6. Vacuoles: Membrane-bound compartments that store and transport various molecules, including nutrients, waste products, and enzymes. Plant cells have a large central vacuole for maintaining turgor pressure and storing metabolites.
7. Mitochondria: Double-membraned organelles responsible for generating energy (ATP) through oxidative phosphorylation and other metabolic processes, such as the citric acid cycle and fatty acid synthesis.
8. Chloroplasts: Double-membraned organelles found in plant cells that convert light energy into chemical energy during photosynthesis, producing oxygen and organic compounds (glucose) from carbon dioxide and water.
9. Endoplasmic reticulum (ER): A network of interconnected membrane-bound tubules involved in protein folding, modification, and transport; it is divided into two types: rough ER (with ribosomes on the surface) and smooth ER (without ribosomes).
10. Nucleus: Double-membraned organelle containing genetic material (DNA) and associated proteins involved in replication, transcription, RNA processing, and DNA repair. The nuclear membrane separates the nucleoplasm from the cytoplasm and contains nuclear pores for transporting molecules between the two compartments.

In medical terms, membranes refer to thin layers of tissue that cover or line various structures in the body. They are composed of connective tissue and epithelial cells, and they can be found lining the outer surface of the body, internal organs, blood vessels, and nerves. There are several types of membranes in the human body, including:

1. Serous Membranes: These membranes line the inside of body cavities and cover the organs contained within them. They produce a lubricating fluid that reduces friction between the organ and the cavity wall. Examples include the pleura (lungs), pericardium (heart), and peritoneum (abdominal cavity).
2. Mucous Membranes: These membranes line the respiratory, gastrointestinal, and genitourinary tracts, as well as the inner surface of the eyelids and the nasal passages. They produce mucus to trap particles, bacteria, and other substances, which helps protect the body from infection.
3. Synovial Membranes: These membranes line the joint cavities and produce synovial fluid, which lubricates the joints and allows for smooth movement.
4. Meninges: These are three layers of membranes that cover and protect the brain and spinal cord. They include the dura mater (outermost layer), arachnoid mater (middle layer), and pia mater (innermost layer).
5. Amniotic Membrane: This is a thin, transparent membrane that surrounds and protects the fetus during pregnancy. It produces amniotic fluid, which provides a cushion for the developing baby and helps regulate its temperature.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Protein transport, in the context of cellular biology, refers to the process by which proteins are actively moved from one location to another within or between cells. This is a crucial mechanism for maintaining proper cell function and regulation.

Intracellular protein transport involves the movement of proteins within a single cell. Proteins can be transported across membranes (such as the nuclear envelope, endoplasmic reticulum, Golgi apparatus, or plasma membrane) via specialized transport systems like vesicles and transport channels.

Intercellular protein transport refers to the movement of proteins from one cell to another, often facilitated by exocytosis (release of proteins in vesicles) and endocytosis (uptake of extracellular substances via membrane-bound vesicles). This is essential for communication between cells, immune response, and other physiological processes.

It's important to note that any disruption in protein transport can lead to various diseases, including neurological disorders, cancer, and metabolic conditions.

Membrane lipids are the main component of biological membranes, forming a lipid bilayer in which various cellular processes take place. These lipids include phospholipids, glycolipids, and cholesterol. Phospholipids are the most abundant type, consisting of a hydrophilic head (containing a phosphate group) and two hydrophobic tails (composed of fatty acid chains). Glycolipids contain a sugar group attached to the lipid molecule. Cholesterol helps regulate membrane fluidity and permeability. Together, these lipids create a selectively permeable barrier that separates cells from their environment and organelles within cells.

Multidrug Resistance-Associated Proteins (MRPs) are a subfamily of ATP-binding cassette (ABC) transporter proteins that play a crucial role in the efflux of various substrates, including drugs and organic anions, out of cells. They are located in the plasma membrane of many cell types, including epithelial cells in the liver, intestine, kidney, and blood-brain barrier.

MRPs are known to transport a wide range of molecules, such as glutathione conjugates, bilirubin, bile acids, and various clinical drugs. One of the most well-known MRPs is MRP1 (ABCC1), which was initially identified in drug-resistant tumor cells. MRP1 can confer resistance to chemotherapeutic agents by actively pumping them out of cancer cells, thereby reducing their intracellular concentration and effectiveness.

The activity of MRPs can have significant implications for the pharmacokinetics and pharmacodynamics of drugs, as they can affect drug absorption, distribution, metabolism, and excretion (ADME). Understanding the function and regulation of MRPs is essential for developing strategies to overcome multidrug resistance in cancer therapy and optimizing drug dosing regimens in various clinical settings.

ATP-binding cassette (ABC) transporters are a family of membrane proteins that utilize the energy from ATP hydrolysis to transport various substrates across extra- and intracellular membranes. These transporters play crucial roles in several biological processes, including detoxification, drug resistance, nutrient uptake, and regulation of cellular cholesterol homeostasis.

The structure of ABC transporters consists of two nucleotide-binding domains (NBDs) that bind and hydrolyze ATP, and two transmembrane domains (TMDs) that form the substrate-translocation pathway. The NBDs are typically located adjacent to each other in the cytoplasm, while the TMDs can be either integral membrane domains or separate structures associated with the membrane.

The human genome encodes 48 distinct ABC transporters, which are classified into seven subfamilies (ABCA-ABCG) based on their sequence similarity and domain organization. Some well-known examples of ABC transporters include P-glycoprotein (ABCB1), multidrug resistance protein 1 (ABCC1), and breast cancer resistance protein (ABCG2).

Dysregulation or mutations in ABC transporters have been implicated in various diseases, such as cystic fibrosis, neurological disorders, and cancer. In cancer, overexpression of certain ABC transporters can contribute to drug resistance by actively effluxing chemotherapeutic agents from cancer cells, making them less susceptible to treatment.

Membrane potential is the electrical potential difference across a cell membrane, typically for excitable cells such as nerve and muscle cells. It is the difference in electric charge between the inside and outside of a cell, created by the selective permeability of the cell membrane to different ions. The resting membrane potential of a typical animal cell is around -70 mV, with the interior being negative relative to the exterior. This potential is generated and maintained by the active transport of ions across the membrane, primarily through the action of the sodium-potassium pump. Membrane potentials play a crucial role in many physiological processes, including the transmission of nerve impulses and the contraction of muscle cells.

Bacterial proteins are a type of protein that are produced by bacteria as part of their structural or functional components. These proteins can be involved in various cellular processes, such as metabolism, DNA replication, transcription, and translation. They can also play a role in bacterial pathogenesis, helping the bacteria to evade the host's immune system, acquire nutrients, and multiply within the host.

Bacterial proteins can be classified into different categories based on their function, such as:

1. Enzymes: Proteins that catalyze chemical reactions in the bacterial cell.
2. Structural proteins: Proteins that provide structural support and maintain the shape of the bacterial cell.
3. Signaling proteins: Proteins that help bacteria to communicate with each other and coordinate their behavior.
4. Transport proteins: Proteins that facilitate the movement of molecules across the bacterial cell membrane.
5. Toxins: Proteins that are produced by pathogenic bacteria to damage host cells and promote infection.
6. Surface proteins: Proteins that are located on the surface of the bacterial cell and interact with the environment or host cells.

Understanding the structure and function of bacterial proteins is important for developing new antibiotics, vaccines, and other therapeutic strategies to combat bacterial infections.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

An erythrocyte, also known as a red blood cell, is a type of cell that circulates in the blood and is responsible for transporting oxygen throughout the body. The erythrocyte membrane refers to the thin, flexible barrier that surrounds the erythrocyte and helps to maintain its shape and stability.

The erythrocyte membrane is composed of a lipid bilayer, which contains various proteins and carbohydrates. These components help to regulate the movement of molecules into and out of the erythrocyte, as well as provide structural support and protection for the cell.

The main lipids found in the erythrocyte membrane are phospholipids and cholesterol, which are arranged in a bilayer structure with the hydrophilic (water-loving) heads facing outward and the hydrophobic (water-fearing) tails facing inward. This arrangement helps to maintain the integrity of the membrane and prevent the leakage of cellular components.

The proteins found in the erythrocyte membrane include integral proteins, which span the entire width of the membrane, and peripheral proteins, which are attached to the inner or outer surface of the membrane. These proteins play a variety of roles, such as transporting molecules across the membrane, maintaining the shape of the erythrocyte, and interacting with other cells and proteins in the body.

The carbohydrates found in the erythrocyte membrane are attached to the outer surface of the membrane and help to identify the cell as part of the body's own immune system. They also play a role in cell-cell recognition and adhesion.

Overall, the erythrocyte membrane is a complex and dynamic structure that plays a critical role in maintaining the function and integrity of red blood cells.

Ion transport refers to the active or passive movement of ions, such as sodium (Na+), potassium (K+), chloride (Cl-), and calcium (Ca2+) ions, across cell membranes. This process is essential for various physiological functions, including nerve impulse transmission, muscle contraction, and maintenance of resting membrane potential.

Ion transport can occur through several mechanisms, including:

1. Diffusion: the passive movement of ions down their concentration gradient, from an area of high concentration to an area of low concentration.
2. Facilitated diffusion: the passive movement of ions through specialized channels or transporters in the cell membrane.
3. Active transport: the energy-dependent movement of ions against their concentration gradient, requiring the use of ATP. This process is often mediated by ion pumps, such as the sodium-potassium pump (Na+/K+-ATPase).
4. Co-transport or symport: the coupled transport of two or more different ions or molecules in the same direction, often driven by an electrochemical gradient.
5. Counter-transport or antiport: the coupled transport of two or more different ions or molecules in opposite directions, also often driven by an electrochemical gradient.

