Calcium calmodulin dependent protein kinase type 4. Medical search

A multifunctional calcium-calmodulin-dependent protein kinase subtype that occurs as an oligomeric protein comprised of twelve subunits. It differs from other enzyme subtypes in that it lacks a phosphorylatable activation domain that can respond to CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE KINASE.

A CALMODULIN-dependent enzyme that catalyzes the phosphorylation of proteins. This enzyme is also sometimes dependent on CALCIUM. A wide range of proteins can act as acceptor, including VIMENTIN; SYNAPSINS; GLYCOGEN SYNTHASE; MYOSIN LIGHT CHAINS; and the MICROTUBULE-ASSOCIATED PROTEINS. (From Enzyme Nomenclature, 1992, p277)

A heat-stable, low-molecular-weight activator protein found mainly in the brain and heart. The binding of calcium ions to this protein allows this protein to bind to cyclic nucleotide phosphodiesterases and to adenyl cyclase with subsequent activation. Thereby this protein modulates cyclic AMP and cyclic GMP levels.

A cyclic GMP-dependent protein kinase subtype that is expressed in SMOOTH MUSCLE tissues and plays a role in regulation of smooth muscle contraction. Two isoforms, PKGIalpha and PKGIbeta, of the type I protein kinase exist due to alternative splicing of its mRNA.

A cyclic GMP-dependent protein kinase subtype that is expressed predominantly in INTESTINES, BRAIN, and KIDNEY. The protein is myristoylated on its N-terminus which may play a role its membrane localization.

A monomeric calcium-calmodulin-dependent protein kinase subtype that is primarily expressed in neuronal tissues; T-LYMPHOCYTES and TESTIS. The activity of this enzyme is regulated by its phosphorylation by CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE KINASE.

A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.

The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.

A group of cyclic GMP-dependent enzymes that catalyze the phosphorylation of SERINE or THREONINE residues of proteins.

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.

A cyclic AMP-dependent protein kinase subtype primarily found in particulate subcellular fractions. They are tetrameric proteins that contain two catalytic subunits and two type II-specific regulatory subunits.

An serine-threonine protein kinase that requires the presence of physiological concentrations of CALCIUM and membrane PHOSPHOLIPIDS. The additional presence of DIACYLGLYCEROLS markedly increases its sensitivity to both calcium and phospholipids. The sensitivity of the enzyme can also be increased by PHORBOL ESTERS and it is believed that protein kinase C is the receptor protein of tumor-promoting phorbol esters.

A group of enzymes that are dependent on CYCLIC AMP and catalyze the phosphorylation of SERINE or THREONINE residues on proteins. Included under this category are two cyclic-AMP-dependent protein kinase subtypes, each of which is defined by its subunit composition.

A monomeric calcium-calmodulin-dependent protein kinase subtype that is expressed in a broad variety of mammalian cell types. Its expression is regulated by the action of CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE KINASE. Several isoforms of this enzyme subtype are encoded by distinct genes.

Toluenes in which one hydrogen of the methyl group is substituted by an amino group. Permitted are any substituents on the benzene ring or the amino group.

Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.

An adenine nucleotide containing one phosphate group which is esterified to both the 3'- and 5'-positions of the sugar moiety. It is a second messenger and a key intracellular regulator, functioning as a mediator of activity for a number of hormones, including epinephrine, glucagon, and ACTH.

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.

Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.

Signal transduction mechanisms whereby calcium mobilization (from outside the cell or from intracellular storage pools) to the cytoplasm is triggered by external stimuli. Calcium signals are often seen to propagate as waves, oscillations, spikes, sparks, or puffs. The calcium acts as an intracellular messenger by activating calcium-responsive proteins.

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 type I cAMP-dependent protein kinase regulatory subunit that plays a role in confering CYCLIC AMP activation of protein kinase activity. It has a lower affinity for cAMP than the CYCLIC-AMP-DEPENDENT PROTEIN KINASE RIBETA SUBUNIT.

The rate dynamics in chemical or physical systems.

The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.

Agents that inhibit PROTEIN KINASES.

A cyclic AMP-dependent protein kinase subtype primarily found in the CYTOPLASM. They are tetrameric proteins that contain two catalytic subunits and two type I-specific regulatory subunits.

Guanosine cyclic 3',5'-(hydrogen phosphate). A guanine nucleotide containing one phosphate group which is esterified to the sugar moiety in both the 3'- and 5'-positions. It is a cellular regulatory agent and has been described as a second messenger. Its levels increase in response to a variety of hormones, including acetylcholine, insulin, and oxytocin and it has been found to activate specific protein kinases. (From Merck Index, 11th ed)

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.

A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.

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.

Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.

Established cell cultures that have the potential to propagate indefinitely.

A mitosporic Ophiostomataceae fungal genus, whose species Sporothrix schenckii is a well-known animal pathogen. The conidia of this soil fungus may be inhaled causing a primary lung infection, or may infect independently via skin punctures.

Proteins which bind calmodulin. They are found in many tissues and have a variety of functions including F-actin cross-linking properties, inhibition of cyclic nucleotide phosphodiesterase and calcium and magnesium ATPases.

A group of enzymes that transfers a phosphate group onto an alcohol group acceptor. EC 2.7.1.

The parts of a macromolecule that directly participate in its specific combination with another molecule.

A superfamily of PROTEIN-SERINE-THREONINE KINASES that are activated by diverse stimuli via protein kinase cascades. They are the final components of the cascades, activated by phosphorylation by MITOGEN-ACTIVATED PROTEIN KINASE KINASES, which in turn are activated by mitogen-activated protein kinase kinase kinases (MAP KINASE KINASE KINASES).

A species of ciliate protozoa. It is used in biomedical research.

A group of compounds that contain the structure SO2NH2.

Proteins to which calcium ions are bound. They can act as transport proteins, regulator proteins, or activator proteins. They typically contain EF HAND MOTIFS.

A specific protein kinase C inhibitor, which inhibits superoxide release from human neutrophils (PMN) stimulated with phorbol myristate acetate or synthetic diacylglycerol.

A phenothiazine with actions similar to CHLORPROMAZINE. It is used as an antipsychotic and an antiemetic.

An intracellular signaling system involving the MAP kinase cascades (three-membered protein kinase cascades). Various upstream activators, which act in response to extracellular stimuli, trigger the cascades by activating the first member of a cascade, MAP KINASE KINASE KINASES; (MAPKKKs). Activated MAPKKKs phosphorylate MITOGEN-ACTIVATED PROTEIN KINASE KINASES which in turn phosphorylate the MITOGEN-ACTIVATED PROTEIN KINASES; (MAPKs). The MAPKs then act on various downstream targets to affect gene expression. In mammals, there are several distinct MAP kinase pathways including the ERK (extracellular signal-regulated kinase) pathway, the SAPK/JNK (stress-activated protein kinase/c-jun kinase) pathway, and the p38 kinase pathway. There is some sharing of components among the pathways depending on which stimulus originates activation of the cascade.

Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.

An enzyme that phosphorylates myosin light chains in the presence of ATP to yield myosin-light chain phosphate and ADP, and requires calcium and CALMODULIN. The 20-kDa light chain is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors. The enzyme plays a central role in the regulation of smooth muscle contraction.

Phosphotransferases that catalyzes the conversion of 1-phosphatidylinositol to 1-phosphatidylinositol 3-phosphate. Many members of this enzyme class are involved in RECEPTOR MEDIATED SIGNAL TRANSDUCTION and regulation of vesicular transport with the cell. Phosphatidylinositol 3-Kinases have been classified both according to their substrate specificity and their mode of action within the cell.

A mitogen-activated protein kinase subfamily that regulates a variety of cellular processes including CELL GROWTH PROCESSES; CELL DIFFERENTIATION; APOPTOSIS; and cellular responses to INFLAMMATION. The P38 MAP kinases are regulated by CYTOKINE RECEPTORS and can be activated in response to bacterial pathogens.

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

A dsRNA-activated cAMP-independent protein serine/threonine kinase that is induced by interferon. In the presence of dsRNA and ATP, the kinase autophosphorylates on several serine and threonine residues. The phosphorylated enzyme catalyzes the phosphorylation of the alpha subunit of EUKARYOTIC INITIATION FACTOR-2, leading to the inhibition of protein synthesis.

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.

A phorbol ester found in CROTON OIL with very effective tumor promoting activity. It stimulates the synthesis of both DNA and RNA.

A cytoplasmic serine threonine kinase involved in regulating CELL DIFFERENTIATION and CELLULAR PROLIFERATION. Overexpression of this enzyme has been shown to promote PHOSPHORYLATION of BCL-2 PROTO-ONCOGENE PROTEINS and chemoresistance in human acute leukemia cells.

A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

ATP:pyruvate 2-O-phosphotransferase. A phosphotransferase that catalyzes reversibly the phosphorylation of pyruvate to phosphoenolpyruvate in the presence of ATP. It has four isozymes (L, R, M1, and M2). Deficiency of the enzyme results in hemolytic anemia. EC 2.7.1.40.

A proline-directed serine/threonine protein kinase which mediates signal transduction from the cell surface to the nucleus. Activation of the enzyme by phosphorylation leads to its translocation into the nucleus where it acts upon specific transcription factors. p40 MAPK and p41 MAPK are isoforms.

Voltage-dependent cell membrane glycoproteins selectively permeable to calcium ions. They are categorized as L-, T-, N-, P-, Q-, and R-types based on the activation and inactivation kinetics, ion specificity, and sensitivity to drugs and toxins. The L- and T-types are present throughout the cardiovascular and central nervous systems and the N-, P-, Q-, & R-types are located in neuronal tissue.

A family of calcium/calmodulin-dependent PROETIN-SERINE-THREONINE KINASES. They are ubiquitously expressed in adult and embryonic mammalian tissues, and their functions are tightly related to the early stages of eukaryotic programmed cell death.

Specific enzyme subunits that form the active sites of the type I and type II cyclic-AMP protein kinases. Each molecule of enzyme contains two catalytic subunits.

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.

The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.

A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.

Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.

The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.

The body of a fungus which is made up of HYPHAE.

A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992)

A serine-threonine protein kinase family whose members are components in protein kinase cascades activated by diverse stimuli. These MAPK kinases phosphorylate MITOGEN-ACTIVATED PROTEIN KINASES and are themselves phosphorylated by MAP KINASE KINASE KINASES. JNK kinases (also known as SAPK kinases) are a subfamily.

A 44-kDa extracellular signal-regulated MAP kinase that may play a role the initiation and regulation of MEIOSIS; MITOSIS; and postmitotic functions in differentiated cells. It phosphorylates a number of TRANSCRIPTION FACTORS; and MICROTUBULE-ASSOCIATED PROTEINS.

Proteins prepared by recombinant DNA technology.

A ubiquitously expressed protein kinase that is involved in a variety of cellular SIGNAL PATHWAYS. Its activity is regulated by a variety of signaling protein tyrosine kinase.

A group of compounds with the heterocyclic ring structure of benzo(c)pyridine. The ring structure is characteristic of the group of opium alkaloids such as papaverine. (From Stedman, 25th ed)

An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.

A subgroup of mitogen-activated protein kinases that activate TRANSCRIPTION FACTOR AP-1 via the phosphorylation of C-JUN PROTEINS. They are components of intracellular signaling pathways that regulate CELL PROLIFERATION; APOPTOSIS; and CELL DIFFERENTIATION.

N-(N-(N(2)-(N-(N-(N-(N-D-Alanyl L-seryl)-L-threonyl)-L-threonyl) L-threonyl)-L-asparaginyl)-L-tyrosyl) L-threonine. Octapeptide sharing sequence homology with HIV envelope protein gp120. It is potentially useful as antiviral agent in AIDS therapy. The core pentapeptide sequence, TTNYT, consisting of amino acids 4-8 in peptide T, is the HIV envelope sequence required for attachment to the CD4 receptor.

A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from GLYCINE or THREONINE. It is involved in the biosynthesis of PURINES; PYRIMIDINES; and other amino acids.

Phosphoproteins are proteins that have been modified by the attachment of a phosphate group, which can regulate their activity and function in various cellular processes.

Cyclic nucleotides are a class of molecules that contain a cyclic phosphate group and a nitrogenous base, and play important roles in cellular signaling pathways.

A chelating agent relatively more specific for calcium and less toxic than EDETIC ACID.

The sum of the weight of all the atoms in a molecule.

Intracellular signaling protein kinases that play a signaling role in the regulation of cellular energy metabolism. Their activity largely depends upon the concentration of cellular AMP which is increased under conditions of low energy or metabolic stress. AMP-activated protein kinases modify enzymes involved in LIPID METABOLISM, which in turn provide substrates needed to convert AMP into ATP.

RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.

The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.

The basic cellular units of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the NERVOUS SYSTEM.

An aspect of protein kinase (EC 2.7.1.37) in which serine residues in protamines and histones are phosphorylated in the presence of ATP.

Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.

Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.

The relationship between the dose of an administered drug and the response of the organism to the drug.

Calcium compounds used as food supplements or in food to supply the body with calcium. Dietary calcium is needed during growth for bone development and for maintenance of skeletal integrity later in life to prevent osteoporosis.

A PROTEIN-TYROSINE KINASE family that was originally identified by homology to the Rous sarcoma virus ONCOGENE PROTEIN PP60(V-SRC). They interact with a variety of cell-surface receptors and participate in intracellular signal transduction pathways. Oncogenic forms of src-family kinases can occur through altered regulation or expression of the endogenous protein and by virally encoded src (v-src) genes.

A curved elevation of GRAY MATTER extending the entire length of the floor of the TEMPORAL HORN of the LATERAL VENTRICLE (see also TEMPORAL LOBE). The hippocampus proper, subiculum, and DENTATE GYRUS constitute the hippocampal formation. Sometimes authors include the ENTORHINAL CORTEX in the hippocampal formation.

A protein kinase C subtype that was originally characterized as a CALCIUM-independent, serine-threonine kinase that is activated by PHORBOL ESTERS and DIACYLGLYCEROLS. It is targeted to specific cellular compartments in response to extracellular signals that activate G-PROTEIN-COUPLED RECEPTORS; TYROSINE KINASE RECEPTORS; and intracellular protein tyrosine kinase.

Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.

PKC beta encodes two proteins (PKCB1 and PKCBII) generated by alternative splicing of C-terminal exons. It is widely distributed with wide-ranging roles in processes such as B-cell receptor regulation, oxidative stress-induced apoptosis, androgen receptor-dependent transcriptional regulation, insulin signaling, and endothelial cell proliferation.

Protein kinases that catalyze the PHOSPHORYLATION of TYROSINE residues in proteins with ATP or other nucleotides as phosphate donors.

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.

Elements of limited time intervals, contributing to particular results or situations.

An enzyme that catalyzes the conversion of phosphatidylinositol (PHOSPHATIDYLINOSITOLS) to phosphatidylinositol 4-phosphate, the first committed step in the biosynthesis of phosphatidylinositol 4,5-bisphosphate.

Differential effects of a calcineurin inhibitor on glutamate-induced phosphorylation of Ca2+/calmodulin-dependent protein kinases in cultured rat hippocampal neurons. (1/181)

Calcium/calmodulin-dependent protein kinases (CaM kinases) are major multifunctional enzymes that play important roles in calcium-mediated signal transduction. To characterize their regulatory mechanisms in neurons, we compared glutamate-induced phosphorylation of CaM kinase IV and CaM kinase II in cultured rat hippocampal neurons. We observed that dephosphorylation of these kinases followed different time courses, suggesting different regulatory mechanisms for each kinase. Okadaic acid, an inhibitor of protein phosphatase (PP) 1 and PP2A, increased the phosphorylation of both kinases. In contrast, cyclosporin A, an inhibitor of calcineurin, showed different effects: the phosphorylation and activity of CaM kinase IV were significantly increased with this inhibitor, but those of CaM kinase II were not significantly increased. Cyclosporin A treatment of neurons increased phosphorylation of Thr196 of CaM kinase IV, the activated form with CaM kinase kinase, which was recognized with an anti-phospho-Thr196 antibody. Moreover, recombinant CaM kinase IV was dephosphorylated and inactivated with calcineurin as well as with PP1, PP2A, and PP2C in vitro. These results suggest that CaM kinase IV, but not CaM kinase II, is directly regulated with calcineurin. (+info)

Inhibition of the Ca2+/calmodulin-dependent protein kinase I cascade by cAMP-dependent protein kinase. (2/181)

Several recent studies have shown that Ca2+/calmodulin-dependent protein kinase I (CaMKI) is phosphorylated and activated by a protein kinase (CaMKK) that is itself subject to regulation by Ca2+/calmodulin. In the present study, we demonstrate that this enzyme cascade is regulated by cAMP-mediated activation of cAMP-dependent protein kinase (PKA). In vitro, CaMKK is phosphorylated by PKA and this is associated with inhibition of enzyme activity. The major site of phosphorylation is threonine 108, although additional sites are phosphorylated with lower efficiency. In vitro, CaMKK is also phosphorylated by CaMKI at the same sites as PKA, suggesting that this regulatory phosphorylation might play a role as a negative-feedback mechanism. In intact PC12 cells, activation of PKA with forskolin resulted in a rapid inhibition of both CaMKK and CaMKI activity. In hippocampal slices CaMKK was phosphorylated under basal conditions, and activation of PKA led to an increase in phosphorylation. Two-dimensional phosphopeptide mapping indicated that activation of PKA led to increased phosphorylation of multiple sites including threonine 108. These results indicate that in vitro and in intact cells the CaMKK/CaMKI cascade is subject to inhibition by PKA-mediated phosphorylation of CaMKK. The phosphorylation and inhibition of CaMKK by PKA is likely to be involved in modulating the balance between cAMP- and Ca2+-dependent signal transduction pathways. (+info)

Substrate recognition by Ca2+/Calmodulin-dependent protein kinase kinase. Role of the arg-pro-rich insert domain. (3/181)

Mammalian Ca2+/CaM-dependent protein kinase kinase (CaM-KK) has been identified and cloned as an activator for two kinases, CaM kinase I (CaM-KI) and CaM kinase IV (CaM-KIV), and a recent report (Yano, S., Tokumitsu, H., and Soderling, T. R. (1998) Nature 396, 584-587) demonstrates that CaM-KK can also activate and phosphorylate protein kinase B (PKB). In this study, we identify a CaM-KK from Caenorhabditis elegans, and comparison of its sequence with the mammalian CaM-KK alpha and beta shows a unique Arg-Pro (RP)-rich insert in their catalytic domains relative to other protein kinases. Deletion of the RP-domain resulted in complete loss of CaM-KIV activation activity and physical interaction of CaM-KK with glutathione S-transferase-CaM-KIV (T196A). However, CaM-KK autophosphorylation and phosphorylation of a synthetic peptide substrate were normal in the RP-domain mutant. Site-directed mutagenesis of three conserved Arg in the RP- domain of CaM-KK confirmed that these positive charges are important for CaM-KIV activation. The RP- domain deletion mutant also failed to fully activate and phosphorylate CaM-KI, but this mutant was indistinguishable from wild-type CaM-KK for the phosphorylation and activation of PKB. These results indicate that the RP-domain in CaM-KK is critical for recognition of downstream CaM-kinases but not for its catalytic activity (i.e. autophosphorylation) and PKB activation. (+info)

The retinoblastoma susceptibility gene product/Sp1 signalling pathway is modulated by Ca2+/calmodulin kinases II and IV activity. (4/181)

To investigate the possible link between Ca2+ signalling and cell cycle control we analysed Ca2+/calmodulin kinases (CamK) interaction with the retinoblastoma susceptibility gene product/SP1 pathway. CamK II and IV activate c-fos transcription through a short promoter region (-99 to -53) containing the retinoblastoma control element (RCE) and a cAMP response element (CRE) related sequences. Deletion analysis revealed that the RCE is a major CamK responsive element and is sufficient to confer CamK and Ca2+ regulation to a minimal promoter. Direct interactions between SP1 and RCE were confirmed by gel shift experiments. Using transient transfection experiments, we show that CamK-dependent transcription is regulated by the retinoblastoma (Rb) susceptibility gene product and the p107 Rb related protein. However, the stimulatory effects of CamKs and Rb on c-fos are blocked by overexpression of both proteins. These effects appear to be directly mediated by SP1 as shown by the use of a Gal4/SP1 fusion proteins. In conclusion, CamK II and IV, two major Ca2+-dependent intracellular effectors, may represent a molecular link between this second messenger transduction pathway and effectors that control cell cycle progression through Rb/SP1 signalling pathway. (+info)

A late phase of cerebellar long-term depression requires activation of CaMKIV and CREB. (5/181)

Recently, it has been shown that cerebellar LTD has a late phase that may be blocked by protein synthesis inhibitors. To understand the mechanisms underlying the late phase, we interfered with the activation of transcription factors that might couple synaptic activation to protein synthesis. Particle-mediated transfection of cultured Purkinje neurons with an expression vector encoding a dominant inhibitory form of CREB resulted in a nearly complete blockade of the late phase. Kinases that activate CREB were inhibited, and LTD was assessed. Inhibition of PKA or the MAPK/RSK cascades were without effect on the late phase, while constructs designed to interfere with CaMKIV function attenuated the late phase. These results indicate that the activation of CaMKIV and CREB are necessary to establish a late phase of cerebellar LTD. (+info)

Ca(2+)-dependent gene expression mediated by MEF2 transcription factors. (6/181)

Ca(2+) induction of a subset of cellular and viral immediate-early activation genes in lymphocytes has been previously mapped to response elements recognized by the MEF2 family of transcription factors. Here, we demonstrate that Ca(2+) activation of MEF2 response elements in T lymphocytes is mediated in synergy by two Ca(2+)/calmodulin-dependent enzymes, the phosphatase calcineurin, and the kinase type IV/Gr (CaMKIV/Gr), which promote transcription by the MEF2 family members MEF2A and MEF2D. Calcineurin up-regulates the activity of both factors by an NFAT-dependent mechanism, while CaMKIV/Gr selectively and independently activates MEF2D. These results identify MEF2 proteins as effectors of a pathway of gene induction in T lymphocytes which integrates diverse Ca(2+) activation signals and may be broadly operative in several tissues. (+info)

Activation of orphan receptor-mediated transcription by Ca(2+)/calmodulin-dependent protein kinase IV. (7/181)

Retinoid-related receptor alpha (RORalpha) is an orphan nuclear receptor that constitutively activates transcription from its cognate response element. We show that RORalpha is Ca(2+ )responsive, and a Ca(2+)/calmodulin-independent form of Ca(2+)/calmodulin-dependent protein kinase IV (CaMKIV) potentiates RORalpha-dependent transcription 20- to 30-fold. Other orphan receptors including RORalpha2, RORgamma and COUP-TFI are also potentiated by CaMKIV. Transcriptional activation by CaMKIV is orphan receptor selective and does not occur with either the thyroid hormone or estrogen receptor. CaMKIV does not phosphorylate RORalpha or its ligand-binding domain (LBD) in vitro, although the LBD is essential for transactivation. Therefore, the RORalpha LBD was used in the mammalian two-hybrid assay to identify a single class of small peptide molecules containing LXXLL motifs that interacted with greater affinity in the presence of CaMKIV. This class of peptides antagonized activation of orphan receptor-mediated transcription by CaMKIV. These studies demonstrate a pivotal role for CaMKIV in the regulation of orphan receptor-mediated transcription. (+info)

Ca(2+)/calmodulin-dependent protein kinase IV is expressed in spermatids and targeted to chromatin and the nuclear matrix. (8/181)

Ca(2+)/calmodulin-dependent protein kinase IV and calspermin are two proteins encoded by the Camk4 gene. Both are highly expressed in the testis, where in situ hybridization studies in rat testes have demonstrated that CaMKIV mRNA is localized to pachytene spermatocytes, while calspermin mRNA is restricted to spermatids. We have examined the expression patterns of both CaMKIV and calspermin in mouse testis and unexpectedly find that CaMKIV is expressed in spermatogonia and spermatids but excluded from spermatocytes, while calspermin is found only in spermatids. CaMKIV and calspermin expression in the testis are stage-dependent and appear to be coordinately regulated. In germ cells, we find that CaMKIV is associated with the chromatin. We further demonstrate that a fraction of CaMKIV in spermatids is hyperphosphorylated and specifically localized to the nuclear matrix. These novel findings may implicate CaMKIV in chromatin remodeling during nuclear condensation of spermatids. (+info)

Calcium-calmodulin-dependent protein kinase type 2 (CaMKII) is a family of enzymes that play a critical role in regulating various cellular processes, including muscle contraction, neurotransmitter release, and gene expression. These enzymes are activated by the binding of calcium ions and calmodulin, a calcium-binding protein, to their regulatory domain. Once activated, CaMKII can phosphorylate a wide range of target proteins, including ion channels, receptors, and transcription factors, leading to changes in cellular behavior. Dysregulation of CaMKII activity has been implicated in a variety of diseases, including heart disease, neurodegenerative disorders, and cancer.

Calcium-calmodulin-dependent protein kinases (CaMKs) are a family of enzymes that play a crucial role in regulating various cellular processes in response to changes in intracellular calcium levels. These enzymes are activated by the binding of calcium ions to a regulatory protein called calmodulin, which then binds to and activates the CaMK. CaMKs are involved in a wide range of cellular functions, including muscle contraction, neurotransmitter release, gene expression, and cell division. They are also involved in the regulation of various diseases, including heart disease, neurological disorders, and cancer. In the medical field, CaMKs are the target of several drugs, including those used to treat heart disease and neurological disorders. For example, calcium channel blockers, which are used to treat high blood pressure and chest pain, can also block the activity of CaMKs. Similarly, drugs that target CaMKs are being developed as potential treatments for neurological disorders such as Alzheimer's disease and Parkinson's disease.

Calmodulin is a small, calcium-binding protein that plays a crucial role in regulating various cellular processes in the body. It is found in all eukaryotic cells and is involved in a wide range of physiological functions, including muscle contraction, neurotransmitter release, and gene expression. Calmodulin is a tetramer, meaning that it is composed of four identical subunits, each of which contains two EF-hand calcium-binding domains. When calcium ions bind to these domains, the structure of calmodulin changes, allowing it to interact with and regulate the activity of various target proteins. In the medical field, calmodulin is often studied in the context of various diseases and disorders, including cardiovascular disease, cancer, and neurological disorders. For example, abnormal levels of calmodulin have been associated with the development of certain types of cancer, and calmodulin inhibitors have been investigated as potential therapeutic agents for treating these diseases. Additionally, calmodulin has been implicated in the pathogenesis of various neurological disorders, including Alzheimer's disease and Parkinson's disease.

Cyclic GMP-Dependent Protein Kinase Type I (PKG-I) is an enzyme that plays a crucial role in various physiological processes in the body, including smooth muscle contraction, neurotransmission, and blood pressure regulation. It is activated by the second messenger molecule cyclic guanosine monophosphate (cGMP), which is produced in response to various stimuli such as nitric oxide (NO) and other hormones. PKG-I is a serine/threonine kinase that phosphorylates specific target proteins, leading to changes in their activity or localization. In smooth muscle cells, PKG-I phosphorylates myosin light chain kinase (MLCK), which in turn phosphorylates and activates myosin light chain (MLC), leading to smooth muscle contraction. In neurons, PKG-I phosphorylates various ion channels and transporters, modulating their activity and contributing to neurotransmission. Dysregulation of PKG-I activity has been implicated in various diseases, including hypertension, heart failure, and erectile dysfunction. Therefore, PKG-I is an important target for the development of new therapeutic agents for these conditions.

Cyclic GMP-Dependent Protein Kinase Type II (PKG II) is a type of protein kinase that plays a crucial role in various cellular processes, including smooth muscle contraction, neurotransmission, and gene expression. It is activated by the second messenger molecule cyclic guanosine monophosphate (cGMP) and phosphorylates specific target proteins, leading to changes in their activity or localization. In the cardiovascular system, PKG II is involved in the regulation of blood vessel tone and blood pressure. It can cause smooth muscle relaxation by phosphorylating myosin light chain kinase, leading to a decrease in intracellular calcium levels and smooth muscle contraction. PKG II is also involved in the regulation of neurotransmitter release in the central nervous system and has been implicated in the pathophysiology of various neurological disorders, including Alzheimer's disease and Parkinson's disease. Overall, PKG II is a key regulator of cellular signaling pathways and plays an important role in maintaining normal physiological function in various tissues and organs.