Abnormalities in ion transport can lead to various medical conditions, such as cystic fibrosis (which involves defective chloride channel function), hypertension (which may be related to altered sodium transport), and certain forms of heart disease (which can result from abnormal calcium handling).

The Golgi apparatus, also known as the Golgi complex or simply the Golgi, is a membrane-bound organelle found in the cytoplasm of most eukaryotic cells. It plays a crucial role in the processing, sorting, and packaging of proteins and lipids for transport to their final destinations within the cell or for secretion outside the cell.

The Golgi apparatus consists of a series of flattened, disc-shaped sacs called cisternae, which are stacked together in a parallel arrangement. These stacks are often interconnected by tubular structures called tubules or vesicles. The Golgi apparatus has two main faces: the cis face, which is closest to the endoplasmic reticulum (ER) and receives proteins and lipids directly from the ER; and the trans face, which is responsible for sorting and dispatching these molecules to their final destinations.

The Golgi apparatus performs several essential functions in the cell:

1. Protein processing: After proteins are synthesized in the ER, they are transported to the cis face of the Golgi apparatus, where they undergo various post-translational modifications, such as glycosylation (the addition of sugar molecules) and sulfation. These modifications help determine the protein's final structure, function, and targeting.
2. Lipid modification: The Golgi apparatus also modifies lipids by adding or removing different functional groups, which can influence their properties and localization within the cell.
3. Protein sorting and packaging: Once proteins and lipids have been processed, they are sorted and packaged into vesicles at the trans face of the Golgi apparatus. These vesicles then transport their cargo to various destinations, such as lysosomes, plasma membrane, or extracellular space.
4. Intracellular transport: The Golgi apparatus serves as a central hub for intracellular trafficking, coordinating the movement of vesicles and other transport carriers between different organelles and cellular compartments.
5. Cell-cell communication: Some proteins that are processed and packaged in the Golgi apparatus are destined for secretion, playing crucial roles in cell-cell communication and maintaining tissue homeostasis.

In summary, the Golgi apparatus is a vital organelle involved in various cellular processes, including post-translational modification, sorting, packaging, and intracellular transport of proteins and lipids. Its proper functioning is essential for maintaining cellular homeostasis and overall organismal health.

Cell membrane permeability refers to the ability of various substances, such as molecules and ions, to pass through the cell membrane. The cell membrane, also known as the plasma membrane, is a thin, flexible barrier that surrounds all cells, controlling what enters and leaves the cell. Its primary function is to protect the cell's internal environment and maintain homeostasis.

The permeability of the cell membrane depends on its structure, which consists of a phospholipid bilayer interspersed with proteins. The hydrophilic (water-loving) heads of the phospholipids face outward, while the hydrophobic (water-fearing) tails face inward, creating a barrier that is generally impermeable to large, polar, or charged molecules.

However, specific proteins within the membrane, called channels and transporters, allow certain substances to cross the membrane. Channels are protein structures that span the membrane and provide a pore for ions or small uncharged molecules to pass through. Transporters, on the other hand, are proteins that bind to specific molecules and facilitate their movement across the membrane, often using energy in the form of ATP.

The permeability of the cell membrane can be influenced by various factors, such as temperature, pH, and the presence of certain chemicals or drugs. Changes in permeability can have significant consequences for the cell's function and survival, as they can disrupt ion balances, nutrient uptake, waste removal, and signal transduction.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Artificial membranes are synthetic or man-made materials that possess properties similar to natural biological membranes, such as selective permeability and barrier functions. These membranes can be designed to control the movement of molecules, ions, or cells across them, making them useful in various medical and biotechnological applications.

Examples of artificial membranes include:

1. Dialysis membranes: Used in hemodialysis for patients with renal failure, these semi-permeable membranes filter waste products and excess fluids from the blood while retaining essential proteins and cells.
2. Hemofiltration membranes: Utilized in extracorporeal circuits to remove larger molecules, such as cytokines or inflammatory mediators, from the blood during critical illnesses or sepsis.
3. Drug delivery systems: Artificial membranes can be used to encapsulate drugs, allowing for controlled release and targeted drug delivery in specific tissues or cells.
4. Tissue engineering: Synthetic membranes serve as scaffolds for cell growth and tissue regeneration, guiding the formation of new functional tissues.
5. Biosensors: Artificial membranes can be integrated into biosensing devices to selectively detect and quantify biomolecules, such as proteins or nucleic acids, in diagnostic applications.
6. Microfluidics: Artificial membranes are used in microfluidic systems for lab-on-a-chip applications, enabling the manipulation and analysis of small volumes of fluids for various medical and biological purposes.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

In the context of medicine, plasma refers to the clear, yellowish fluid that is the liquid component of blood. It's composed of water, enzymes, hormones, antibodies, clotting factors, and other proteins. Plasma serves as a transport medium for cells, nutrients, waste products, gases, and other substances throughout the body. Additionally, it plays a crucial role in the immune response and helps regulate various bodily functions.

Plasma can be collected from blood donors and processed into various therapeutic products, such as clotting factors for people with hemophilia or immunoglobulins for patients with immune deficiencies. This process is called plasma fractionation.

Cation transport proteins are a type of membrane protein that facilitate the movement of cations (positively charged ions) across biological membranes. These proteins play a crucial role in maintaining ion balance and electrical excitability within cells, as well as in various physiological processes such as nutrient uptake, waste elimination, and signal transduction.

There are several types of cation transport proteins, including:

1. Ion channels: These are specialized protein structures that form a pore or channel through the membrane, allowing ions to pass through rapidly and selectively. They can be either voltage-gated or ligand-gated, meaning they open in response to changes in electrical potential or binding of specific molecules, respectively.

2. Ion pumps: These are active transport proteins that use energy from ATP hydrolysis to move ions against their electrochemical gradient, effectively pumping them from one side of the membrane to the other. Examples include the sodium-potassium pump (Na+/K+-ATPase) and calcium pumps (Ca2+ ATPase).

3. Ion exchangers: These are antiporter proteins that facilitate the exchange of one ion for another across the membrane, maintaining electroneutrality. For example, the sodium-proton exchanger (NHE) moves a proton into the cell in exchange for a sodium ion being moved out.

4. Symporters: These are cotransporter proteins that move two or more ions together in the same direction, often coupled with the transport of a solute molecule. An example is the sodium-glucose cotransporter (SGLT), which facilitates glucose uptake into cells by coupling its movement with that of sodium ions.

Collectively, cation transport proteins help maintain ion homeostasis and contribute to various cellular functions, including electrical signaling, enzyme regulation, and metabolic processes. Dysfunction in these proteins can lead to a range of diseases, such as neurological disorders, cardiovascular disease, and kidney dysfunction.

Bacterial outer membrane proteins (OMPs) are a type of protein found in the outer membrane of gram-negative bacteria. The outer membrane is a unique characteristic of gram-negative bacteria, and it serves as a barrier that helps protect the bacterium from hostile environments. OMPs play a crucial role in maintaining the structural integrity and selective permeability of the outer membrane. They are involved in various functions such as nutrient uptake, transport, adhesion, and virulence factor secretion.

OMPs are typically composed of beta-barrel structures that span the bacterial outer membrane. These proteins can be classified into several groups based on their size, function, and structure. Some of the well-known OMP families include porins, autotransporters, and two-partner secretion systems.

Porins are the most abundant type of OMPs and form water-filled channels that allow the passive diffusion of small molecules, ions, and nutrients across the outer membrane. Autotransporters are a diverse group of OMPs that play a role in bacterial pathogenesis by secreting virulence factors or acting as adhesins. Two-partner secretion systems involve the cooperation between two proteins to transport effector molecules across the outer membrane.

Understanding the structure and function of bacterial OMPs is essential for developing new antibiotics and therapies that target gram-negative bacteria, which are often resistant to conventional treatments.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

Biological models, also known as physiological models or organismal models, are simplified representations of biological systems, processes, or mechanisms that are used to understand and explain the underlying principles and relationships. These models can be theoretical (conceptual or mathematical) or physical (such as anatomical models, cell cultures, or animal models). They are widely used in biomedical research to study various phenomena, including disease pathophysiology, drug action, and therapeutic interventions.

Examples of biological models include:

1. Mathematical models: These use mathematical equations and formulas to describe complex biological systems or processes, such as population dynamics, metabolic pathways, or gene regulation networks. They can help predict the behavior of these systems under different conditions and test hypotheses about their underlying mechanisms.
2. Cell cultures: These are collections of cells grown in a controlled environment, typically in a laboratory dish or flask. They can be used to study cellular processes, such as signal transduction, gene expression, or metabolism, and to test the effects of drugs or other treatments on these processes.
3. Animal models: These are living organisms, usually vertebrates like mice, rats, or non-human primates, that are used to study various aspects of human biology and disease. They can provide valuable insights into the pathophysiology of diseases, the mechanisms of drug action, and the safety and efficacy of new therapies.
4. Anatomical models: These are physical representations of biological structures or systems, such as plastic models of organs or tissues, that can be used for educational purposes or to plan surgical procedures. They can also serve as a basis for developing more sophisticated models, such as computer simulations or 3D-printed replicas.

Overall, biological models play a crucial role in advancing our understanding of biology and medicine, helping to identify new targets for therapeutic intervention, develop novel drugs and treatments, and improve human health.

Sodium is an essential mineral and electrolyte that is necessary for human health. In a medical context, sodium is often discussed in terms of its concentration in the blood, as measured by serum sodium levels. The normal range for serum sodium is typically between 135 and 145 milliequivalents per liter (mEq/L).

Sodium plays a number of important roles in the body, including:

* Regulating fluid balance: Sodium helps to regulate the amount of water in and around your cells, which is important for maintaining normal blood pressure and preventing dehydration.
* Facilitating nerve impulse transmission: Sodium is involved in the generation and transmission of electrical signals in the nervous system, which is necessary for proper muscle function and coordination.
* Assisting with muscle contraction: Sodium helps to regulate muscle contractions by interacting with other minerals such as calcium and potassium.

Low sodium levels (hyponatremia) can cause symptoms such as confusion, seizures, and coma, while high sodium levels (hypernatremia) can lead to symptoms such as weakness, muscle cramps, and seizures. Both conditions require medical treatment to correct.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Calcium is an essential mineral that is vital for various physiological processes in the human body. The medical definition of calcium is as follows:

Calcium (Ca2+) is a crucial cation and the most abundant mineral in the human body, with approximately 99% of it found in bones and teeth. It plays a vital role in maintaining structural integrity, nerve impulse transmission, muscle contraction, hormonal secretion, blood coagulation, and enzyme activation.

Calcium homeostasis is tightly regulated through the interplay of several hormones, including parathyroid hormone (PTH), calcitonin, and vitamin D. Dietary calcium intake, absorption, and excretion are also critical factors in maintaining optimal calcium levels in the body.

Hypocalcemia refers to low serum calcium levels, while hypercalcemia indicates high serum calcium levels. Both conditions can have detrimental effects on various organ systems and require medical intervention to correct.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

Endocytosis is the process by which cells absorb substances from their external environment by engulfing them in membrane-bound structures, resulting in the formation of intracellular vesicles. This mechanism allows cells to take up large molecules, such as proteins and lipids, as well as small particles, like bacteria and viruses. There are two main types of endocytosis: phagocytosis (cell eating) and pinocytosis (cell drinking). Phagocytosis involves the engulfment of solid particles, while pinocytosis deals with the uptake of fluids and dissolved substances. Other specialized forms of endocytosis include receptor-mediated endocytosis and caveolae-mediated endocytosis, which allow for the specific internalization of molecules through the interaction with cell surface receptors.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Transport vesicles are membrane-bound sacs or containers within cells that are responsible for the intracellular transport of proteins, lipids, and other cargo. These vesicles form when a portion of a donor membrane buds off, enclosing the cargo inside. There are different types of transport vesicles, including:

1. Endoplasmic reticulum (ER) vesicles: These vesicles form from the ER and transport proteins to the Golgi apparatus for further processing.
2. Golgi-derived vesicles: After proteins have been processed in the Golgi, they are packaged into transport vesicles that can deliver them to their final destinations within the cell or to the plasma membrane for secretion.
3. Endocytic vesicles: These vesicles form when a portion of the plasma membrane invaginates and pinches off, engulfing extracellular material or fluid. Examples include clathrin-coated vesicles and caveolae.
4. Lysosomal vesicles: These vesicles transport materials to lysosomes for degradation.
5. Secretory vesicles: These vesicles store proteins and other molecules that will be secreted from the cell. When stimulated, these vesicles fuse with the plasma membrane, releasing their contents to the extracellular space.

Membrane fluidity, in the context of cell biology, refers to the ability of the phospholipid bilayer that makes up the cell membrane to change its structure and organization in response to various factors. The membrane is not a static structure but rather a dynamic one, with its lipids constantly moving and changing position.

Membrane fluidity is determined by the fatty acid composition of the phospholipids that make up the bilayer. Lipids with unsaturated fatty acids have kinks in their hydrocarbon chains, which prevent them from packing closely together and increase membrane fluidity. In contrast, lipids with saturated fatty acids can pack closely together, reducing membrane fluidity.

Membrane fluidity is important for various cellular processes, including the movement of proteins within the membrane, the fusion of vesicles with the membrane during exocytosis and endocytosis, and the ability of the membrane to respond to changes in temperature and other environmental factors. Abnormalities in membrane fluidity have been linked to various diseases, including cancer, neurological disorders, and infectious diseases.

Electron microscopy (EM) is a type of microscopy that uses a beam of electrons to create an image of the sample being examined, resulting in much higher magnification and resolution than light microscopy. There are several types of electron microscopy, including transmission electron microscopy (TEM), scanning electron microscopy (SEM), and reflection electron microscopy (REM).

In TEM, a beam of electrons is transmitted through a thin slice of the sample, and the electrons that pass through the sample are focused to form an image. This technique can provide detailed information about the internal structure of cells, viruses, and other biological specimens, as well as the composition and structure of materials at the atomic level.

In SEM, a beam of electrons is scanned across the surface of the sample, and the electrons that are scattered back from the surface are detected to create an image. This technique can provide information about the topography and composition of surfaces, as well as the structure of materials at the microscopic level.

REM is a variation of SEM in which the beam of electrons is reflected off the surface of the sample, rather than scattered back from it. This technique can provide information about the surface chemistry and composition of materials.

Electron microscopy has a wide range of applications in biology, medicine, and materials science, including the study of cellular structure and function, disease diagnosis, and the development of new materials and technologies.

Anion transport proteins are specialized membrane transport proteins that facilitate the movement of negatively charged ions, known as anions, across biological membranes. These proteins play a crucial role in maintaining ionic balance and regulating various physiological processes within the body.

There are several types of anion transport proteins, including:

1. Cl-/HCO3- exchangers (also known as anion exchangers or band 3 proteins): These transporters facilitate the exchange of chloride (Cl-) and bicarbonate (HCO3-) ions across the membrane. They are widely expressed in various tissues, including the red blood cells, gastrointestinal tract, and kidneys, where they help regulate pH, fluid balance, and electrolyte homeostasis.
2. Sulfate permeases: These transporters facilitate the movement of sulfate ions (SO42-) across membranes. They are primarily found in the epithelial cells of the kidneys, intestines, and choroid plexus, where they play a role in sulfur metabolism and absorption.
3. Cl- channels: These proteins form ion channels that allow chloride ions to pass through the membrane. They are involved in various physiological processes, such as neuronal excitability, transepithelial fluid transport, and cell volume regulation.
4. Cation-chloride cotransporters: These transporters move both cations (positively charged ions) and chloride anions together across the membrane. They are involved in regulating neuronal excitability, cell volume, and ionic balance in various tissues.

Dysfunction of anion transport proteins has been implicated in several diseases, such as cystic fibrosis (due to mutations in the CFTR Cl- channel), distal renal tubular acidosis (due to defects in Cl-/HCO3- exchangers), and some forms of epilepsy (due to abnormalities in cation-chloride cotransporters).

Endosomes are membrane-bound compartments within eukaryotic cells that play a critical role in intracellular trafficking and sorting of various cargoes, including proteins and lipids. They are formed by the invagination of the plasma membrane during endocytosis, resulting in the internalization of extracellular material and cell surface receptors.

Endosomes can be classified into early endosomes, late endosomes, and recycling endosomes based on their morphology, molecular markers, and functional properties. Early endosomes are the initial sorting stations for internalized cargoes, where they undergo sorting and processing before being directed to their final destinations. Late endosomes are more acidic compartments that mature from early endosomes and are responsible for the transport of cargoes to lysosomes for degradation.

Recycling endosomes, on the other hand, are involved in the recycling of internalized cargoes back to the plasma membrane or to other cellular compartments. Endosomal sorting and trafficking are regulated by a complex network of molecular interactions involving various proteins, lipids, and intracellular signaling pathways.

Defects in endosomal function have been implicated in various human diseases, including neurodegenerative disorders, developmental abnormalities, and cancer. Therefore, understanding the mechanisms underlying endosomal trafficking and sorting is of great importance for developing therapeutic strategies to treat these conditions.

Vesicular transport proteins are specialized proteins that play a crucial role in the intracellular trafficking and transportation of various biomolecules, such as proteins and lipids, within eukaryotic cells. These proteins facilitate the formation, movement, and fusion of membrane-bound vesicles, which are small, spherical structures that carry cargo between different cellular compartments or organelles.

There are several types of vesicular transport proteins involved in this process:

1. Coat Proteins (COPs): These proteins form a coat around the vesicle membrane and help shape it into its spherical form during the budding process. They also participate in selecting and sorting cargo for transportation. Two main types of COPs exist: COPI, which is involved in transport between the Golgi apparatus and the endoplasmic reticulum (ER), and COPII, which mediates transport from the ER to the Golgi apparatus.

2. SNARE Proteins: These proteins are responsible for the specific recognition and docking of vesicles with their target membranes. They form complexes that bring the vesicle and target membranes close together, allowing for fusion and the release of cargo into the target organelle. There are two types of SNARE proteins: v-SNAREs (vesicle SNAREs) and t-SNAREs (target SNAREs), which interact to form a stable complex during membrane fusion.

3. Rab GTPases: These proteins act as molecular switches that regulate the recruitment of coat proteins, motor proteins, and SNAREs during vesicle transport. They cycle between an active GTP-bound state and an inactive GDP-bound state, controlling the various stages of vesicular trafficking, such as budding, transport, tethering, and fusion.

4. Tethering Proteins: These proteins help to bridge the gap between vesicles and their target membranes before SNARE-mediated fusion occurs. They play a role in ensuring specificity during vesicle docking and may also contribute to regulating the timing of membrane fusion events.

5. Soluble N-ethylmaleimide-sensitive factor Attachment Protein Receptors (SNAREs): These proteins are involved in intracellular transport, particularly in the trafficking of vesicles between organelles. They consist of a family of coiled-coil domain-containing proteins that form complexes to mediate membrane fusion events.