Calcium-calmodulin-dependent protein kinase type 4 (CaMK4) is a protein kinase enzyme that plays a role in various cellular processes, including cell growth, differentiation, and gene expression. It is activated by the binding of calcium ions and the calcium-binding protein calmodulin, which together form a complex that can phosphorylate other proteins. CaMK4 is involved in a number of physiological processes, including learning and memory, muscle contraction, and the regulation of the cell cycle. It has also been implicated in a number of diseases, including cancer, neurodegenerative disorders, and cardiovascular disease.

Protein kinases are enzymes that catalyze the transfer of a phosphate group from ATP (adenosine triphosphate) to specific amino acid residues on proteins. This process, known as phosphorylation, can alter the activity, localization, or stability of the target protein, and is a key mechanism for regulating many cellular processes, including cell growth, differentiation, metabolism, and signaling pathways. Protein kinases are classified into different families based on their sequence, structure, and substrate specificity. Some of the major families of protein kinases include serine/threonine kinases, tyrosine kinases, and dual-specificity kinases. Each family has its own unique functions and roles in cellular signaling. In the medical field, protein kinases are important targets for the development of drugs for the treatment of various diseases, including cancer, diabetes, and cardiovascular disease. Many cancer drugs target specific protein kinases that are overactive in cancer cells, while drugs for diabetes and cardiovascular disease often target kinases involved in glucose metabolism and blood vessel function, respectively.

Cyclic GMP-dependent protein kinases (PKG) are a family of enzymes that play a crucial role in regulating various cellular processes, including smooth muscle contraction, neurotransmitter release, and gene expression. These enzymes are activated by the second messenger molecule cyclic guanosine monophosphate (cGMP), which is produced in response to various stimuli such as nitric oxide (NO) and other signaling molecules. PKG is a serine/threonine kinase that phosphorylates target proteins on specific amino acid residues, leading to changes in their activity or localization. The activity of PKG is tightly regulated by its subcellular localization, substrate availability, and the concentration of cGMP. In the medical field, PKG is of great interest due to its role in various diseases, including cardiovascular disease, hypertension, and erectile dysfunction. PKG inhibitors have been developed as potential therapeutic agents for these conditions, and ongoing research is exploring the potential of PKG activators as novel treatments for various diseases.

Calcium is a chemical element with the symbol Ca and atomic number 20. It is a vital mineral for the human body and is essential for many bodily functions, including bone health, muscle function, nerve transmission, and blood clotting. In the medical field, calcium is often used to diagnose and treat conditions related to calcium deficiency or excess. For example, low levels of calcium in the blood (hypocalcemia) can cause muscle cramps, numbness, and tingling, while high levels (hypercalcemia) can lead to kidney stones, bone loss, and other complications. Calcium supplements are often prescribed to people who are at risk of developing calcium deficiency, such as older adults, vegetarians, and people with certain medical conditions. However, it is important to note that excessive calcium intake can also be harmful, and it is important to follow recommended dosages and consult with a healthcare provider before taking any supplements.

Cyclic AMP-dependent protein kinase type II (PKA II) is a type of protein kinase enzyme that plays a crucial role in regulating various cellular processes in the body. It is activated by the presence of cyclic AMP (cAMP), a second messenger molecule that is produced in response to various stimuli, such as hormones and neurotransmitters. PKA II is a heterotetrameric enzyme composed of two regulatory subunits and two catalytic subunits. The regulatory subunits bind to cAMP and prevent the catalytic subunits from phosphorylating their target proteins. When cAMP levels rise, the regulatory subunits are phosphorylated, which releases the catalytic subunits and allows them to phosphorylate their target proteins. PKA II is involved in a wide range of cellular processes, including gene expression, metabolism, and cell division. It plays a particularly important role in the regulation of the nervous system, where it is involved in the transmission of signals between neurons and the modulation of synaptic plasticity. Dysregulation of PKA II activity has been implicated in a number of diseases, including neurological disorders such as Alzheimer's disease and Parkinson's disease, as well as metabolic disorders such as diabetes and obesity.

Protein kinase C (PKC) is a family of enzymes that play a crucial role in various cellular processes, including cell growth, differentiation, and apoptosis. In the medical field, PKC is often studied in relation to its involvement in various diseases, including cancer, cardiovascular disease, and neurodegenerative disorders. PKC enzymes are activated by the binding of diacylglycerol (DAG) and calcium ions, which leads to the phosphorylation of target proteins. This phosphorylation can alter the activity, localization, or stability of the target proteins, leading to changes in cellular signaling pathways. PKC enzymes are divided into several subfamilies based on their structure and activation mechanisms. The different subfamilies have distinct roles in cellular signaling and are involved in different diseases. For example, some PKC subfamilies are associated with cancer progression, while others are involved in the regulation of the immune system. Overall, PKC enzymes are an important area of research in the medical field, as they have the potential to be targeted for the development of new therapeutic strategies for various diseases.

Cyclic AMP-dependent protein kinases (also known as cAMP-dependent protein kinases or PKA) are a family of enzymes that play a crucial role in regulating various cellular processes in the body. These enzymes are activated by the presence of cyclic AMP (cAMP), a second messenger molecule that is produced in response to various stimuli, such as hormones, neurotransmitters, and growth factors. PKA is a heterotetrameric enzyme composed of two regulatory subunits and two catalytic subunits. The regulatory subunits bind to cAMP and prevent the catalytic subunits from phosphorylating their target proteins. When cAMP levels rise, the regulatory subunits are activated and release the catalytic subunits, allowing them to phosphorylate their target proteins. PKA is involved in a wide range of cellular processes, including metabolism, gene expression, cell proliferation, and differentiation. It phosphorylates various proteins, including enzymes, transcription factors, and ion channels, leading to changes in their activity and function. In the medical field, PKA plays a critical role in various diseases and disorders, including cancer, diabetes, and cardiovascular disease. For example, PKA is involved in the regulation of insulin secretion in pancreatic beta cells, and its dysfunction has been implicated in the development of type 2 diabetes. PKA is also involved in the regulation of blood pressure and heart function, and its dysfunction has been linked to the development of hypertension and heart disease.

Calcium-calmodulin-dependent protein kinase type 1 (CaMKI) is a type of protein kinase that plays a crucial role in regulating various cellular processes, including cell growth, differentiation, and apoptosis. It is activated by the binding of calcium ions and calmodulin, a calcium-binding protein, to its regulatory domain. CaMKI is involved in a wide range of physiological processes, including muscle contraction, neurotransmitter release, and gene expression. It has also been implicated in the development of various diseases, including cancer, cardiovascular disease, and neurodegenerative disorders. In the medical field, CaMKI is a potential target for the development of new drugs to treat these diseases. For example, drugs that inhibit CaMKI activity have been shown to have anti-cancer effects in preclinical studies. Additionally, CaMKI has been proposed as a biomarker for the diagnosis and prognosis of certain diseases, such as Alzheimer's disease.

Benzylamines are a class of organic compounds that contain a benzene ring and an amine group (-NH2) attached to a carbon atom in the ring. They are commonly used in the pharmaceutical industry as intermediates in the synthesis of various drugs, including antidepressants, anesthetics, and antihistamines. Some benzylamines have also been studied for their potential therapeutic effects, such as their ability to reduce inflammation and pain. In the medical field, benzylamines are typically used as research tools or as starting materials for the synthesis of more complex drugs.

Cyclic AMP (cAMP) is a signaling molecule that plays a crucial role in many cellular processes, including metabolism, gene expression, and cell proliferation. It is synthesized from adenosine triphosphate (ATP) by the enzyme adenylyl cyclase, and its levels are regulated by various hormones and neurotransmitters. In the medical field, cAMP is often studied in the context of its role in regulating cellular signaling pathways. For example, cAMP is involved in the regulation of the immune system, where it helps to activate immune cells and promote inflammation. It is also involved in the regulation of the cardiovascular system, where it helps to regulate heart rate and blood pressure. In addition, cAMP is often used as a tool in research to study cellular signaling pathways. For example, it is commonly used to activate or inhibit specific signaling pathways in cells, allowing researchers to study the effects of these pathways on cellular function.

In the medical field, isoenzymes refer to different forms of enzymes that have the same chemical structure and catalytic activity, but differ in their amino acid sequence. These differences can arise due to genetic variations or post-translational modifications, such as phosphorylation or glycosylation. Isoenzymes are often used in medical diagnosis and treatment because they can provide information about the function and health of specific organs or tissues. For example, the presence of certain isoenzymes in the blood can indicate liver or kidney disease, while changes in the levels of specific isoenzymes in the brain can be indicative of neurological disorders. In addition, isoenzymes can be used as biomarkers for certain diseases or conditions, and can be targeted for therapeutic intervention. For example, drugs that inhibit specific isoenzymes can be used to treat certain types of cancer or heart disease.

Calcium signaling is a complex process that involves the movement of calcium ions (Ca2+) within and between cells. Calcium ions play a crucial role in many cellular functions, including muscle contraction, neurotransmitter release, gene expression, and cell division. Calcium signaling is regulated by a network of proteins that sense changes in calcium levels and respond by activating or inhibiting specific cellular processes. In the medical field, calcium signaling is important for understanding the mechanisms underlying many diseases, including cardiovascular disease, neurodegenerative disorders, and cancer. Calcium signaling is also a target for many drugs, including those used to treat hypertension, arrhythmias, and osteoporosis. Understanding the complex interactions between calcium ions and the proteins that regulate them is therefore an important area of research in medicine.

In the medical field, an amino acid sequence refers to the linear order of amino acids in a protein molecule. Proteins are made up of chains of amino acids, and the specific sequence of these amino acids determines the protein's structure and function. The amino acid sequence is determined by the genetic code, which is a set of rules that specifies how the sequence of nucleotides in DNA is translated into the sequence of amino acids in a protein. Each amino acid is represented by a three-letter code, and the sequence of these codes is the amino acid sequence of the protein. The amino acid sequence is important because it determines the protein's three-dimensional structure, which in turn determines its function. Small changes in the amino acid sequence can have significant effects on the protein's structure and function, and this can lead to diseases or disorders. For example, mutations in the amino acid sequence of a protein involved in blood clotting can lead to bleeding disorders.

Cyclic AMP-dependent protein kinase (PKA) RIalpha subunit is a regulatory subunit of the PKA enzyme, which is involved in the regulation of various cellular processes, including metabolism, gene expression, and cell proliferation. The PKA enzyme is a heterotetramer composed of two regulatory subunits (RIalpha or RIIalpha) and two catalytic subunits (Calpha or Cbeta). The regulatory subunits bind to and inhibit the catalytic subunits in the absence of the second messenger cyclic AMP (cAMP). When cAMP levels increase, the regulatory subunits are phosphorylated by cAMP-dependent protein kinase A (PKA), which leads to the release of the catalytic subunits and activation of the enzyme. The RIalpha subunit is expressed in a variety of tissues, including the brain, heart, and muscle, and is involved in the regulation of various physiological processes, including muscle contraction, glucose metabolism, and gene expression.

Cyclic AMP-dependent protein kinase type I (PKA-I) is a type of enzyme that plays a crucial role in regulating various cellular processes in the body. It is activated by the presence of cyclic AMP (cAMP), a second messenger molecule that is produced in response to various stimuli, such as hormones and neurotransmitters. PKA-I is a heterotetrameric enzyme composed of two regulatory subunits and two catalytic subunits. The regulatory subunits bind to cAMP and prevent the catalytic subunits from phosphorylating their target proteins. When cAMP levels rise, the regulatory subunits are phosphorylated by other kinases, which releases the catalytic subunits and allows them to phosphorylate their target proteins. PKA-I is involved in a wide range of cellular processes, including metabolism, gene expression, and cell proliferation. It phosphorylates various proteins, including enzymes, transcription factors, and ion channels, to regulate their activity and function. Dysregulation of PKA-I activity has been implicated in various diseases, including cancer, diabetes, and neurological disorders.

Cyclic GMP (cGMP) is a signaling molecule that plays a crucial role in regulating various physiological processes in the body, including smooth muscle contraction, neurotransmission, and blood pressure regulation. It is synthesized from guanosine triphosphate (GTP) by the enzyme guanylate cyclase and is degraded by the enzyme phosphodiesterase. In the medical field, cGMP is often studied in the context of its role in the regulation of blood vessels and the cardiovascular system. For example, cGMP is involved in the dilation of blood vessels, which helps to lower blood pressure and improve blood flow. It is also involved in the regulation of heart rate and contractility. Abnormal levels of cGMP can lead to a variety of medical conditions, including hypertension, heart failure, and erectile dysfunction. In these cases, medications that either increase or decrease cGMP levels may be used to treat the underlying condition.

In the medical field, "Cells, Cultured" refers to cells that have been grown and maintained in a controlled environment outside of their natural biological context, typically in a laboratory setting. This process is known as cell culture and involves the isolation of cells from a tissue or organism, followed by their growth and proliferation in a nutrient-rich medium. Cultured cells can be derived from a variety of sources, including human or animal tissues, and can be used for a wide range of applications in medicine and research. For example, cultured cells can be used to study the behavior and function of specific cell types, to develop new drugs and therapies, and to test the safety and efficacy of medical products. Cultured cells can be grown in various types of containers, such as flasks or Petri dishes, and can be maintained at different temperatures and humidity levels to optimize their growth and survival. The medium used to culture cells typically contains a combination of nutrients, growth factors, and other substances that support cell growth and proliferation. Overall, the use of cultured cells has revolutionized medical research and has led to many important discoveries and advancements in the field of medicine.

Protein-Serine-Threonine Kinases (PSTKs) are a family of enzymes that play a crucial role in regulating various cellular processes, including cell growth, differentiation, metabolism, and apoptosis. These enzymes phosphorylate specific amino acids, such as serine and threonine, on target proteins, thereby altering their activity, stability, or localization within the cell. PSTKs are involved in a wide range of diseases, including cancer, diabetes, cardiovascular disease, and neurodegenerative disorders. Therefore, understanding the function and regulation of PSTKs is important for developing new therapeutic strategies for these diseases.