Overall, these various classes of proteins work together to ensure the specificity and efficiency of vesicular transport in eukaryotic cells. Dysregulation or mutation of these proteins can lead to various diseases, including neurodegenerative disorders and cancer.

Membrane glycoproteins are proteins that contain oligosaccharide chains (glycans) covalently attached to their polypeptide backbone. They are integral components of biological membranes, spanning the lipid bilayer and playing crucial roles in various cellular processes.

The glycosylation of these proteins occurs in the endoplasmic reticulum (ER) and Golgi apparatus during protein folding and trafficking. The attached glycans can vary in structure, length, and composition, which contributes to the diversity of membrane glycoproteins.

Membrane glycoproteins can be classified into two main types based on their orientation within the lipid bilayer:

1. Type I (N-linked): These glycoproteins have a single transmembrane domain and an extracellular N-terminus, where the oligosaccharides are predominantly attached via asparagine residues (Asn-X-Ser/Thr sequon).
2. Type II (C-linked): These glycoproteins possess two transmembrane domains and an intracellular C-terminus, with the oligosaccharides linked to tryptophan residues via a mannose moiety.

Membrane glycoproteins are involved in various cellular functions, such as:

* Cell adhesion and recognition
* Receptor-mediated signal transduction
* Enzymatic catalysis
* Transport of molecules across membranes
* Cell-cell communication
* Immunological responses

Some examples of membrane glycoproteins include cell surface receptors (e.g., growth factor receptors, cytokine receptors), adhesion molecules (e.g., integrins, cadherins), and transporters (e.g., ion channels, ABC transporters).

In the field of medicine, "time factors" refer to the duration of symptoms or time elapsed since the onset of a medical condition, which can have significant implications for diagnosis and treatment. Understanding time factors is crucial in determining the progression of a disease, evaluating the effectiveness of treatments, and making critical decisions regarding patient care.

For example, in stroke management, "time is brain," meaning that rapid intervention within a specific time frame (usually within 4.5 hours) is essential to administering tissue plasminogen activator (tPA), a clot-busting drug that can minimize brain damage and improve patient outcomes. Similarly, in trauma care, the "golden hour" concept emphasizes the importance of providing definitive care within the first 60 minutes after injury to increase survival rates and reduce morbidity.

Time factors also play a role in monitoring the progression of chronic conditions like diabetes or heart disease, where regular follow-ups and assessments help determine appropriate treatment adjustments and prevent complications. In infectious diseases, time factors are crucial for initiating antibiotic therapy and identifying potential outbreaks to control their spread.

Overall, "time factors" encompass the significance of recognizing and acting promptly in various medical scenarios to optimize patient outcomes and provide effective care.

Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.

Fluorescence microscopy is a type of microscopy that uses fluorescent dyes or proteins to highlight and visualize specific components within a sample. In this technique, the sample is illuminated with high-energy light, typically ultraviolet (UV) or blue light, which excites the fluorescent molecules causing them to emit lower-energy, longer-wavelength light, usually visible light in the form of various colors. This emitted light is then collected by the microscope and detected to produce an image.

Fluorescence microscopy has several advantages over traditional brightfield microscopy, including the ability to visualize specific structures or molecules within a complex sample, increased sensitivity, and the potential for quantitative analysis. It is widely used in various fields of biology and medicine, such as cell biology, neuroscience, and pathology, to study the structure, function, and interactions of cells and proteins.

There are several types of fluorescence microscopy techniques, including widefield fluorescence microscopy, confocal microscopy, two-photon microscopy, and total internal reflection fluorescence (TIRF) microscopy, each with its own strengths and limitations. These techniques can provide valuable insights into the behavior of cells and proteins in health and disease.

The endoplasmic reticulum (ER) is a network of interconnected tubules and sacs that are present in the cytoplasm of eukaryotic cells. It is a continuous membranous organelle that plays a crucial role in the synthesis, folding, modification, and transport of proteins and lipids.

The ER has two main types: rough endoplasmic reticulum (RER) and smooth endoplasmic reticulum (SER). RER is covered with ribosomes, which give it a rough appearance, and is responsible for protein synthesis. On the other hand, SER lacks ribosomes and is involved in lipid synthesis, drug detoxification, calcium homeostasis, and steroid hormone production.

In summary, the endoplasmic reticulum is a vital organelle that functions in various cellular processes, including protein and lipid metabolism, calcium regulation, and detoxification.

Potassium is a essential mineral and an important electrolyte that is widely distributed in the human body. The majority of potassium in the body (approximately 98%) is found within cells, with the remaining 2% present in blood serum and other bodily fluids. Potassium plays a crucial role in various physiological processes, including:

1. Regulation of fluid balance and maintenance of normal blood pressure through its effects on vascular tone and sodium excretion.
2. Facilitation of nerve impulse transmission and muscle contraction by participating in the generation and propagation of action potentials.
3. Protein synthesis, enzyme activation, and glycogen metabolism.
4. Regulation of acid-base balance through its role in buffering systems.

The normal serum potassium concentration ranges from 3.5 to 5.0 mEq/L (milliequivalents per liter) or mmol/L (millimoles per liter). Potassium levels outside this range can have significant clinical consequences, with both hypokalemia (low potassium levels) and hyperkalemia (high potassium levels) potentially leading to serious complications such as cardiac arrhythmias, muscle weakness, and respiratory failure.

Potassium is primarily obtained through the diet, with rich sources including fruits (e.g., bananas, oranges, and apricots), vegetables (e.g., leafy greens, potatoes, and tomatoes), legumes, nuts, dairy products, and meat. In cases of deficiency or increased needs, potassium supplements may be recommended under the guidance of a healthcare professional.