In the medical field, a cell line refers to a group of cells that have been derived from a single parent cell and have the ability to divide and grow indefinitely in culture. These cells are typically grown in a laboratory setting and are used for research purposes, such as studying the effects of drugs or investigating the underlying mechanisms of diseases. Cell lines are often derived from cancerous cells, as these cells tend to divide and grow more rapidly than normal cells. However, they can also be derived from normal cells, such as fibroblasts or epithelial cells. Cell lines are characterized by their unique genetic makeup, which can be used to identify them and compare them to other cell lines. Because cell lines can be grown in large quantities and are relatively easy to maintain, they are a valuable tool in medical research. They allow researchers to study the effects of drugs and other treatments on specific cell types, and to investigate the underlying mechanisms of diseases at the cellular level.

Calmodulin-binding proteins (CaMBPs) are a group of proteins that interact with the calcium-binding protein calmodulin (CaM) in the cell. These proteins play important roles in various cellular processes, including signal transduction, gene expression, and cell division. CaM is a small, ubiquitous protein that is found in all eukaryotic cells. It is composed of two globular domains, each of which can bind to one molecule of calcium. When calcium levels in the cell increase, CaM binds to calcium ions and undergoes a conformational change that allows it to interact with other proteins, including CaMBPs. CaMBPs are a diverse group of proteins that include enzymes, ion channels, and transcription factors. Some examples of CaMBPs include: * Phosphodiesterase 4D (PDE4D): an enzyme that breaks down cyclic AMP (cAMP) in the cell, which is an important second messenger in signal transduction. * Calmodulin-dependent protein kinase II (CaMKII): an enzyme that plays a key role in the regulation of neuronal signaling and learning and memory. * Ryanodine receptor (RyR): a protein that regulates the release of calcium ions from the endoplasmic reticulum in muscle cells. * Calmodulin-dependent transcription activator (CAMTA): a transcription factor that regulates the expression of genes involved in plant development and stress responses. Overall, CaMBPs are important regulators of cellular signaling and function, and their activity is tightly controlled by calcium levels in the cell.

In the medical field, binding sites refer to specific locations on the surface of a protein molecule where a ligand (a molecule that binds to the protein) can attach. These binding sites are often formed by a specific arrangement of amino acids within the protein, and they are critical for the protein's function. Binding sites can be found on a wide range of proteins, including enzymes, receptors, and transporters. When a ligand binds to a protein's binding site, it can cause a conformational change in the protein, which can alter its activity or function. For example, a hormone may bind to a receptor protein, triggering a signaling cascade that leads to a specific cellular response. Understanding the structure and function of binding sites is important in many areas of medicine, including drug discovery and development, as well as the study of diseases caused by mutations in proteins that affect their binding sites. By targeting specific binding sites on proteins, researchers can develop drugs that modulate protein activity and potentially treat a wide range of diseases.

Mitogen-Activated Protein Kinases (MAPKs) are a family of enzymes that play a crucial role in cellular signaling pathways. They are involved in regulating various cellular processes such as cell growth, differentiation, proliferation, survival, and apoptosis. MAPKs are activated by extracellular signals such as growth factors, cytokines, and hormones, which bind to specific receptors on the cell surface. This activation leads to a cascade of phosphorylation events, where MAPKs phosphorylate and activate downstream effector molecules, such as transcription factors, that regulate gene expression. In the medical field, MAPKs are of great interest due to their involvement in various diseases, including cancer, inflammatory disorders, and neurological disorders. For example, mutations in MAPK signaling pathways are commonly found in many types of cancer, and targeting these pathways has become an important strategy for cancer therapy. Additionally, MAPKs are involved in the regulation of immune responses, and dysregulation of these pathways has been implicated in various inflammatory disorders. Finally, MAPKs play a role in the development and maintenance of the nervous system, and dysfunction of these pathways has been linked to neurological disorders such as Alzheimer's disease and Parkinson's disease.

Sulfonamides are a class of synthetic antimicrobial drugs that were first discovered in the 1930s. They are commonly used to treat a variety of bacterial infections, including urinary tract infections, respiratory infections, and skin infections. Sulfonamides work by inhibiting the production of folic acid by bacteria, which is essential for their growth and reproduction. They are often used in combination with other antibiotics to increase their effectiveness. Sulfonamides are generally well-tolerated, but can cause side effects such as nausea, vomiting, and allergic reactions in some people.

Calcium-binding proteins are a class of proteins that have a high affinity for calcium ions. They play important roles in a variety of cellular processes, including signal transduction, gene expression, and cell motility. Calcium-binding proteins are found in many different types of cells and tissues, and they can be classified into several different families based on their structure and function. Some examples of calcium-binding proteins include calmodulin, troponin, and parvalbumin. These proteins are often regulated by changes in intracellular calcium levels, and they play important roles in the regulation of many different physiological processes.

Trifluoperazine is a medication that belongs to a class of drugs called antipsychotics. It is primarily used to treat schizophrenia, a mental disorder characterized by hallucinations, delusions, and disorganized thinking. Trifluoperazine works by blocking the action of dopamine, a neurotransmitter that plays a role in the brain's reward and pleasure centers. It can also be used to treat other conditions, such as bipolar disorder and Tourette's syndrome. Trifluoperazine is usually taken orally in tablet form, and the dosage and duration of treatment will depend on the individual patient's needs and response to the medication. Like all medications, trifluoperazine can have side effects, and it is important to discuss these with a healthcare provider before starting treatment.

In the medical field, the term "cattle" refers to large domesticated animals that are raised for their meat, milk, or other products. Cattle are a common source of food and are also used for labor in agriculture, such as plowing fields or pulling carts. In veterinary medicine, cattle are often referred to as "livestock" and may be treated for a variety of medical conditions, including diseases, injuries, and parasites. Some common medical issues that may affect cattle include respiratory infections, digestive problems, and musculoskeletal disorders. Cattle may also be used in medical research, particularly in the fields of genetics and agriculture. For example, scientists may study the genetics of cattle to develop new breeds with desirable traits, such as increased milk production or resistance to disease.

Myosin-Light-Chain Kinase (MLCK) is an enzyme that plays a crucial role in regulating muscle contraction. It is a calcium-dependent enzyme that phosphorylates the regulatory light chain of myosin, which is a component of the thick filament in muscle fibers. Phosphorylation of the regulatory light chain leads to the activation of myosin, which in turn causes the sliding of actin filaments over myosin filaments, resulting in muscle contraction. MLCK is also involved in regulating the contraction of smooth muscle cells, which are found in the walls of blood vessels, the gut, and other organs. Activation of MLCK in smooth muscle cells leads to the contraction of the muscle fibers, which can contribute to the regulation of blood pressure and the movement of food through the digestive system. In addition to its role in muscle contraction, MLCK has been implicated in a number of other physiological processes, including the regulation of cell migration, the formation of blood clots, and the development of certain types of cancer.

Phosphatidylinositol 3-kinases (PI3Ks) are a family of enzymes that play a critical role in cellular signaling pathways. They are involved in a wide range of cellular processes, including cell growth, proliferation, differentiation, survival, migration, and metabolism. PI3Ks are activated by various extracellular signals, such as growth factors, hormones, and neurotransmitters, and they generate second messengers by phosphorylating phosphatidylinositol lipids on the inner leaflet of the plasma membrane. This leads to the recruitment and activation of downstream effector molecules, such as protein kinases and phosphatases, which regulate various cellular processes. Dysregulation of PI3K signaling has been implicated in the development of various diseases, including cancer, diabetes, and neurological disorders. Therefore, PI3Ks are important targets for the development of therapeutic agents for these diseases.

P38 Mitogen-Activated Protein Kinases (MAPKs) are a family of serine/threonine protein kinases that play a crucial role in regulating various cellular processes, including cell proliferation, differentiation, survival, and apoptosis. They are activated by a variety of extracellular stimuli, such as cytokines, growth factors, and stress signals, and are involved in the regulation of inflammation, immune responses, and metabolic processes. In the medical field, p38 MAPKs have been implicated in the pathogenesis of various diseases, including cancer, inflammatory disorders, and neurodegenerative diseases. Targeting p38 MAPKs with small molecule inhibitors or other therapeutic agents has been proposed as a potential strategy for the treatment of these diseases. However, further research is needed to fully understand the role of p38 MAPKs in disease pathogenesis and to develop effective therapeutic interventions.

In the medical field, a base sequence refers to the specific order of nucleotides (adenine, thymine, cytosine, and guanine) that make up the genetic material (DNA or RNA) of an organism. The base sequence determines the genetic information encoded within the DNA molecule and ultimately determines the traits and characteristics of an individual. The base sequence can be analyzed using various techniques, such as DNA sequencing, to identify genetic variations or mutations that may be associated with certain diseases or conditions.

eIF-2 Kinase is an enzyme that plays a crucial role in regulating protein synthesis in cells. It phosphorylates a specific site on the alpha subunit of eukaryotic initiation factor 2 (eIF2), which is a key component of the machinery that initiates the process of translating messenger RNA (mRNA) into proteins. Under normal conditions, eIF2 is in a dephosphorylated state and is able to bind to initiator tRNA and other components of the translation machinery to initiate protein synthesis. However, when cells are under stress, such as from viral infection or nutrient deprivation, the activity of eIF2 Kinase is increased, leading to the phosphorylation of eIF2. This, in turn, inhibits the ability of eIF2 to bind to initiator tRNA, which slows down or shuts down protein synthesis. The regulation of eIF2 Kinase activity is an important mechanism for controlling protein synthesis in cells and maintaining cellular homeostasis. Dysregulation of eIF2 Kinase activity has been implicated in a number of diseases, including viral infections, neurodegenerative disorders, and certain types of cancer.

Tetradecanoylphorbol acetate (TPA) is a synthetic compound that belongs to a class of chemicals called phorbol esters. It is a potent tumor promoter and has been used in research to study the mechanisms of cancer development and progression. TPA works by activating protein kinase C (PKC), a family of enzymes that play a key role in cell signaling and proliferation. When TPA binds to a specific receptor on the cell surface, it triggers a cascade of events that leads to the activation of PKC, which in turn promotes cell growth and division. TPA has been shown to promote the growth of tumors in animal models and has been linked to the development of certain types of cancer in humans, including skin cancer and breast cancer. It is also used in some experimental treatments for cancer, although its use is limited due to its potential toxicity and side effects.

Protein kinase C-alpha (PKC-alpha) is a type of protein kinase enzyme that plays a crucial role in various cellular processes, including cell growth, differentiation, and apoptosis. It is a member of the protein kinase C (PKC) family of enzymes, which are involved in the regulation of cell signaling pathways. PKC-alpha is activated by the binding of diacylglycerol (DAG) and calcium ions, which are released from intracellular stores in response to various stimuli, such as hormones, growth factors, and neurotransmitters. Once activated, PKC-alpha phosphorylates a wide range of target proteins, including transcription factors, ion channels, and enzymes, leading to changes in cellular behavior. In the medical field, PKC-alpha has been implicated in various diseases and disorders, including cancer, cardiovascular disease, and neurodegenerative diseases. For example, PKC-alpha has been shown to play a role in the development and progression of various types of cancer, including breast cancer, prostate cancer, and colon cancer. In addition, PKC-alpha has been implicated in the pathogenesis of cardiovascular diseases, such as atherosclerosis and hypertension, as well as neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease. Therefore, PKC-alpha is an important target for the development of new therapeutic strategies for the treatment of various diseases and disorders.

Pyruvate kinase (PK) is an enzyme that plays a crucial role in cellular metabolism. It catalyzes the conversion of phosphoenolpyruvate (PEP) to pyruvate, which is a key step in glycolysis, the process by which cells convert glucose into energy. In the medical field, PK is of particular interest because it is involved in the regulation of glucose metabolism in various tissues, including the liver, muscle, and red blood cells. PK is also a potential target for the development of new drugs to treat a variety of diseases, including cancer, diabetes, and sickle cell anemia. Mutations in the PK gene can lead to a deficiency in the enzyme, which can result in a number of metabolic disorders. For example, a deficiency in PK in red blood cells can cause a type of anemia called pyruvate kinase deficiency, which can cause fatigue, jaundice, and other symptoms. In addition, mutations in the PK gene have been linked to an increased risk of certain types of cancer, including liver cancer and colon cancer.

Mitogen-Activated Protein Kinase 1 (MAPK1), also known as Extracellular Signal-regulated Kinase 1 (ERK1), is a protein kinase enzyme that plays a crucial role in cellular signaling pathways. It is part of the mitogen-activated protein kinase (MAPK) family, which is involved in regulating various cellular processes such as cell proliferation, differentiation, survival, and apoptosis. MAPK1 is activated by a variety of extracellular signals, including growth factors, cytokines, and hormones, and it transduces these signals into the cell by phosphorylating and activating downstream target proteins. These target proteins include transcription factors, cytoskeletal proteins, and enzymes involved in metabolism. In the medical field, MAPK1 is of interest because it is involved in the development and progression of many diseases, including cancer, inflammatory disorders, and neurological disorders. For example, mutations in the MAPK1 gene have been associated with various types of cancer, including breast cancer, colon cancer, and glioblastoma. In addition, MAPK1 has been implicated in the pathogenesis of inflammatory diseases such as rheumatoid arthritis and psoriasis, as well as neurological disorders such as Alzheimer's disease and Parkinson's disease. Therefore, understanding the role of MAPK1 in cellular signaling pathways and its involvement in various diseases is important for the development of new therapeutic strategies for these conditions.

Calcium channels are specialized proteins found in the cell membrane of many types of cells, including neurons, muscle cells, and epithelial cells. These channels allow calcium ions to pass through the cell membrane, regulating the flow of calcium into and out of the cell. Calcium channels play a crucial role in many physiological processes, including muscle contraction, neurotransmitter release, and the regulation of gene expression. Calcium channels can be classified into several types based on their structure and function, including voltage-gated calcium channels, ligand-gated calcium channels, and store-operated calcium channels. In the medical field, calcium channels are the target of many drugs, including anti-seizure medications, anti-anxiety medications, and antiarrhythmics. Abnormalities in calcium channel function have been linked to a variety of diseases, including hypertension, heart disease, and neurological disorders such as epilepsy and multiple sclerosis.