... synaptic cleft by simultaneously reversing the direction of transport through the primary plasma membrane transport proteins ... norepinephrine, serotonin, and histamine-from cellular cytosol into synaptic vesicles. In nigrostriatal pathway and mesolimbic ... SLC18A2 is an integral membrane protein that transports monoamines-particularly neurotransmitters such as dopamine, ... The solute carrier family 18 member 2 (SLC18A2) also known as vesicular monoamine transporter 2 (VMAT2) is a protein that in ...
... cascade via protein kinases that results in the phosphorylation of monoamine transporters located at the plasma membrane (i.e ... Serotonin-norepinephrine releasing agent (SNRA) Serotonin-dopamine releasing agent (SDRA) Serotonin-norepinephrine-dopamine ... these transporters transport monoamines in reverse (i.e., they move monoamines from the neuronal cytoplasm into the synaptic ... They may enter the presynaptic neuron primarily via plasma membrane transporters, such as the dopamine transporter (DAT), ...
... s (MATs) are proteins that function as integral plasma-membrane transporters to regulate concentrations of ... and norepinephrine). MATs are located just outside the synaptic cleft (peri-synaptically), transporting monoamine transmitter ... All MATs contain sites for protein kinase phosphorylation by cAMP-dependent protein kinase, protein kinase C (PKC) and Ca2+/ ... The ion concentration gradient generated by the plasma membrane Na+/K+ ATPase provides the driving force for the transporter- ...
The encoded protein contains twelve putative transmembrane domains and is a plasma integral membrane protein. OCT3 is widely ... Known substrates for transport include: histamine, serotonin, norepinephrine, dopamine and MPP+. Capacity for transport and ... 2007). "The organic cation transporters (OCT1, OCT2, EMT) and the plasma membrane monoamine transporter (PMAT) show ... Transport activity of OCT3 is inhibited by recreational and pharmaceutical drugs, including MDMA, phencyclidine (PCP), MK-801, ...
They are found closer to the plasma membrane of the cell. This requires norepinephrine to diffuse from the site it is released ... Membrane proteins, Neurotransmitter transporters, Norepinephrine, Solute carrier family). ... can transport norepinephrine and dopamine. The reuptake of norepinephrine and dopamine is essential in regulating the ... The transport of norepinephrine back into presynaptic cell is made possible by the cotransport with Na+ and Cl−. The sequential ...
This protein is an integral membrane protein that transports the monoamine neurotransmitters (serotonin, dopamine, ... norepinephrine) as well as adenosine, from synaptic spaces into presynaptic neurons or neighboring glial cells. It is ... The plasma membrane monoamine transporter (PMAT) is a low-affinity monoamine transporter protein which in humans is encoded by ... Membrane proteins, Neurotransmitter transporters, Solute carrier family, Molecular neuroscience, All stub articles, Membrane ...
... and cause an internal translocation so that the opening in the protein now faces the other side of the plasma membrane. The ... "A closer look at amphetamine-induced reverse transport and trafficking of the dopamine and norepinephrine transporters". ... A membrane transport protein (or simply transporter) is a membrane protein involved in the movement of ions, small molecules, ... Unlike channel proteins which only transport substances through membranes passively, carrier proteins can transport ions and ...
... norepinephrine plasma membrane transport proteins MeSH D12.776.157.530.562.374.750 - gaba plasma membrane transport proteins ... glycine plasma membrane transport proteins MeSH D12.776.157.530.450.625.186 - norepinephrine plasma membrane transport proteins ... dopamine plasma membrane transport proteins MeSH D12.776.157.530.450.625.139 - gaba plasma membrane transport proteins MeSH ... glycine plasma membrane transport proteins MeSH D12.776.157.530.562.374.875 - serotonin plasma membrane transport proteins MeSH ...
... norepinephrine plasma membrane transport proteins MeSH D12.776.543.585.562.374.750 - gaba plasma membrane transport proteins ... glycine plasma membrane transport proteins MeSH D12.776.543.585.450.625.186 - norepinephrine plasma membrane transport proteins ... dopamine plasma membrane transport proteins MeSH D12.776.543.585.450.625.139 - gaba plasma membrane transport proteins MeSH ... glycine plasma membrane transport proteins MeSH D12.776.543.585.562.374.875 - serotonin plasma membrane transport proteins MeSH ...
SVCT1 and SVCT2 import the reduced form of ascorbate across plasma membranes. GLUT1 and GLUT3 are glucose transporters, and ... Ascorbic acid is absorbed in the body by both active transport and simple diffusion. Sodium-Dependent Active Transport - Sodium ... a multifunctional protein with catalytic, processing, and routing domains". Protein Science. 2 (4): 489-497. doi:10.1002/pro. ... Dopamine beta-hydroxylase participates in the biosynthesis of norepinephrine from dopamine. Peptidylglycine alpha-amidating ...
... through specific transport proteins, such as the SLC27 family fatty acid transport protein. Red blood cells do not contain ... Phospholipids comprise the plasma membrane and other membranes that enclose all the organelles within the cells, such as the ... These lipases are activated by high epinephrine and glucagon levels in the blood (or norepinephrine secreted by sympathetic ... Fatty acids are an integral part of the phospholipids that make up the bulk of the plasma membranes, or cell membranes, of ...
... or transport monoamines out of the neuron; in other words, the reversed membrane transporter will push dopamine, norepinephrine ... Approximately 20% of amphetamine circulating in the bloodstream is bound to plasma proteins. Following absorption, amphetamine ... norepinephrine transporter, or serotonin transporter) to either stop transporting monoamines altogether (via transporter ... Transcription factors are proteins that increase or decrease the expression of specific genes. In simpler terms, this necessary ...
In addition to its effect on the plasma membrane monoamine transporters, methamphetamine inhibits synaptic vesicle function by ... production and either completely inhibits or reverses the transport direction of the dopamine transporter (DAT), norepinephrine ... it triggers transporter phosphorylation via protein kinase A (PKA) and protein kinase C (PKC) signaling, ultimately resulting ... Transcription factors are proteins that increase or decrease the expression of specific genes. In simpler terms, this necessary ...
The ion transport system moves potassium across the cell membrane using two mechanisms. One is active and pumps sodium out of, ... Plasma potassium is normally kept at 3.5 to 5.5 millimoles (mmol) [or milliequivalents (mEq)] per liter by multiple mechanisms ... ISBN 978-0-07-110595-8. Vašák, Milan; Schnabl, Joachim (2016). "Chapter 8. Sodium and Potassium Ions in Proteins and Enzyme ... in cortex regulates norepinephrine levels, network state, and behavioral output". Proceedings of the National Academy of ...
... must enter the presynaptic neuron through a membrane transport protein or be able to diffuse across the presynaptic membrane in ... indicating that trace amine induced LLA does not act on receptors found on the plasma membrane but requires their transport to ... In dopamine, norepinephrine, and serotonin neurons, the primary membrane transporters are DAT, NET, and SERT respectively. ... In model cell systems, hTAAR1 has extremely poor membrane expression. A method to induce hTAAR1 membrane expression has been ...
"Functional interaction between monoamine plasma membrane transporters and the synaptic PDZ domain-containing protein PICK1". ... transport, and degradation. The gene for DAT, known as DAT1, is located on chromosome 5p15. The protein encoding region of the ... In contrast, the human serotonin transporter (hSERT) and human norepinephrine transporter (hNET) do not contain zinc binding ... Apart from these innate protein-protein interactions, recent studies demonstrated that viral proteins such as HIV-1 Tat protein ...
... neurotransmitters can also be released via reverse transport through membrane transport proteins.[citation needed] Autocrine ... For example, epinephrine and norepinephrine can function as hormones when released from the adrenal gland and are transported ... This secretion is possible because the vesicle transiently fuses with the plasma membrane. In the context of neurotransmission ... There are three types: A membrane ligand (protein, oligosaccharide, lipid) and a membrane protein of two adjacent cells ...
Torres GE, Gainetdinov RR, Caron MG (January 2003). "Plasma membrane monoamine transporters: structure, regulation and function ... is separating the high level of plasma homovanillic acid contributed by the metabolism of norepinephrine. Although dopamine is ... These amino acids are found in nearly every protein and so are readily available in food, with tyrosine being the most common. ... After synthesis, dopamine is transported from the cytosol into synaptic vesicles by a solute carrier-a vesicular monoamine ...
Because neurotransmitters are too large and hydrophilic to diffuse through the membrane, specific transport proteins are ... Reuptake is the reabsorption of a neurotransmitter by a neurotransmitter transporter located along the plasma membrane of an ... an inhibitor of norepinephrine reuptake protein, NET). By examining the dose-response curves (using a normal medium as control ... transporter proteins use transmembrane ion gradients and electrical potential to transport neurotransmitter across the membrane ...
... , or transporter reversal, is a phenomenon in which the substrates of a membrane transport protein are moved ... and other monoamine transporters that are located along the plasma membrane of neurons (specifically, DAT, NET, and SERT). ... "A closer look at amphetamine-induced reverse transport and trafficking of the dopamine and norepinephrine transporters". ... Transporter reversal typically occurs when a membrane transport protein is phosphorylated by a particular protein kinase, which ...
Sympathetic nervous system terminals release Norepinephrine onto a Beta-3 adrenergic receptor on the plasma membrane. This ... Kunji, E.R.S.; King, M.S.; Ruprecht, J.J.; Thangaratnarajah, C. (2020). "The SLC25 Carrier Family: Important Transport Proteins ... Both proteins are integral membrane proteins, localized to the inner mitochondrial membrane, and they have a similar pattern of ... The substrate comes in to the half open UCP1 protein from the cytoplasmic side of the membrane, the protein closes the ...