Death-Associated Protein Kinases (DAPKs) are a family of serine/threonine protein kinases that play a role in regulating cell survival and death. They are named for their association with programmed cell death, or apoptosis, although they have also been implicated in other cellular processes such as autophagy and differentiation. DAPKs are expressed in a variety of tissues and cell types, and their activity is regulated by a number of factors including calcium levels, phosphorylation, and interactions with other proteins. In response to cellular stress or injury, DAPKs can become activated and promote apoptosis by phosphorylating and activating other pro-apoptotic proteins. Alternatively, they can also be inhibited by anti-apoptotic proteins, leading to cell survival. DAPKs have been implicated in a number of diseases, including cancer, neurodegenerative disorders, and cardiovascular disease. For example, some studies have suggested that DAPK1, a member of the DAPK family, may play a role in the development of certain types of cancer by promoting apoptosis in cancer cells. However, other studies have suggested that DAPKs may also have anti-tumor effects by inhibiting the growth and survival of cancer cells. Further research is needed to fully understand the role of DAPKs in health and disease.

Cyclic AMP-dependent protein kinase catalytic subunits, also known as cAMP-dependent protein kinases or PKA, are a family of enzymes that play a crucial role in regulating various cellular processes in the body. These enzymes are activated by the presence of cyclic AMP (cAMP), a second messenger molecule that is produced in response to various stimuli, such as hormones and neurotransmitters. The catalytic subunits of PKA are responsible for the catalytic activity of the enzyme, which involves the transfer of a phosphate group from ATP to a substrate protein. This process can alter the activity of the substrate protein, leading to changes in cellular function. PKA is involved in a wide range of cellular processes, including metabolism, gene expression, and cell proliferation. Dysregulation of PKA activity has been implicated in a number of diseases, including cancer, diabetes, and neurological disorders. In the medical field, PKA is an important target for drug development, as modulating its activity can have therapeutic effects in various diseases. For example, drugs that inhibit PKA activity are being developed as potential treatments for cancer, while drugs that activate PKA are being investigated as potential treatments for diabetes and other metabolic disorders.

Blotting, Western is a laboratory technique used to detect specific proteins in a sample by transferring proteins from a gel to a membrane and then incubating the membrane with a specific antibody that binds to the protein of interest. The antibody is then detected using an enzyme or fluorescent label, which produces a visible signal that can be quantified. This technique is commonly used in molecular biology and biochemistry to study protein expression, localization, and function. It is also used in medical research to diagnose diseases and monitor treatment responses.

Phosphoprotein phosphatases are enzymes that remove phosphate groups from phosphoproteins, which are proteins that have been modified by the addition of a phosphate group. These enzymes play a crucial role in regulating cellular signaling pathways by modulating the activity of phosphoproteins. There are several types of phosphoprotein phosphatases, including protein tyrosine phosphatases (PTPs), protein serine/threonine phosphatases (S/T phosphatases), and phosphatases that can dephosphorylate both tyrosine and serine/threonine residues. Phosphoprotein phosphatases are involved in a wide range of cellular processes, including cell growth and division, metabolism, and immune response. Dysregulation of phosphoprotein phosphatase activity has been implicated in various diseases, including cancer, diabetes, and neurodegenerative disorders.

Mitogen-Activated Protein Kinase Kinases (MAPKKs), also known as Mitogen-Activated Protein Kinase Activators (MAPKAs), are a family of enzymes that play a crucial role in regulating various cellular processes, including cell proliferation, differentiation, survival, and apoptosis. MAPKKs are responsible for activating Mitogen-Activated Protein Kinases (MAPKs), which are a group of serine/threonine kinases that transmit signals from the cell surface to the nucleus. MAPKKs are activated by various extracellular signals, such as growth factors, cytokines, and hormones, and they in turn activate MAPKs by phosphorylating them on specific residues. MAPKKs are involved in a wide range of cellular processes, including cell cycle progression, differentiation, and apoptosis. They are also involved in the regulation of inflammation, immune responses, and cancer development. Dysregulation of MAPKK signaling has been implicated in various diseases, including cancer, autoimmune disorders, and neurodegenerative diseases. In the medical field, MAPKKs are being studied as potential therapeutic targets for the treatment of various diseases. For example, inhibitors of MAPKKs are being developed as potential anti-cancer agents, as they can block the activation of MAPKs and prevent cancer cell proliferation and survival. Additionally, MAPKKs are being studied as potential targets for the treatment of inflammatory and autoimmune disorders, as they play a key role in regulating immune responses.

Mitogen-Activated Protein Kinase 3 (MAPK3), also known as extracellular signal-regulated kinase 1 (ERK1), is a protein kinase enzyme that plays a crucial role in cellular signaling pathways. It is part of the mitogen-activated protein kinase (MAPK) family, which is involved in regulating various cellular processes such as cell proliferation, differentiation, survival, and apoptosis. MAPK3 is activated by a variety of extracellular signals, including growth factors, cytokines, and hormones, and it transduces these signals into the cell by phosphorylating and activating downstream target proteins. These target proteins include transcription factors, cytoskeletal proteins, and enzymes involved in metabolism. In the medical field, MAPK3 is of interest because it has been implicated in the development and progression of various diseases, including cancer, neurodegenerative disorders, and inflammatory diseases. For example, dysregulation of MAPK3 signaling has been observed in many types of cancer, and targeting this pathway has been proposed as a potential therapeutic strategy. Additionally, MAPK3 has been shown to play a role in the pathogenesis of conditions such as Alzheimer's disease and Parkinson's disease, as well as in the regulation of immune responses and inflammation.

Recombinant proteins are proteins that are produced by genetically engineering bacteria, yeast, or other organisms to express a specific gene. These proteins are typically used in medical research and drug development because they can be produced in large quantities and are often more pure and consistent than proteins that are extracted from natural sources. Recombinant proteins can be used for a variety of purposes in medicine, including as diagnostic tools, therapeutic agents, and research tools. For example, recombinant versions of human proteins such as insulin, growth hormones, and clotting factors are used to treat a variety of medical conditions. Recombinant proteins can also be used to study the function of specific genes and proteins, which can help researchers understand the underlying causes of diseases and develop new treatments.

Protein Kinase C-delta (PKC-delta) is a type of protein kinase enzyme that plays a role in various cellular processes, including cell proliferation, differentiation, and apoptosis. It is a member of the Protein Kinase C (PKC) family of enzymes, which are involved in the regulation of cell signaling pathways. In the medical field, PKC-delta has been implicated in a number of diseases and conditions, including cancer, neurodegenerative disorders, and inflammatory diseases. For example, PKC-delta has been shown to play a role in the development and progression of various types of cancer, including breast cancer, prostate cancer, and leukemia. It has also been implicated in the pathogenesis of neurodegenerative disorders such as Alzheimer's disease and Parkinson's disease, as well as in the regulation of inflammation and immune responses. PKC-delta is a potential therapeutic target for the development of new drugs for the treatment of these diseases. However, more research is needed to fully understand the role of PKC-delta in disease pathogenesis and to develop effective targeted therapies.

In the medical field, Isoquinolines are a class of organic compounds that are derived from the isoquinoline ring system. They are nitrogen-containing heterocyclic compounds that have a six-membered ring with two nitrogen atoms and four carbon atoms. Isoquinolines have a variety of biological activities and are used in the development of drugs for the treatment of various diseases. For example, some isoquinolines have been found to have anti-inflammatory, analgesic, and anti-tumor properties. They are also used as antimalarial agents, antiarrhythmics, and as inhibitors of various enzymes. Some well-known drugs that contain isoquinoline rings include quinine, which is used to treat malaria, and hyoscine, which is used as an antispasmodic. Other examples include the anti-inflammatory drug nimesulide and the antiarrhythmic drug quinidine.

Adenosine triphosphate (ATP) is a molecule that serves as the primary energy currency in living cells. It is composed of three phosphate groups attached to a ribose sugar and an adenine base. In the medical field, ATP is essential for many cellular processes, including muscle contraction, nerve impulse transmission, and the synthesis of macromolecules such as proteins and nucleic acids. ATP is produced through cellular respiration, which involves the breakdown of glucose and other molecules to release energy that is stored in the bonds of ATP. Disruptions in ATP production or utilization can lead to a variety of medical conditions, including muscle weakness, fatigue, and neurological disorders. In addition, ATP is often used as a diagnostic tool in medical testing, as levels of ATP can be measured in various bodily fluids and tissues to assess cellular health and function.

JNK Mitogen-Activated Protein Kinases (JNK MAPKs) are a family of serine/threonine protein kinases that play a crucial role in cellular signaling pathways. They are activated in response to various cellular stresses, including oxidative stress, UV radiation, and cytokines. JNK MAPKs are involved in the regulation of cell proliferation, differentiation, and apoptosis, as well as the inflammatory response. Dysregulation of JNK MAPK signaling has been implicated in a variety of diseases, including cancer, neurodegenerative disorders, and inflammatory diseases. Therefore, JNK MAPKs are an important target for the development of new therapeutic strategies.

Peptide T is a synthetic peptide that is used in the diagnosis and monitoring of autoimmune diseases, particularly myasthenia gravis. It is a fragment of the acetylcholine receptor (AChR) protein, which is the target of the autoimmune response in myasthenia gravis. Peptide T is used in laboratory tests to detect antibodies against the AChR, which are produced by the immune system in people with myasthenia gravis. These antibodies can block the AChR, leading to muscle weakness and fatigue. Peptide T is also used to monitor the effectiveness of treatment for myasthenia gravis, as the level of antibodies in the blood can be used to assess the severity of the disease and the response to therapy.

Serine is an amino acid that is a building block of proteins. It is a non-essential amino acid, meaning that it can be synthesized by the body from other compounds. In the medical field, serine is known to play a role in various physiological processes, including the production of neurotransmitters, the regulation of blood sugar levels, and the maintenance of healthy skin and hair. It is also used as a dietary supplement to support these functions and to promote overall health. In some cases, serine may be prescribed by a healthcare provider to treat certain medical conditions, such as liver disease or depression.

Phosphoproteins are proteins that have been modified by the addition of a phosphate group to one or more of their amino acid residues. This modification is known as phosphorylation, and it is a common post-translational modification that plays a critical role in regulating many cellular processes, including signal transduction, metabolism, and gene expression. Phosphoproteins are involved in a wide range of biological functions, including cell growth and division, cell migration and differentiation, and the regulation of gene expression. They are also involved in many diseases, including cancer, diabetes, and cardiovascular disease. Phosphoproteins can be detected and studied using a variety of techniques, including mass spectrometry, Western blotting, and immunoprecipitation. These techniques allow researchers to identify and quantify the phosphorylation status of specific proteins in cells and tissues, and to study the effects of changes in phosphorylation on protein function and cellular processes.

In the medical field, "Nucleotides, Cyclic" refers to a class of molecules that are composed of a cyclic structure containing a nitrogenous base, a pentose sugar, and a phosphate group. These molecules are important components of DNA and RNA, which are the genetic material of all living organisms. Cyclic nucleotides are a subclass of nucleotides that have a cyclic structure formed by the condensation of the sugar and phosphate groups. They are involved in various cellular signaling pathways and have been implicated in the regulation of a wide range of physiological processes, including blood pressure, heart rate, and immune function. Examples of cyclic nucleotides include cyclic adenosine monophosphate (cAMP) and cyclic guanosine monophosphate (cGMP). These molecules are synthesized from their respective nucleoside triphosphates (ATP and GTP) by the action of enzymes called adenylate cyclase and guanylate cyclase, respectively.

I'm sorry, but I couldn't find any information on a medication or compound called "Egtazic Acid" in the medical field. It's possible that you may have misspelled the name or that it is a relatively new or obscure medication. If you have any additional information or context, please let me know and I'll do my best to help you.

AMP-Activated Protein Kinases (AMPK) are a family of enzymes that play a critical role in regulating cellular energy metabolism and maintaining cellular homeostasis. They are activated in response to a decrease in the ratio of ATP to AMP, which occurs under conditions of energy stress, such as during exercise or fasting. AMPK acts as a cellular energy sensor, and its activation leads to a variety of metabolic changes that help to restore energy balance. These changes include increasing glucose uptake and metabolism, inhibiting fatty acid synthesis, and stimulating fatty acid oxidation. AMPK also plays a role in regulating cell growth and survival, and has been implicated in the development of a number of diseases, including diabetes, obesity, and cancer. In the medical field, AMPK is a target for the development of new drugs for the treatment of metabolic disorders and other diseases. Activation of AMPK has been shown to improve insulin sensitivity, reduce body weight, and lower blood pressure, making it a promising therapeutic target for the treatment of type 2 diabetes, obesity, and cardiovascular disease.

In the medical field, RNA, Messenger (mRNA) refers to a type of RNA molecule that carries genetic information from DNA in the nucleus of a cell to the ribosomes, where proteins are synthesized. During the process of transcription, the DNA sequence of a gene is copied into a complementary RNA sequence called messenger RNA (mRNA). This mRNA molecule then leaves the nucleus and travels to the cytoplasm of the cell, where it binds to ribosomes and serves as a template for the synthesis of a specific protein. The sequence of nucleotides in the mRNA molecule determines the sequence of amino acids in the protein that is synthesized. Therefore, changes in the sequence of nucleotides in the mRNA molecule can result in changes in the amino acid sequence of the protein, which can affect the function of the protein and potentially lead to disease. mRNA molecules are often used in medical research and therapy as a way to introduce new genetic information into cells. For example, mRNA vaccines work by introducing a small piece of mRNA that encodes for a specific protein, which triggers an immune response in the body.

Protamine kinase is an enzyme that is involved in the regulation of blood clotting. It is responsible for converting protamine sulfate, a substance that is used to neutralize the anticoagulant effects of heparin, into protamine. Protamine sulfate is often used in conjunction with heparin during medical procedures, such as surgery or catheterization, to prevent excessive bleeding. Protamine kinase helps to ensure that the appropriate amount of protamine is present to neutralize the heparin, preventing the formation of blood clots.