Approximately 20% of amphetamine circulating in the bloodstream is bound to plasma proteins. Following absorption, amphetamine ... since both MAOIs and amphetamine increase plasma catecholamines (i.e., norepinephrine and dopamine); therefore, concurrent use ... Although the monoamine transport cycle has been resolved in considerable detail, kinetic knowledge on the molecular actions of ... Amphetamine can enter the presynaptic neuron either through DAT or by diffusing across the neuronal membrane directly. As a ...
One transport protein or many?". Pharmacology & Therapeutics. 239: 108283. doi:10.1016/j.pharmthera.2022.108283. PMID 36162727 ... Cocaine has a short elimination half life of 0.7-1.5 hours and is extensively metabolized by plasma esterases and also by liver ... The juices are absorbed slowly by the mucous membrane of the inner cheek and by the gastrointestinal tract when swallowed. ... Azizi SA (December 2020). "Monoamines: Dopamine, Norepinephrine, and Serotonin, Beyond Modulation, "Switches" That Alter the ...
Membrane fluidity Membrane lipids Membrane nanotube Membrane potential Membrane protein Membrane topology Membrane transport ... Phosphatidylglycerol Phosphatidylinositol Phosphatidylserine Physics of skiing Pink algae Plasma membrane monoamine transporter ... Nav1.1 Nav1.2 Nav1.4 Nav1.5 Nectin Neurophysins Nicolas Rashevsky Nicotinic acetylcholine receptor Niosome Norepinephrine ... IgSF CAM Inner membrane Inner mitochondrial membrane Insect wing Integral membrane protein Interbilayer forces in membrane ...
The PMAT also suggestively transports dopamine and norepinephrine, albeit at Km values even higher than that of 5-HT (330- ... 63) investigated the role of [] protein kinase[] in the phase change in S. gregaria: ... cAMP-dependent protein kinase A (PKA ... The 5-HT receptors, the receptors for serotonin, are located on the cell membrane of nerve cells and other cell types in ... Hahn P (July 1984). "Effect of litter size on plasma cholesterol and insulin and some liver and adipose tissue enzymes in adult ...
Norepinephrine enters vesicles by V-ATPase[citation needed]. V-ATPases are also found in the plasma membranes of a wide variety ... Transport proteins, Transmembrane proteins). ... Plasma membrane V-ATPases are involved in processes such as pH ... V-ATPases couple the energy of ATP hydrolysis to proton transport across intracellular and plasma membranes of eukaryotic cells ... Emma B, Forest O, Barry B (June 1997). "Mutations of pma-1, the Gene Encoding the Plasma Membrane H+ATPase of Neurospora crassa ...
Its plasma protein binding is approximately 80%. Dibenzepin was first introduced, in Switzerland and West Germany, in 1965. It ... "Initial serotonin transport into viable platelets and imipramine binding to platelet membranes". J Neural Transm (Vienna). 109 ... Dibenzepin acts as a selective norepinephrine reuptake inhibitor (NRI), with similar potency to that of imipramine. It is also ...
In pigs, the protein's half-life is two hours. When the peptide is continuously infused, it leads to diarrhea and ... The membrane potential exerts powerful effects on the lymphocyte activation. The resting potential results primarily from a ... In contrast to when the plasma concentration of margatoxin is higher than 10nM, the transient hyperactivity occurs in pigs. It ... Margatoxin influences nicotinic ACh-receptor agonist-induced norepinephrine release. Upon activation of muscarinic ACh ...
Inositol 1,4,5-trisphosphate (IP3) then binds to receptor proteins in the plasma membrane of the endoplasmic reticulum (ER). ... This protein works as a transcription factor for MafA in an unknown manner and MafA is transported out of the cell. MafA is ... The net effect of norepinephrine from sympathetic nerves and epinephrine from adrenal glands on insulin release is inhibition ... to a G protein-coupled membrane receptor. Phospholipase C cleaves the membrane phospholipid, phosphatidyl inositol 4,5- ...
Atomoxetine is widely distributed and is highly (98%) bound to plasma proteins, mainly albumin. The volume of distribution for ... The NET is located in the plasma membrane of noradrenergic neurons and serves as the fundamental mechanism by terminating the ... "Clinical doses of atomoxetine significantly occupy both norepinephrine and serotonin transports: Implications on treatment of ... Atomoxetine selectively inhibits norepinephrine reuptake by blocking the presynaptic norepinephrine transporter (NET) in the ...
Norepinephrine Plasma Membrane Transport Proteins Medicine & Life Sciences 100% * Tourette Syndrome Medicine & Life Sciences 90 ... Rippel, CA, Kobets, AJ, Yoon, DY, Williams, PN, Shugart, YY, Bridges, DD, Vandenbergh, DJ & Singer, HS 2006, Norepinephrine ... Norepinephrine transporter polymorphisms in Tourette syndrome with and without attention deficit hyperactivity disorder: No ... Norepinephrine transporter polymorphisms in Tourette syndrome with and without attention deficit hyperactivity disorder: No ...
Norepinephrine Plasma Membrane Transport Proteins 12% * Intracellular Membranes 11% * Dopamine Plasma Membrane Transport ...
Norepinephrine Plasma Membrane Transport Proteins 29% * Joints 27% * Efferent Pathways 27% * Neurological Rehabilitation 27% ...
Norepinephrine Plasma Membrane Transport Proteins 22% * Sympathectomy 19% 6 Scopus citations * Large-scale, three-dimensional ... Cadherin-11, Sparc-related modular calcium binding protein-2, and Pigment epithelium-derived factor are promising non-invasive ...
Norepinephrine Plasma Membrane Transport Proteins Medicine & Life Sciences 16% View full fingerprint ... keywords = "depression, dopamine, geriatric psychiatry, membrane transport proteins, norepinephrine, polymorphism receptor, ... Two polymorphisms, rs2242466 (-182T/C) and rs5569 (1287G/A), in the norepinephrine transporter gene (SLC6A2 or NET) have been ... Two polymorphisms, rs2242466 (-182T/C) and rs5569 (1287G/A), in the norepinephrine transporter gene (SLC6A2 or NET) have been ...
Netarsudil: Dual inhibitor of Rho-kinase and the norepinephrine plasma membrane transport protein; increases trabecular outflow ... Netarsudil and active metabolite: Little to no quantifiable plasma concentrations measured during 8 days of daily use ...
... synaptic cleft by simultaneously reversing the direction of transport through the primary plasma membrane transport proteins ... norepinephrine, serotonin, and histamine-from cellular cytosol into synaptic vesicles. In nigrostriatal pathway and mesolimbic ... SLC18A2 is an integral membrane protein that transports monoamines-particularly neurotransmitters such as dopamine, ... The solute carrier family 18 member 2 (SLC18A2) also known as vesicular monoamine transporter 2 (VMAT2) is a protein that in ...
Norepinephrine Plasma Membrane Transport Proteins, Progesterone, Stroke Volume, Sympathetic Nervous System, Vascular Resistance ... Hormonal influences on cardiovascular norepinephrine transporter responses in healthy women. Creators Name:. Moldovanova, I. ... During head-up tilt with norepinephrine transporter inhibition, blood pressure and stroke volume decreased to a greater extent ... The tachycardic response to head-up tilt with norepinephrine transporter inhibition was augmented in the follicular phase. Our ...
D3.633.100.79.80.70.216.500 Norepinephrine Plasma Membrane Transport Proteins D12.776.157.530.937.600 D12.776.543.585.937.700 ... Dopamine Plasma Membrane Transport Proteins D12.776.157.530.937.500 D12.776.543.585.937.500 Doppler Effect G1.595.210 G1.226 ... Serotonin Plasma Membrane Transport Proteins D12.776.157.530.937.624 D12.776.543.585.937.747 Sex Determination Processes G5.355 ... Glutamate Plasma Membrane Transport Proteins D12.776.157.530.937.250.500 D12.776.543.585.937.250.500 Glycochenodeoxycholic Acid ...
D3.633.100.79.80.70.216.500 Norepinephrine Plasma Membrane Transport Proteins D12.776.157.530.937.600 D12.776.543.585.937.700 ... Dopamine Plasma Membrane Transport Proteins D12.776.157.530.937.500 D12.776.543.585.937.500 Doppler Effect G1.595.210 G1.226 ... Serotonin Plasma Membrane Transport Proteins D12.776.157.530.937.624 D12.776.543.585.937.747 Sex Determination Processes G5.355 ... Glutamate Plasma Membrane Transport Proteins D12.776.157.530.937.250.500 D12.776.543.585.937.250.500 Glycochenodeoxycholic Acid ...
D3.633.100.79.80.70.216.500 Norepinephrine Plasma Membrane Transport Proteins D12.776.157.530.937.600 D12.776.543.585.937.700 ... Dopamine Plasma Membrane Transport Proteins D12.776.157.530.937.500 D12.776.543.585.937.500 Doppler Effect G1.595.210 G1.226 ... Serotonin Plasma Membrane Transport Proteins D12.776.157.530.937.624 D12.776.543.585.937.747 Sex Determination Processes G5.355 ... Glutamate Plasma Membrane Transport Proteins D12.776.157.530.937.250.500 D12.776.543.585.937.250.500 Glycochenodeoxycholic Acid ...
D3.633.100.79.80.70.216.500 Norepinephrine Plasma Membrane Transport Proteins D12.776.157.530.937.600 D12.776.543.585.937.700 ... Dopamine Plasma Membrane Transport Proteins D12.776.157.530.937.500 D12.776.543.585.937.500 Doppler Effect G1.595.210 G1.226 ... Serotonin Plasma Membrane Transport Proteins D12.776.157.530.937.624 D12.776.543.585.937.747 Sex Determination Processes G5.355 ... Glutamate Plasma Membrane Transport Proteins D12.776.157.530.937.250.500 D12.776.543.585.937.250.500 Glycochenodeoxycholic Acid ...
D3.633.100.79.80.70.216.500 Norepinephrine Plasma Membrane Transport Proteins D12.776.157.530.937.600 D12.776.543.585.937.700 ... Dopamine Plasma Membrane Transport Proteins D12.776.157.530.937.500 D12.776.543.585.937.500 Doppler Effect G1.595.210 G1.226 ... Serotonin Plasma Membrane Transport Proteins D12.776.157.530.937.624 D12.776.543.585.937.747 Sex Determination Processes G5.355 ... Glutamate Plasma Membrane Transport Proteins D12.776.157.530.937.250.500 D12.776.543.585.937.250.500 Glycochenodeoxycholic Acid ...
metabolism Humans Male Middle Aged Norepinephrine Plasma Membrane Transport Proteins/antagonists & inhibitors Occipital Lobe/ ...
Norepinephrine Plasma Membrane Transport Proteins. *Organic Anion Transport Protein 1. *Organic Cation Transport Proteins ... "Organic Anion Transport Protein 1" by people in this website by year, and whether "Organic Anion Transport Protein 1" was a ... Dopamine Plasma Membrane Transport Proteins. *Equilibrative Nucleoside Transport Proteins. *Glucose Transport Proteins, ... "Organic Anion Transport Protein 1" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH ...