Cytosol is the fluid inside the cytoplasm of a cell, which is the gel-like substance that fills the cell membrane. It is also known as the cytoplasmic matrix or cytosolic matrix. The cytosol is a complex mixture of water, ions, organic molecules, and various enzymes and other proteins that play important roles in cellular metabolism, signaling, and transport. It is the site of many cellular processes, including protein synthesis, energy production, and waste removal. The cytosol is also the site of many cellular organelles, such as the mitochondria, ribosomes, and endoplasmic reticulum, which are responsible for carrying out specific cellular functions.

Recombinant fusion proteins are proteins that are produced by combining two or more genes in a single molecule. These proteins are typically created using genetic engineering techniques, such as recombinant DNA technology, to insert one or more genes into a host organism, such as bacteria or yeast, which then produces the fusion protein. Fusion proteins are often used in medical research and drug development because they can have unique properties that are not present in the individual proteins that make up the fusion. For example, a fusion protein might be designed to have increased stability, improved solubility, or enhanced targeting to specific cells or tissues. Recombinant fusion proteins have a wide range of applications in medicine, including as therapeutic agents, diagnostic tools, and research reagents. Some examples of recombinant fusion proteins used in medicine include antibodies, growth factors, and cytokines.

Calcium, dietary refers to the amount of calcium that is obtained from food and beverages consumed by an individual. Calcium is an essential mineral that plays a crucial role in maintaining strong bones and teeth, as well as regulating muscle function, nerve transmission, and blood clotting. The recommended daily intake of calcium varies depending on age, sex, and other factors. For adults, the recommended daily intake of calcium is 1000-1300 milligrams per day. Calcium can be obtained from a variety of sources, including dairy products (such as milk, cheese, and yogurt), leafy green vegetables (such as kale and spinach), fortified foods (such as cereal and orange juice), and certain types of fish (such as salmon and sardines). In the medical field, monitoring an individual's dietary calcium intake is important for maintaining optimal bone health and preventing conditions such as osteoporosis. A deficiency in dietary calcium can lead to weakened bones and an increased risk of fractures, while an excess of calcium can lead to kidney stones and other health problems.

In the medical field, "src-family kinases" (SFKs) refer to a group of non-receptor tyrosine kinases that are involved in a variety of cellular processes, including cell growth, differentiation, migration, and survival. SFKs are activated by a variety of stimuli, including growth factors, cytokines, and hormones, and they play a critical role in regulating cell signaling pathways. SFKs are a subfamily of the larger tyrosine kinase family, which includes over 90 different kinases that are involved in a wide range of cellular processes. SFKs are characterized by their unique domain structure, which includes an N-terminal myristoylation site, a src homology 2 (SH2) domain, and a src homology 3 (SH3) domain. SFKs are involved in a variety of diseases, including cancer, cardiovascular disease, and inflammatory disorders. In cancer, SFKs are often overexpressed or activated, leading to uncontrolled cell growth and proliferation. In cardiovascular disease, SFKs are involved in the regulation of blood vessel function and the development of atherosclerosis. In inflammatory disorders, SFKs play a role in the activation of immune cells and the production of inflammatory mediators. Overall, SFKs are an important group of kinases that play a critical role in regulating cellular signaling pathways and are involved in a variety of diseases.

Protein Kinase C-epsilon (PKC-epsilon) is a type of protein kinase enzyme that plays a role in various cellular processes, including cell growth, differentiation, and apoptosis. It is a member of the Protein Kinase C (PKC) family of enzymes, which are involved in the regulation of cell signaling pathways. PKC-epsilon is activated by the binding of diacylglycerol (DAG) and calcium ions, which are produced by the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by phospholipase C (PLC). Once activated, PKC-epsilon phosphorylates various substrates, including other proteins, lipids, and nucleotides, leading to changes in cellular behavior. In the medical field, PKC-epsilon has been implicated in various diseases, including cancer, cardiovascular disease, and neurodegenerative disorders. For example, PKC-epsilon has been shown to play a role in the development and progression of breast cancer, and its inhibition has been proposed as a potential therapeutic strategy for this disease. Additionally, PKC-epsilon has been implicated in the regulation of blood pressure and the development of hypertension, as well as in the pathogenesis of Alzheimer's disease and other neurodegenerative disorders.

Protein kinase C beta (PKCβ) is a type of protein kinase enzyme that plays a role in various cellular processes, including cell proliferation, differentiation, and apoptosis. It is a member of the protein kinase C (PKC) family of enzymes, which are involved in the regulation of cell signaling pathways. In the medical field, PKCβ has been implicated in a variety of diseases and conditions, including cancer, cardiovascular disease, and neurodegenerative disorders. For example, PKCβ has been shown to play a role in the development and progression of various types of cancer, including breast cancer, prostate cancer, and colon cancer. It has also been linked to the development of cardiovascular disease, such as atherosclerosis and hypertension, and to the progression of neurodegenerative disorders, such as Alzheimer's disease and Parkinson's disease. PKCβ is activated by the binding of diacylglycerol (DAG) and calcium ions, which leads to the phosphorylation of target proteins and the regulation of various cellular processes. Inhibition of PKCβ has been shown to have potential therapeutic benefits in the treatment of various diseases and conditions, and several PKCβ inhibitors are currently being investigated in preclinical and clinical studies.

Protein-tyrosine kinases (PTKs) are a family of enzymes that play a crucial role in various cellular processes, including cell growth, differentiation, metabolism, and signal transduction. These enzymes catalyze the transfer of a phosphate group from ATP to the hydroxyl group of tyrosine residues on specific target proteins, thereby modifying their activity, localization, or interactions with other molecules. PTKs are involved in many diseases, including cancer, cardiovascular disease, and neurological disorders. They are also targets for many drugs, including those used to treat cancer and other diseases. In the medical field, PTKs are studied to understand their role in disease pathogenesis and to develop new therapeutic strategies.

1-Phosphatidylinositol 4-kinase (PI4K) is an enzyme that plays a crucial role in the biosynthesis of phosphatidylinositol 4-phosphate (PI4P), a phospholipid that is involved in various cellular processes such as vesicle trafficking, signal transduction, and membrane organization. PI4K is a family of enzymes that are encoded by multiple genes and are found in different cellular compartments, including the endoplasmic reticulum, Golgi apparatus, plasma membrane, and endosomes. Dysregulation of PI4K activity has been implicated in various diseases, including cancer, neurodegenerative disorders, and immune system dysfunction. Therefore, PI4K is an important target for the development of new therapeutic strategies.

Calcium/calmodulin-dependent protein kinase type IV is an enzyme that in humans is encoded by the CAMK4 gene. The product of ... calmodulin-dependent protein kinase I by calmodulin and by Ca2+/calmodulin-dependent protein kinase kinase". J. Biol. Chem. 273 ... Phosphorylation by cyclic AMP-dependent protein kinase, protein kinase C, and calcium/calmodulin protein kinase; identification ... and activation of Ca2+-calmodulin-dependent protein kinase IV by Ca2+-calmodulin-dependent protein kinase Ia kinase. ...

https://en.wikipedia.org/wiki/CAMK4

CAMK2G and CAMK2D belong to the same calcium/calmodulin dependent protein kinase subfamily. These kinases play important roles ... Namely apoptosis of type 2 alveolar epithelial cell (L2) through the AMPK-regulated endoplasmic reticulum (ER) stress-triggered ... Including the activation of ERK and other mitogen-activated protein kinases. eNOS or endothelial nitric oxide synthase ... Mifflin, L.; Ofengeim, D.; Yuan, J. (2020). "Receptor-interacting protein kinase 1 (RIPK1) as a therapeutic target". Nature ...

https://en.wikipedia.org/wiki/4-Methyl-2,4-bis(4-hydroxyphenyl)pent-1-ene

This gene is also known by several other names: CMG 2 (CAMGUK protein 2), calcium/calmodulin-dependent serine protein kinase 3 ... Hsueh YP, Roberts AM, Volta M, Sheng M, Roberts RG (June 2001). "Bipartite interaction between neurofibromatosis type I protein ... "Entrez Gene: CASK Calcium/calmodulin-dependent serine protein kinase (MAGUK family)". Tarpey PS, Smith R, Pleasance E, Whibley ... Zhu ZQ, Wang D, Xiang D, Yuan YX, Wang Y (January 2014). "Calcium/calmodulin-dependent serine protein kinase is involved in ...

https://en.wikipedia.org/wiki/CASK

... a calcium pump EC 7.2.2.10. The protein encoded by this gene belongs to the family of P-type primary ion transport ATPases ... Wang KK, Wright LC, Machan CL, Allen BG, Conigrave AD, Roufogalis BD (May 1991). "Protein kinase C phosphorylates the carboxyl ... "Primary structure of the cAMP-dependent phosphorylation site of the plasma membrane calcium pump". Biochemistry. 28 (10): 4253- ... Kessler F, Falchetto R, Heim R, Meili R, Vorherr T, Strehler EE, Carafoli E (December 1992). "Study of calmodulin binding to ...

https://en.wikipedia.org/wiki/ATP2B1

Harris AS, Croall DE, Morrow JS (1988). "The calmodulin-binding site in alpha-fodrin is near the calcium-dependent protease-I ... "Primary structure of a gamma subunit of G protein, gamma 12, and its phosphorylation by protein kinase C". J. Biol. Chem. 270 ( ... The European Consortium on Men1, (GENEM 1; Groupe d'Etude des Néoplasies Endocriniennes Multiples de type 1)". Genomics. 37 (3 ... Sorimachi H, Ohmi S, Emori Y, Kawasaki H, Saido TC, Ohno S, Minami Y, Suzuki K (1990). "A novel member of the calcium-dependent ...

https://en.wikipedia.org/wiki/Calpain-1_catalytic_subunit

PIK1 It binds to many proteins, some in calcium dependent and some in calcium independent ways, and switches many of the ... G-protein-coupled receptor kinase 2) D2 dopamine receptor IL1RAPL1 (interleukin-1 receptor accessory protein-like 1 protein) ... calcium-binding protein. Frq can substitute for calmodulin in some situations. It is thought to be associated with neuronal ... The designation 'NCS-1' came from the assumption that the protein was expressed only in neuronal cell types, which is not the ...

https://en.wikipedia.org/wiki/Neuronal_calcium_sensor-1

Calcium/calmodulin-dependent protein kinase type II beta chain is an enzyme that in humans is encoded by the CAMK2B gene. The ... "Entrez Gene: CAMK2B calcium/calmodulin-dependent protein kinase (CaM kinase) II beta". Walikonis RS, Oguni A, Khorosheva EM, ... Sequence analyses of human brain calcium/calmodulin-dependent protein kinase II". Mol. Biol. Rep. 28 (1): 35-41. doi:10.1023/A: ... Novak G, Seeman P, Tallerico T (2001). "Schizophrenia: elevated mRNA for calcium-calmodulin-dependent protein kinase IIbeta in ...

https://en.wikipedia.org/wiki/CAMK2B

"Structure and expression of a calcium-binding protein gene contained within a calmodulin-regulated protein kinase gene". ... encodes myosin light chain kinase which is a calcium/calmodulin dependent enzyme. Four transcript variants that produce four ... Reaction type: phospho group transfer) It requires Ca2+ and calmodulin for activity. The 20-kDa light chain from smooth muscle ... "Kinase-related protein (telokin) is phosphorylated by smooth-muscle myosin light-chain kinase and modulates the kinase activity ...

https://en.wikipedia.org/wiki/Telokin

... by protein kinase C and calcium/calmodulin kinase II in vitro". J. Neurochem. 71 (3): 1307-14. doi:10.1046/j.1471-4159.1998. ... Kubes M, Cordier J, Glowinski J, Girault JA, Chneiweiss H (1998). "Endothelin induces a calcium-dependent phosphorylation of ... "Molecular characterization of the human PEA15 gene on 1q21-q22 and association with type 2 diabetes mellitus in Pima Indians". ... "Protein kinase B/Akt binds and phosphorylates PED/PEA-15, stabilizing its antiapoptotic action". Mol. Cell. Biol. 23 (13): 4511 ...

https://en.wikipedia.org/wiki/PEA15

... a novel two EF-hand calcium-binding protein that suppresses Ca2+/calmodulin-dependent protein kinase II activity in the brain ... Expression of CaBP1 helps to block Ca2+-dependent facilitation of P/Q-type Ca2+ current which is markedly reduced facilitation ... Calcium binding protein 1 is a protein that in humans is encoded by the CABP1 gene. Calcium-binding protein 1 is a calcium- ... Calcium-binding protein 1 which is a neuron -specific member of the calmodulin (CaM) superfamily which modulates Ca2+-dependent ...

https://en.wikipedia.org/wiki/Calcium-binding_protein_1

Zhang S, Ehlers MD, Bernhardt JP, Su CT, Huganir RL (August 1998). "Calmodulin mediates calcium-dependent inactivation of N- ... a striated muscle-restricted PDZ and LIM domain-containing protein, binds to alpha-actinin-2 and protein kinase C". The Journal ... Young P, Ferguson C, Bañuelos S, Gautel M (March 1998). "Molecular structure of the sarcomeric Z-disk: two types of titin ... ". "Protein Information - Basic Information: Protein COPaKB ID: P35609". Cardiac Organellar Protein Atlas Knowledgebase. ...

https://en.wikipedia.org/wiki/Alpha-actinin-2

... the microtubule-associated tau proteins and S100b regulate tau phosphorylation by the Ca2+/calmodulin-dependent protein kinase ... "The calcium-modulated proteins, S100A1 and S100B, as potential regulators of the dynamics of type III intermediate filaments". ... S100 calcium-binding protein B (S100B) is a protein of the S-100 protein family. S100 proteins are localized in the cytoplasm ... the microtubule-associated tau proteins and S100b regulate tau phosphorylation by the Ca2+/calmodulin-dependent protein kinase ...

https://en.wikipedia.org/wiki/S100B

... suggesting that inhibition of Ca2+/calmodulin-dependent protein kinase II may also be a potential treatment strategy. These ... which can be explained by decreased voltage-dependent calcium channel expression, specifically Ca(v)1.3, which is responsible ... Initially, a Glu1425Gly mutation in ANK2 was found to cause dominantly-inherited long QT syndrome type 4, cardiac arrhythmia. ... Effects on ryanodine receptors specifically were also rescued by a potent Ca2+/calmodulin-dependent protein kinase II inhibitor ...

https://en.wikipedia.org/wiki/Ankyrin-2

... encoding enzyme Pyridoxal kinase PFKL: encoding enzyme ATP-dependent 6-phosphofructokinase, liver type PIGP: encoding ... encoding protein RWD domain-containing protein 2B S100B: encoding calcium binding protein SAMSN1: encoding SAM domain- ... binding protein 3 PCNT: encoding protein centrosomal pericentrin PCP4: encoding calmodulin regulator protein PCP4 PDE9A: ... a C-type lectin CLDN8: encoding protein claudin-8 CLDN14: encoding protein claudin-14 CLDN17: encoding protein claudin-17 CLIC6 ...

https://en.wikipedia.org/wiki/Chromosome_21

... independent pathway involving calcium-binding protein 39 (Cab39) and serine threonine kinase with no lysine member 4 (WNK4) in ... WNK4 enhances TRPV5 by increasing its forward trafficking to the plasma membrane in a kinase-dependent manner. The inhibitory ... However, when Ca2+ levels are elevated, Ca2+/calmodulin complex binds to the C-terminal region, derepressing WNK4 kinase ... calcium channels), Na-K-2Cl cotransporter 1 and 2 (NKCC1/2), K+-Cl− cotransporter type 2 (KCC2), and other channels/ ...

https://en.wikipedia.org/wiki/WNK4

... p39 interact with the alpha-subunit of Ca2+/calmodulin-dependent protein kinase II and alpha-actinin-1 in a calcium-dependent ... "Regulation of type 1 protein phosphatase/inhibitor-2 complex by glycogen synthase kinase-3beta in intact cells". Journal of ... p39 interact with the alpha-subunit of Ca2+/calmodulin-dependent protein kinase II and alpha-actinin-1 in a calcium-dependent ... Cyclin-dependent kinase 5 activator 2 is an enzyme that in humans is encoded by the CDK5R2 gene. The protein encoded by this ...

https://en.wikipedia.org/wiki/CDK5R2

"Calmodulin is involved in the Ca2+-dependent activation of ceramide kinase as a calcium sensor". J. Biol. Chem. 280 (49): 40436 ... CERK shares sequence homology with sphingosine kinase type I, including an N-terminal pleckstrin homology (PH) domain and a ... It was demonstrated that C-1-P perpetuates the phosphorylation of glycogen synthase kinase-3 β and retinoblastoma protein, ... CERK was later confirmed to bind calmodulin in the presence of calcium, indicating the calmodulin first binds calcium and then ...

https://en.wikipedia.org/wiki/Ceramide_kinase

... encoding protein Chromosome 10 open reading frame 99 CAMK1D: calcium/calmodulin-dependent protein kinase ID CCAR1: Cell ... zinc finger protein 37A ZNF438: zinc finger protein 438 ZRANB1: Zinc finger ranbp2-type containing 1 The following diseases are ... encoding protein Transmembrane protein 26 TMEM72: encoding protein Transmembrane protein 72 TYSND1: encoding protein Trypsin ... encoding protein F-box and leucine rich repeat protein 15 FGFR2: fibroblast growth factor receptor 2 (bacteria-expressed kinase ...

https://en.wikipedia.org/wiki/Chromosome_10

... and a calcium/calmodulin-dependent kinase (CAMK-1), and additional kinases, reaching its peak around mid-subjective day. Kinase ... with just one of the proteins present. The choice of which protein is made is the result of temperature-dependent splicing of ... Because sFRQ favors a longer period than lFRQ, free running rhythms in wild type Neurospora are somewhat decreased with ... A similar palette of kinases modifies the clock proteins in all cases. Negative feedback White Collar-1 Baker CL, Loros JJ, ...

https://en.wikipedia.org/wiki/Frequency_(gene)

... and calmodulin (CaM). Calmodulin has been shown to activate cyclic nucleotide PDE in a calcium-dependent manner and the ... of PDE1A1 and PDE1A2 by protein kinase A and of PDE1B1 by CaM Kinase II decreases their sensitivity to calmodulin activation. ... basal and calmodulin stimulated purified PDE1. Since nimodipine at lower concentrations blocks the L-type calcium channel, it ... is a phosphodiesterase enzyme also known as calcium- and calmodulin-dependent phosphodiesterase. It is one of the 11 families ...

https://en.wikipedia.org/wiki/PDE1

"Interleukin 10 is induced by recombinant HIV-1 Nef protein involving the calcium/calmodulin-dependent phosphodiesterase signal ... "Entry - *114205 - CALCIUM CHANNEL, VOLTAGE-DEPENDENT, L TYPE, ALPHA-1C SUBUNIT; CACNA1C - OMIM". omim.org. Retrieved 2023-06-01 ... with melittin and microtubule-associated tau proteins and inhibition of phosphorylation of tau proteins by protein kinase C". ... Calmodulin 2 is a protein that in humans is encoded by the CALM2 gene. A member of the calmodulin family of signaling molecules ...

https://en.wikipedia.org/wiki/CALM2

Calcium/calmodulin-dependent protein kinase type II gamma chain is an enzyme that in humans is encoded by the CAMK2G gene. The ... "Entrez Gene: CAMK2G calcium/calmodulin-dependent protein kinase (CaM kinase) II gamma". Moyers JS, Bilan PJ, Zhu J, Kahn CR ( ... Calcium/calmodulin-dependent protein kinase type II subunit gamma) at the PDBe-KB. Portal: Biology This article incorporates ... calmodulin-dependent protein kinase subfamily. Calcium signaling is crucial for several aspects of plasticity at glutamatergic ...

https://en.wikipedia.org/wiki/CAMK2G

Calmodulin-dependent kinase II and Rho-kinase are also found to phosphorylate calponin at Ser175 and Thr184 in vitro. Of these ... Dephosphorylation of calponin is catalyzed by type 2B protein phosphatase Unphosphorylated calponin binds to actin and inhibits ... Calcium-dependent mechanisms of regulation of smooth muscle contraction". Biochemistry and Cell Biology. 69 (12): 771-800. doi: ... the main site of regulatory phosphorylation by calmodulin-dependent kinase II and Rho-kinase is Ser175. ...

https://en.wikipedia.org/wiki/Calponin_1

Bouvard D, Block MR (1998). "Calcium/calmodulin-dependent protein kinase II controls integrin alpha5beta1-mediated cell ... kinase is upstream of phosphatidylinositol 3-kinase/Akt in regulating fibroblast survival in response to contraction of type I ... 2007). "MAP kinase-dependent, NF-kappaB-independent regulation of inhibitor of apoptosis protein genes by TNF-alpha". J. Cell. ... 2006). "Integrin cytoplasmic domain-associated protein-1 (ICAP-1) interacts with the ROCK-I kinase at the plasma membrane". J. ...

https://en.wikipedia.org/wiki/ITGB1BP1

"Calcium/calmodulin-dependent protein kinase II phosphorylation drives synapse-associated protein 97 into spines". The Journal ... AMPARs are composed of four types of subunits encoded by different genes, designated as GRIA1 (also named GluA1 or GluR1), ... is the influx of calcium through the NMDA receptors and the resultant activation of Ca2+/calmodulin-dependent protein kinase ( ... element-binding protein through a phosphatidylinositol 3-kinase-dependent stimulation of the mitogen-activated protein kinase ...

https://en.wikipedia.org/wiki/AMPA_receptor

... but phosphorylation of both these subunits by protein kinase A (PKA, or cAMP-dependent protein kinase) reduces their respective ... Defects in phosphorylase kinase genes are the cause of glycogen storage disease type IX (GSD type IX) and GSD type VI (formerly ... activated when the β and α subunits are phosphorylated by protein kinase A and the delta subunit has bound to calcium ions. In ... The δ subunit is the ubiquitous eukaryotic protein calmodulin which itself has 4 calcium ion binding sites. When cytosolic Ca2+ ...

https://en.wikipedia.org/wiki/Phosphorylase_kinase

... including elongation factor 1A and the calcium sensing protein calmodulin. Many eukaryotic proteins are post-translationally ... The arginine methylation of proteins can either inhibit or promote protein-protein interactions depending on the type of ... GTP-binding proteins, nuclear lamins and certain protein kinases. Many of these proteins participate in cell signaling, and ... A well-characterized example of a methylation dependent protein-protein interaction is related to the selective methylation of ...

https://en.wikipedia.org/wiki/Protein_methylation

The increase in presynaptic calcium concentration activates calcium-calmodulin-dependent protein kinase (CaMK). CaMK ... The protein dense projections vary in size and shape depending on the type of synapse examined. One striking example of the ... The protein ELKS binds to the cell adhesion protein, β-neurexin, and other proteins within the complex such as Piccolo and ... that cause a local influx of calcium. The increase in calcium is detected by proteins in the active zone and forces vesicles ...

https://en.wikipedia.org/wiki/Active_zone

Barry FA, Gibbins JM (Apr 2002). "Protein kinase B is regulated in platelets by the collagen receptor glycoprotein VI". The ... Andrews RK, Suzuki-Inoue K, Shen Y, Tulasne D, Watson SP, Berndt MC (Jun 2002). "Interaction of calmodulin with the cytoplasmic ... Collagen fibers are the most thrombogenic macromolecular components of the extracellular matrix, with collagen types I, III, ... "Expression and function of the mouse collagen receptor glycoprotein VI is strictly dependent on its association with the ...

https://en.wikipedia.org/wiki/GPVI

... s are also modulated by G protein-coupled receptors and the adrenergic nervous system. Protein Kinase A ( ... "Switching off calcium-dependent inactivation in L-type calcium channels by an autoinhibitory domain". Proceedings of the ... As the pore opens and causes an influx of calcium, calcium binds to calmodulin and then interacts with the loop that connects ... which led to further categorization of the HVA channels into L-type, P-type, and N-type. L-type calcium channels were peptide ...

https://en.wikipedia.org/wiki/L-type_calcium_channel

Calcium-Calmodulin-Dependent Protein Kinase Type 4 100% * Cyclic AMP Response Element-Binding Protein 74% ... synaptic plasticity and cAMP response element-binding protein activation in Ca2+/calmodulin-dependent protein kinase type IV/Gr ... Immunosurveillance and therapy of multiple myeloma are CD226 dependent. Guillerey, C., De Andrade, L. F., Vuckovic, S., Miles, ... Inflammatory monocytes and NK cells play a crucial role in DNAM-1-dependent control of cytomegalovirus infection. Rovis, T. L. ...

https://profiles.wustl.edu/en/organisations/center-for-brain-immunology-glia-big/publications/?ordering=title&descending=true&page=13

https://en.wikipedia.org/wiki/CAMK4

SAK3 boosts calcium/calmodulin-dependent necessary protein kinase Two along with proteasome activity, therefore selling amyloid ... Many of us just lately launched a singular healing agent with regard to Advert therapy, the actual T-type calcium supplement ... Interrogating Tissue layer Proteins Construction as well as Fat. * Post author By admin ... These types of properties, along with its significant distinct floor, help make graphene appealing for any wide range of ...

https://dihydroartemisinininhibitor.com/

... interaction and modulation by calcium/calmodulin-dependent protein kinase II. J. Biol. Chem. ... Endothelin-1 and photoreleased diacylglycerol increase L-type Ca2+ current by activation of protein kinase C in rat ventricular ... interaction and modulation by calcium/calmodulin-dependent protein kinase II. J. Biol. Chem. ... Endothelin-1 and photoreleased diacylglycerol increase L-type Ca2+ current by activation of protein kinase C in rat ventricular ...

https://journals.biologists.com/jcs/article-split/119/16/3363/29059/Inositol-1-4-5-trisphosphate-supports-the

Calcium-dependent signaling pathways and heat shock protein expression regulate dimorphism in Paracoccidioides brasiliensis and ... with a heat shock protein 70-type profile, initiates the assembly of proteins necessary for mycelial growth. ... Yeast-form-specific genes identified in Histoplasma capsulatum function in calcium/calmodulin signaling pathways and sulphur ... albicans and other fungi transmit external stimuli through 2 major protein kinase cascades. These govern multiple functions, ...

https://wwwnc.cdc.gov/eid/article/11/4/04-1291_article

https://wwwnc.cdc.gov/eid/article/11/4/04-1291

In addition, antagonism of Ca2+/calmodulin-dependent kinase II (CaMKII) and protein kinase A (PKA) counteracted mangiferins ... Inhibition of glutamate release was blocked by removing extracellular calcium and by treatment with the vacuolar-type H+-ATPase ... Our data suggest that lappaconitine reduces Ca2+ influx through R-type Ca2+ channels, subsequently reducing the protein kinase ... R-type) channel blocker SNX-482 or the protein kinase A inhibitor H89. Nevertheless, the lappaconitine-mediated inhibition of ...

https://pesquisa.bvsalud.org/portal/?lang=pt&q=mh:4-Aminopiridina/farmacologia

Griffith, L. C., Wang, J., Zhong, Y., Wu, C. F., Greenspan, R. J. (1994) Calcium/calmodulin-dependent protein kinase II and ... organs, tissues, organelles, cell types and functions (66)*cell types and functions (66)*cell functions (66)*neural plasticity ... Lau, B. Y. B., Krishnan, K., Huang, Z. J., Shea, S. D. (January 2020) Maternal experience-dependent cortical plasticity in mice ... Debski, E. A., Cline, H. T., Constantine-Paton, M. (January 1990) Activity-dependent tuning and the NMDA receptor. J Neurobiol ...

http://repository.cshl.edu/view/subjects/neural=5Fplasticity.type.html

Calcium-Calmodulin-Dependent Protein Kinase Type 2 52% * Cyclic AMP Response Element-Binding Protein 52% ... Functional Diversification of SRSF Protein Kinase to Control Ubiquitin-Dependent Neurodevelopmental Signaling. Bustos, F., ... Ezh2-dependent H3K27me3 modification dynamically regulates vitamin D3-dependent epigenetic control of CYP24A1 gene expression ... Anti-neoplastic drugs increase caveolin-1-dependent migration, invasion and metastasis of cancer cells. Díaz-Valdivia, N. I., ...