Cyclic S-Oxides *Thiadiazoles Norepinephrine Plasma Membrane Transport Proteins/antagonists & inhibitors. J Med Chem. 2011 Oct ... Sulfonamides *Thiadiazoles Proto-Oncogene Proteins c-akt/antagonists & inhibitors. Mol Cancer Ther 2010 Mar;9(3):706-17 1,3,4- ... Cyclic S-Oxides *Thiadiazoles Amyloid Precursor Protein Secretases/antagonists & inhibitors. Chem Biol 2007 Feb;14(2):209-19 ... Thiadiazoles *Cyclooctanes Amyloid Precursor Protein Secretases/antagonists & inhibitors. J Med Chem 2009 Jun 11;52(11):3441-4 ...
Glycine Plasma Membrane Transport Proteins [D12.776.157.530.450.625.155] * Norepinephrine Plasma Membrane Transport Proteins [ ... Glycine Plasma Membrane Transport Proteins [D12.776.543.585.450.625.155] * Norepinephrine Plasma Membrane Transport Proteins [ ... Dopamine Plasma Membrane Transport Proteins [D12.776.157.530.450.625.124] * GABA Plasma Membrane Transport Proteins [D12.776. ... Dopamine Plasma Membrane Transport Proteins [D12.776.543.585.450.625.124] * GABA Plasma Membrane Transport Proteins [D12.776. ...
Carcinoma de células escamosas de cabeça e pescoço; Estresse Psicológico; Norepinephrine Plasma Membrane Transport Proteins; ...
Norepinephrine Plasma Membrane Transport Proteins * Community-Institutional Relations Explore _. Similar People (60) ... Identifying pharmacodynamic protein markers of centrally active drugs in humans: a pilot study in a novel clinical model. J ... Multiple-dose plasma pharmacokinetic and safety study of LY450108 and LY451395 (AMPA receptor potentiators) and their ... Dihydroxyphenylglycol as a Biomarker of Norepinephrine Transporter Inhibition by Atomoxetine: Human Model to Assess Central and ...
Norepinephrine Plasma Membrane Transport Proteins [D12.776.157.530.937.600] * Organic Anion Transport Protein 1 [D12.776. ... Norepinephrine Plasma Membrane Transport Proteins [D12.776.543.585.937.700] * Organic Cation Transport Proteins [D12.776. ... Proteins [D12.776] * Membrane Proteins [D12.776.543] * Membrane Transport Proteins [D12.776.543.585] * Solute Carrier Proteins ... Amino Acids, Peptides, and Proteins [D12] * Proteins [D12.776] * Membrane Proteins [D12.776.543] * Membrane Transport Proteins ...
Norepinephrine Plasma Membrane Transport Proteins, Norepinephrine/metabolism, Rats, Regression Analysis, Serotonin Plasma ... Tags: *Membrane Glycoproteins, *Membrane Transport Proteins, *Nerve Tissue Proteins, 1998, Animals, Boja J W, Carrier Proteins ... Tags: *Membrane Transport Proteins, *Nerve Tissue Proteins, *Symporters, 1998, Animals, Binding, Binding Sites, Boja J W, ... Dopamine Plasma Membrane Transport Proteins, Dopamine/metabolism, Estradiol/*pharmacology, European journal of pharmacology, ...
Membrane Transport Proteins/*genetics/metabolism, Messenger/*metabolism, Mice, Molecular Sequence Data, Norepinephrine Plasma ... Molecular brain research, Delayed-Action Preparations, Dluzen Dean E, Dopamine Plasma Membrane Transport Proteins, Drug ... Membrane Transport Proteins, Olfactory Bulb/*drug effects/enzymology/*physiology, Ovariectomy, Park June-Hee, Rats, RNA, ... Tags: *Membrane Glycoproteins, *Nerve Tissue Proteins, 2002, Animals, Brain research. ...
Norepinephrine Plasma Membrane Transport Proteins. *Organic Anion Transport Protein 1. *Organic Cation Transport Proteins ... "Glucose Transport Proteins, Facilitative" by people in this website by year, and whether "Glucose Transport Proteins, ... A family of monosaccharide transport proteins characterized by 12 membrane spanning helices. They facilitate passive diffusion ... Dopamine Plasma Membrane Transport Proteins. *Equilibrative Nucleoside Transport Proteins. *Glucose Transport Proteins, ...
Glutamate Plasma Membrane Transport Proteins. *Glycine Plasma Membrane Transport Proteins. *Norepinephrine Plasma Membrane ... Serotonin Plasma Membrane Transport Proteins*Serotonin Plasma Membrane Transport Proteins. *Serotonin Plasma Membrane ... Plasma Membrane Neurotransmitter Transport Proteins [D12.776.157.530.562.374]. *Serotonin Plasma Membrane Transport Proteins [ ... Plasma Membrane Neurotransmitter Transport Proteins [D12.776.543.585.562.374]. *Serotonin Plasma Membrane Transport Proteins [ ...
Glutamate Plasma Membrane Transport Proteins. *Glycine Plasma Membrane Transport Proteins. *Norepinephrine Plasma Membrane ... Plasma Membrane Neurotransmitter Transport Proteins [D12.776.157.530.562.374]. *Glycine Plasma Membrane Transport Proteins [ ... Plasma Membrane Neurotransmitter Transport Proteins [D12.776.543.585.562.374]. *Glycine Plasma Membrane Transport Proteins [ ... Glycine Plasma Membrane Transport Proteins*Glycine Plasma Membrane Transport Proteins. *Neurotransmitter Transporters, Glycine- ...
involved_in protein localization to plasma membrane ISS Inferred from Sequence or Structural Similarity. more info ... Ion_trans; Ion transport protein. pfam03521. Location:467 → 679. Kv2channel; Kv2 voltage-gated K+ channel. ... involved_in positive regulation of norepinephrine secretion ISS Inferred from Sequence or Structural Similarity. more info ... Ion_trans; Ion transport protein. pfam03521. Location:467 → 679. Kv2channel; Kv2 voltage-gated K+ channel. ...
Norepinephrine Plasma Membrane Transport Proteins. *Organic Anion Transport Protein 1. *Organic Cation Transport Proteins ... Dopamine Plasma Membrane Transport Proteins. *Equilibrative Nucleoside Transport Proteins. *Glucose Transport Proteins, ... Amino Acid Transport System y+L*Amino Acid Transport System y+L ... Amino Acid Transport System y+. *Amino Acid Transport System y+ ... "Amino Acid Transport System y+L" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH ( ...
Norepinephrine Plasma Membrane Transport Proteins [D12.776.157.530.937.600] * Organic Anion Transport Protein 1 [D12.776. ... Norepinephrine Plasma Membrane Transport Proteins [D12.776.543.585.937.700] * Organic Cation Transport Proteins [D12.776. ... Proteins [D12.776] * Membrane Proteins [D12.776.543] * Membrane Transport Proteins [D12.776.543.585] * Solute Carrier Proteins ... Amino Acids, Peptides, and Proteins [D12] * Proteins [D12.776] * Membrane Proteins [D12.776.543] * Membrane Transport Proteins ...
multidrug resistance protein. NET. norepinephrine transporter. OCT. organic cation transporter. PMAT. plasma membrane monoamine ... 2010) Adenosine transport by plasma membrane monoamine transporter: reinvestigation and comparison with organic cations. Drug ... 2007) Metformin transport by a newly cloned proton-stimulated organic cation transporter (plasma membrane monoamine transporter ... 2010) Selective transport of monoamine neurotransmitters by human plasma membrane monoamine transporter and organic cation ...
GO:0016323 C:basolateral plasma membrane GO:0005887 C:integral to plasma membrane ... 8] "Comparison of type I and type II organic cation transport by organic cation transporters and organic anion-transporting ... Basolateral cell membrane1 / Multi-pass membrane protein2 Substrate. amino acid, polyamine Cross database links:. ... GO:0005333 F:norepinephrine transmembrane transporter activity GO:0015101 F:organic cation transmembrane transporter activity ...
  • Epinephrine, Norepinephrine, and Phenylephrine select α1 receptors agonistically. (proprofs.com)
  • In a fasting state, increased glucagon and epinephrine and norepinephrine secretion induce autophagy, and glucocorticoids have also been shown to induce autophagy by stimulating the transcription of autophagy genes such as ATG5, LC3, and Beclin-1 in various tissues 8 . (nature.com)
  • As such, dopamine is the simplest possible catecholamine , a family that also includes the neurotransmitters norepinephrine and epinephrine. (alchetron.com)
  • Transporters on the plasma membrane of tumor cells are promising molecular "Trojan horses" to deliver drugs and imaging agents into cancer cells. (aspetjournals.org)
  • Norepinephrine transporter, organic cation transporters, and multidrug and toxin extrusion proteins play differential roles in tumor targeting, systemic elimination, and accumulation in normal tissues. (aspetjournals.org)
  • 8] "Comparison of 'type I' and 'type II' organic cation transport by organic cation transporters and organic anion-transporting polypeptides. (tcdb.org)
  • Venous estradiol and progesterone concentrations were higher in the luteal than in the follicular phase but did not differ between placebo and norepinephrine transporter inhibition testing days. (mdc-berlin.de)
  • In the supine position, norepinephrine transporter inhibition increased blood pressure and stroke volume to a greater extent during the follicular than during the luteal phase. (mdc-berlin.de)
  • Conversely, the increase in heart rate and cardiac output with norepinephrine transporter inhibition was augmented in the luteal compared with the follicular phase. (mdc-berlin.de)
  • The tachycardic response to head-up tilt with norepinephrine transporter inhibition was augmented in the follicular phase. (mdc-berlin.de)
  • Our study suggests that sex hormones alter the hemodynamic response to norepinephrine transporter inhibition in women. (mdc-berlin.de)
  • Dihydroxyphenylglycol as a Biomarker of Norepinephrine Transporter Inhibition by Atomoxetine: Human Model to Assess Central and Peripheral Effects of Dosing. (sc-ctsi.org)
  • Although many substituted amphetamines induce the release of neurotransmitters from vesicles through SLC18A2 while inhibiting uptake through SLC18A2, they may facilitate the release of monoamine neurotransmitters into the synaptic cleft by simultaneously reversing the direction of transport through the primary plasma membrane transport proteins for monoamines (i.e., the dopamine transporter, norepinephrine transporter, and serotonin transporter) in monoamine neurons. (wikipedia.org)
  • SLC18A2 is an integral membrane protein that transports monoamines-particularly neurotransmitters such as dopamine, norepinephrine, serotonin, and histamine-from cellular cytosol into synaptic vesicles. (wikipedia.org)
  • Two polymorphisms, rs2242466 (-182T/C) and rs5569 (1287G/A), in the norepinephrine transporter gene (SLC6A2 or NET) have been associated with antidepressant response. (elsevierpure.com)
  • Gender differences in human cardiovascular norepinephrine transporter function may be mediated through female sex hormones. (mdc-berlin.de)
  • The phenomenon may be explained by an effect of female sex hormones on norepinephrine transporter function, on compensatory cardiovascular responses, or both. (mdc-berlin.de)
  • In relation to phospholipids, they represent the main structural element of cell membranes, while cholesterol is a precursor of hormones and a constituent of bile. (lupinepublishers.com)
  • 11) Why is it that steroid hormones use receptors inside of target cells, whereas protein, peptide, and amino acid hormones do not? (easynotecards.com)
  • 17) Membrane receptors are used by which of the following types of hormones? (easynotecards.com)
  • The blood carries the hormones to target cells that contain specific receptor proteins for the hormones, and which therefore can respond in a specific fashion to them. (50webs.org)
  • The rs6280 variant (Ser9Gly) of the dopamine receptor 3 (DRD3) gene may influence the binding affinity of D3 receptors as a result of serine to glycine substitution of the receptor protein. (elsevierpure.com)
  • However, evidence is now accumulating for rapid corticosteroid actions 25 , 26 , and the existence of membrane-bound steroid receptors that may mediate these rapid actions 27 , 28 . (ersjournals.com)
  • By binding to α2 receptors in the CNS, clonidine can modulate the release of norepinephrine, resulting in a decrease in sympathetic outflow and ultimately leading to a decrease in heart rate. (proprofs.com)
  • At their best, they usually rely on some mysterious things called ionic pumps, that perform active transport, powered by little motors, under instructions from molecules that act on their specific receptors. (raypeat.com)
  • Two types of estrogen receptor exist: ER, which is a member of the nuclear hormone family of intracellular receptors, and the estrogen G protein-coupled receptor GPR30 , which is a G protein-coupled. (absoluteastronomy.com)
  • G protein-coupled receptors , also known as seven-transmembrane domain receptors, 7TM receptors, heptahelical receptors, serpentine receptor, and G protein-linked receptors , comprise a large protein family of transmembrane receptors that sense molecules outside the cell and activate inside signal. (absoluteastronomy.com)
  • The solute carrier family 18 member 2 (SLC18A2) also known as vesicular monoamine transporter 2 (VMAT2) is a protein that in humans is encoded by the SLC18A2 gene. (wikipedia.org)
  • Jacobs, Russell E. Year: 2006 DOI: 10.1016/j.neuroimage.2005.08.037 PMCID: PMC3376084 Shiverer is an important model of central nervous system dysmyelination characterized by a deletion in the gene encoding myelin basic protein with relevance to human dysmyelinating and demyelinating diseases. (caltech.edu)
  • Finally, using a kinesin light chain 1 knockout mouse, we find that conventional kinesin is a participant but not essential to neuronal transport of Mn^(2+) in the optic tract. (caltech.edu)
  • C) interfere with norepinephrine at a neuronal synapse. (easynotecards.com)
  • Sodium-iodide symporters (NIS) actively transport iodide ions from the bloodstream into thyroid follicular cells against a sodium electrochemical gradient, which is maintained by the sodium-potassium pump (Na+/K+-ATPase). (myendoconsult.com)
  • Iodide ions are then transported to the apical membrane of the thyroid follicular cells by the action of pendrin, an anion exchanger protein. (myendoconsult.com)
  • At the apical membrane of the thyroid follicular cell, the thyroid peroxidase (TPO) enzyme, in the presence of hydrogen peroxide (H2O2), catalyzes the oxidation of iodide to form reactive iodine species[7]. (myendoconsult.com)
  • A subclass of symporters that specifically transport SODIUM CHLORIDE and/or POTASSIUM CHLORIDE across cellular membranes in a tightly coupled process. (nih.gov)
  • Sodium chloride-dependent neurotransmitter symporters located primarily on the PLASMA MEMBRANE of serotonergic neurons. (musc.edu)
  • A family of sodium chloride-dependent neurotransmitter symporters that transport the amino acid GLYCINE. (childrensmercy.org)
  • 2. Polypeptides and proteins. (50webs.org)
  • Proteins are large polypeptides, so the distinction between the two categories is somewhat arbitrary. (50webs.org)
  • This movement of ions can be called active transport, without invoking the mysterious machinery of membrane pumps. (raypeat.com)
  • The cell membrane is selectively permeable to ions and organic molecules and controls the movement of substances in and out of cells. (absoluteastronomy.com)
  • In particular, human organic cation transporter 2 (hOCT2) and multidrug and toxin extrusion proteins 1 and 2-K (hMATE1/2-K) likely mediate renal secretion of mIBG, whereas hOCT1 and hOCT3 may contribute to mIBG uptake into normal tissues such as the liver, salivary glands, and heart. (aspetjournals.org)
  • A) Steroids can cross the cell membrane because they are lipids and the membrane is lipid. (easynotecards.com)
  • 17] "Novel single nucleotide polymorphisms of organic cation transporter 1 (SLC22A1) affecting transport functions. (tcdb.org)
  • Organic Anion Transport Protein 1" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (ucdenver.edu)
  • This graph shows the total number of publications written about "Organic Anion Transport Protein 1" by people in this website by year, and whether "Organic Anion Transport Protein 1" was a major or minor topic of these publications. (ucdenver.edu)
  • Below are the most recent publications written about "Organic Anion Transport Protein 1" by people in Profiles. (ucdenver.edu)
  • It is capable of transporting a variety organic anions and mediates sodium-independent uptake of bile in the liver. (nih.gov)
  • Below are the most recent publications written about "Serotonin Plasma Membrane Transport Proteins" by people in Profiles. (musc.edu)
  • Below are the most recent publications written about "Amino Acid Transport System y+L" by people in Profiles. (musc.edu)
  • This results in an elevated intra-follicular iodide concentration compared to the plasma. (myendoconsult.com)
  • Drosophila transmembrane protein 214 (dTMEM214) regulates midgut glucose uptake and systemic glucose homeostasis. (ouhsc.edu)
  • Here we use the power of mouse genetics and the simplicity of the visual system to test rigorously the parameters affecting Mn^(2+) uptake, transport and trans-synaptic tracing. (caltech.edu)
  • higher doses may cause severe mucous membrane irritation, burning, and lacrimation, and lower respiratory effects such as bronchitis, pulmonary edema, or pneumonia. (cdc.gov)
  • In line with the pulmonary toxicity findings, in vitro cytotoxicity and membrane damage in macrophages were observed only at the higher doses. (cdc.gov)
  • 3) ________ are chemical messengers that are released by cells and transported in the bloodstream to alter the activities of specific cells in other tissues. (easynotecards.com)
  • Amino acids in TMS1 confer major functional differences between human and mouse orthologs of the polyspecific membrane transporter, OCT1. (tcdb.org)
  • In the interaction with proteins, lead binds with virtually every available functional group, including sulfhydryl, amine, phosphate, and carboxyl groups, with sulfhydryl having the highest affinity. (cdc.gov)
  • These products are often proteins, but in non-protein coding genes such as ribosomal RNA , transfer RNA or small nuclear RNA genes, the product is a functional RNA. (absoluteastronomy.com)
  • Living beings depend on genes, as they specify all proteins and functional RNA chains. (absoluteastronomy.com)
  • A leucine-sensitive amino acid transport system with high affinity for basic amino acids( AMINO ACIDS, BASIC). (musc.edu)
  • Antidiuretic hormone is a polypeptide with eight amino acids, too small to accurately be called a protein. (50webs.org)
  • No research has been done for the determination of plasma levels of tryptophan metabolites in patients of monopolar and bipolar depression. (scirp.org)
  • In patients of major monopolar depression age and gender differences of plasma levels of tryptophan metabolites disappear although significant differences are observed in healthy volunteers. (scirp.org)
  • We analyzed plasma levels of patients of major monopolar depression and preliminarily reported that plasma levels of 5-HT, but not 5-HIAA, were lower in depressive patients [6]. (scirp.org)
  • However, since there are significant gender and age differences in plasma levels of TRP metabolites in healthy volunteers, we decided to analyze differences of TRP metabolites in patients of major monopolar depression and bipolar depression. (scirp.org)
  • Initially, lead is distributed to the blood plasma and soft tissues, but under steady state conditions 99% of the lead in blood is found in the erythrocyte, where much of it is bound to hemoglobin. (cdc.gov)
  • Most thyroxine is bound to carrier proteins, such as thyroxine-binding globulin (TBG), transthyretin, and albumin in circulation, with only a tiny fraction (approximately 0.03%) present as free thyroxine (FT4)[3]. (myendoconsult.com)
  • T3 circulates bound to carrier proteins (mainly TBG and albumin), with a small fraction (approximately 0.3%) existing as free triiodothyronine (FT3). (myendoconsult.com)
  • A class of nucleotide translocases found abundantly in mitochondria that function as integral components of the inner mitochondrial membrane. (nih.gov)
  • B) the opening of calcium ion channels in the membrane. (easynotecards.com)
  • These mechanisms include the ability of lead to inhibit or mimic the action of calcium and to interact with proteins. (cdc.gov)
  • Protein deficiency is an important cause of deranged calcium metabolism. (raypeat.com)
  • They facilitate passive diffusion of GLUCOSE across the CELL MEMBRANE. (ouhsc.edu)
  • In addition, a number of chemicals-norepinephrine, for example-are secreted both as a neurotransmitter and a hormone. (50webs.org)
  • mIBG enters cancer cells through the norepinephrine transporter (NET) where the radioactive decay of 131 I causes DNA damage, cell death, and tumor necrosis. (aspetjournals.org)
  • E) block the production of a cell membrane. (easynotecards.com)
  • Autophagy is generally considered as a cell survival/protection mechanism because it removes toxic or obsolete proteins and organelles and recycles the degradation products for use as sources for energy and metabolites in anabolic pathways 3 . (nature.com)
  • The cell membrane or plasma membrane is a biological membrane that separates the interior of all cells from the outside environment. (absoluteastronomy.com)
  • Glycine Plasma Membrane Transport Proteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (childrensmercy.org)
  • Anfinsen CB (1973) Principles that govern the folding of protein chains. (springer.com)
  • Lead also binds to metallothionein, a sulfhydryl-rich protein, but does not appear to displace cadmium or zinc. (cdc.gov)
  • Each follicle is composed of a rim of simple cuboidal epithelial cells encircling a mass of colloidal storage protein named thyroglobulin. (myendoconsult.com)
  • Plasma factors were measured after plasma was separated from blood (3000 rpm/min. (scirp.org)