https://researchers.unab.cl/en/persons/martin-alejandro-montecino-leonard-4/publications/?type=%2Fdk%2Fatira%2Fpure%2Fresearchoutput%2Fresearchoutputtypes%2Fcontributiontojournal%2Farticle

CASK: calcium/calmodulin dependent serine protein kinase. *CASQ2: calsequestrin 2. *CASR: calcium sensing receptor ... CNBP: CCHC-type zinc finger nucleic acid binding protein. *CNGA3: cyclic nucleotide gated channel subunit alpha 3 ... CDKN1C: cyclin dependent kinase inhibitor 1C. *CDKN1B: cyclin dependent kinase inhibitor 1B ...

https://medlineplus.gov/genetics/gene-c/

... spleen tyrosine kinase; CaMKIV, calcium/calmodulin-dependent kinase IV; CREB/CREM, cAMP response element (CRE) binding protein ... G. M. Kammer, I. U. Khan, and C. J. Malemud, "Deficient type I protein kinase A isozyme activity in systemic lupus ... First, high levels of antilymphocytic antibodies in patients with SLE activate calcium/calmodulin-dependent kinase IV (CaMKIV) ... the activities of pathways involving protein kinase C and p56-lymphocyte-specific protein tyrosine kinase (p56lck) have also ...

https://www.hindawi.com/journals/jir/2014/419029/

NCS1 regulates G protein-coupled receptor phosphorylation in a calcium-dependent manner and can substitute for calmodulin. NCS1 ... NCS1 takes part in neuron differentiation through inhibition of the activity of N-type voltage-gated calcium channel. ... NCS1 regulates GRK1 and substitutes for calmodulin. NCS1 stimulates PI4KB kinase activity and participates in long-term ... Neuronal Calcium Sensor 1, Frequenin-Like Ubiquitous Protein, Frequenin-Like Protein, Frequenin Homolog, FREQ, FLUP, Frequenin ...

https://www.prospecbio.com/ncs1_213_aa_human

Impairments of cerebellar-dependent motor control and learning are implicated in some forms of autism spectrum disorder (ASD). ... Moreover, developmental elimination of surplus climbing fibres-a model for activity-dependent synaptic pruning-is impaired. ... We find that in patDp/+ mice delay eyeblink conditioning-a form of cerebellum-dependent motor learning-is impaired, and observe ... protein kinase C (PKC)39 and calcium/calmodulin-dependent kinase II (CaMKII)40. To examine whether the elimination of surplus ...

https://www.nature.com/articles/ncomms6586?error=cookies_not_supported&code=eacd88b6-4ae7-4fdd-9ebe-7d66970f699d

TYPE 1; CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE TYPE 2; CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE TYPE 4; and PROTEIN ... HN - 2008(1995) BX - Calcium-Calmodulin-Dependent Kinase Kinase MH - Calcium-Calmodulin-Dependent Protein Kinase Type 1 UI - ... Calcium-Calmodulin-Dependent Protein Kinase Type 3 BX - Calmodulin-Dependent Protein Kinase III MH - Cyclic AMP-Dependent ... CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE KINASE. HN - 2008(1991) BX - Calmodulin-Dependent Protein Kinase IV MH - Elongation ...

https://decs2013.bvsalud.org/I/dcsnew2008.txt

https://decs2012.bvsalud.org/I/dcsnew2008.txt

https://decs2016.bvsalud.org/I/dcsnew2008.txt

https://decs2019.bvsalud.org/I/dcsnew2008.txt

Calcium-/Calmodulin-Dependent Protein Kinase II (CaMKII) Inhibition Induces Learning and Memory Impairment and Apoptosis. Wang ... Article type * Books and Documents * Clinical Trial * Meta-Analysis * Randomized Controlled Trial ... doi: 10.1038/s41388-021-01920-4. Epub 2022 Feb 16. Oncogene. 2022. PMID: 35173310 ...

https://pubmed.ncbi.nlm.nih.gov/?cmd=search&term=Min+D%5Bau%5D&dispmax=50

... by cAMP-dependent proteins Pfn1 kinase A (PKA) [7]. Phosphorylation in response to a hormonal cause has also been proven to ... extracellular calcium mineral influx, calmodulin, as well as the phosphorylation of two threonine residues (Thr 157 and Thr 239 ... by cAMP-dependent protein kinase A (PKA) [7]. Phosphorylation in response to a hormonal result in has also been shown to ... by cAMP-dependent protein kinase A (PKA) [7]. Phosphorylation in response to a hormonal trigger has also been shown to mediate ...

http://idplink.net/2022/11/27/the-structure-of-wild-type-aqp5-is-shown-in-blue-for-comparison/

Signal transduction by G-proteins, rho-kinase and protein phosphatase to smooth muscle and non-muscle myosin II. J Physiol. ... Huwentoxin-I, a N-type calcium channel blocker isolated from the venom of the Chinese tarantula Ornithoctonus huwena, has ... which binds to calmodulin leading to change in its conformation, exposing sites of interaction with myosin-light-chain kinase ( ... The latter activates cGMP-dependent ion channels, reducing cytosolic calcium via sequestration, extrusion and opening of ...

https://www.scielo.br/j/jvatitd/a/HcCPwsqnL486NgyLCZRZfpm/?format=html&lang=en

Dopamine D1-dependent trafficking of striatal N-methyl-D-aspartate glutamate receptors requires Fyn protein tyrosine kinase but ... Genetic reduction of chronic muscle pain in mice lacking calcium/calmodulin-stimulated adenylyl cyclases. Vadakkan, K.I., Wang ... However, the mRNA levels of the NMDA-R subunits, determined by quantitative RT-PCR, were the same as in wild-type mice [36]. ... Thus, the NMDA-R protein level is regulated by the Reelin protein level in a Fyn-dependent manner in the mouse brain [36]. ...

https://www.wikigenes.org/e/gene/e/14810.html

1,2,6-thiadiazinones as novel narrow spectrum calcium/calmodulin-dependent protein kinase kinase 2 (CaMKK2) inhibitors DOI: ... Type: Journal Paper Journal: Molecules , VOL 23 State: Published (Approved) Published: May 2018 Diamond Proposal Number(s): ... Journal Keywords: thiadiazinone; hinge binder; kinase inhibitor design; kinase water network; CaMKK2 ... can function as a chemotype for the design of ATP-competitive kinase inhibitors. Using insights from a co-crystal structure of ...

https://publications.diamond.ac.uk/pubman/viewpublication?publicationId=9378

... subunit of the type 1 cAMP-dependent protein kinase as an inhibitor and substrate of the cGMP-dependent protein kinase. J Biol ... 1992) Role of cGMP and cGMP-dependent protein kinase in nitrovasodilator inhibition of agonist-evoked calcium elevation in ... Another possibility is that PKG may phosphorylate CREB indirectly via some other kinase such Ca2+/calmodulin-dependent kinase ( ... 1981) Effect of phosphorylation on the regulatory subunit of the type 1 cAMP-dependent protein kinase. J Biol Chem 256:4536- ...

https://www.jneurosci.org/content/19/23/10250

Name: calcium/calmodulin-dependent protein kinase II alpha. Synonyms: alpha-CaMKII. Type: Gene ... Synonyms: Gnas1, Gs-alpha, Gs alpha, G alpha s, Nesp55, P2, P3, P1, neuroendocrine-specific Golgi protein p55 isoform 1, ... When maintaining a live colony, heterozygous mice may be bred together, bred with wild-type siblings, or bred with C57BL/6J ... Name: transformation/transcription domain-associated protein. Synonyms: transactivation/transformation-domain associated ...

https://www.mmrrc.org/catalog/sds.php?mmrrc_id=39783

OHare HM An Aspartate-Specific Solute-Binding Protein Regulates Protein Kinase G Activity to Control Glutamate Metabolism in ... The Structural Basis of Calcium-Dependent Inactivation of the Transient Receptor Potential Vanilloid 5 Channel. Biochemistry. ... Lipid-Protein Interactions in Niemann-Pick Type C Disease: Insights from Molecular Modeling. International Journal of Molecular ... A Novel Mechanism for Calmodulin-Dependent Inactivation of Transient Receptor Potential Vanilloid 6. Biochemistry 57(18):2611- ...

https://le.ac.uk/research/institutes/structural-chemical-biology/publications

This plasmid contains the mouse calcium/calmodulin-dependent kinase II alpha subunit promoter. ... Tag / Fusion Protein *mCherry (C terminal on insert). Cloning Information * Cloning method Restriction Enzyme ... Vector type. Mammalian Expression, AAV Growth in Bacteria. * Bacterial Resistance(s). Ampicillin, 100 μg/mL ... Retrograde functionality is dependent on high viral titers. Addgene recommends not diluting your AAV preps prior to use. ...

https://www.addgene.org/26975/

The presence of auto-antibodies that target synaptic machinery proteins was documented recently in immune-mediated cerebellar ... P/Q-type)-mediated increase in [Ca2+]i [62]. The increase in [Ca2+]i level activates Ca2+/calmodulin-dependent protein kinase ... Graus F, Lang B, Pozo-Rosich P, Saiz A, Casamitjana R, Vincent A. P/Q type calcium-channel antibodies in paraneoplastic ... P/Q type Ca2+ voltage-gated channel; PLC, phospholipase C; PKC, protein kinase C; IP3, inositol triphosphate; GRIP, glutamate ...

https://link.springer.com/article/10.1007/s12311-021-01359-z

Nishizawa Y.Estrogen induces a rapid increase of calcium-calmodulin-dependent protein kinase II activity in the hippocampus. ... Moriguchi S., Shioda N., Yamamoto Y., Tagashira H., Fukunaga K.The T-type voltage-gated calcium channel as a molecular target ... Fukunaga K., Soderling T.R., Miyamoto E.Activation of Ca2+/calmodulin-dependent protein kinase II and protein kinase C by ... Fukunaga K., Horikawa K., Shibata S., Takeuchi Y., Miyamoto E.Ca2+/ calmodulin-dependent protein kinase II-dependent long-term ...

https://complete.bioone.org/journals/environmental-health-insights/volume-7/issue-1/EHI.S10346/Influence-of-Maternal-Exposure-to-2378-Tetrachlorodibenzo-p-dioxin-on/10.1177/EHI.S10346.full

A growing family of proteins is regulated by protein kinase C and calmodulin through IQ domains, a regulatory motif originally ... Protein. Disease. Unconventional myosin-VIIa (Q13402) (SMART). OMIM:276903: Usher syndrome, type 1B ; Deafness, autosomal ... Calmodulin (CaM) is recognized as a major calcium sensor and orchestrator of regulatory events through its interaction with a ... A modified version of the IQ motif as a consensus for Ca2+-independent binding and two related motifs for Ca2+-dependent ...

https://smart.embl.de/smart/do_annotation.pl?DOMAIN=IQ&START=765&END=787&E_VALUE=3.65e-4&TYPE=SMART&BLAST=KLRAACIRIQKTIRGWLLRKRYL

1995). "Phosphorylation and activation of Ca2+-calmodulin-dependent protein kinase IV by Ca2+-calmodulin-dependent protein kinase Ia kinase. (wikipedia.org)
A unique phosphorylation-dependent mechanism for the activation of Ca2+/calmodulin-dependent protein kinase type IV/GR". J. Biol. (wikipedia.org)
4-AP-elicited PKA and synapsin I or synaptosomal-associated protein of 25 kDa (SNAP-25) phosphorylation at PKA-specific residues were also attenuated by cynarin. (bvsalud.org)
Our data indicate that cynarin, through the suppression of P/Q-type Ca2+ channels, inhibits PKA activation and attenuates synapsin I and SNAP-25 phosphorylation at PKA-specific residues, thus decreasing synaptic vesicle availability and contributing to glutamate release inhibition in cerebral cortex terminals. (bvsalud.org)
Mangiferin also decreased the phosphorylation of CaMKII, PKA, and synapsin I elicited by 4-aminopyridine treatment. (bvsalud.org)
NCS1 regulates G protein-coupled receptor phosphorylation in a calcium-dependent manner and can substitute for calmodulin. (prospecbio.com)
AQP5 plasma membrane large quantity in transfected HEK293 cells is definitely rapidly and reversibly Chlorpheniramine maleate controlled by at least three self-employed mechanisms including phosphorylation at Ser156, protein kinase A activity and extracellular tonicity. (idplink.net)
Constructions of gated AQPs have exposed the molecular details of AQP gating by phosphorylation, pH and Ca2+ for the spinach aquaporin SoPIP2;1 [4] and mechanosensitivity for the candida aquaporin AQY1 [5]. (idplink.net)
The best-characterised example of this type of rules is definitely that of human being AQP2 in the kidney: AQP2 large quantity in the apical membrane is dependent on vasopressin-activated phosphorylation of a carboxy-terminal serine residue (Ser 256) by cAMP-dependent protein kinase A (PKA) [7]. (idplink.net)
exposure to hypotonic conditions resulted in rapid recruitment to the cell surface via a mechanism dependent on transient receptor potential channels, extracellular calcium influx, calmodulin, and the phosphorylation of two threonine residues (Thr 157 and Thr 239) of AQP1 [13]. (idplink.net)
We furthermore demonstrate that p110δ is phosphorylated at residues Y524 and S1039 and that phosphorylation requires an intact binding site for PI3-kinase in c-Kit/D816V. (ku.dk)
PKC phosphorylation of these proteins also inhibits their binding to RNA in vitro. (embl.de)
A CALMODULIN-dependent enzyme that catalyzes the phosphorylation of proteins. (bvsalud.org)

The product of this gene belongs to the serine/threonine protein kinase cluster, and to the Ca2+/calmodulin-dependent protein kinase (CAMK) group. (wikipedia.org)
This enzyme is a multifunctional serine/threonine protein kinase with limited tissue distribution, that has been implicated in transcriptional regulation in lymphocytes, neurons, and male germ cells. (wikipedia.org)

This plasmid contains the mouse calcium/calmodulin-dependent kinase II alpha subunit promoter. (addgene.org)
The NR2B subunit of the NMDA receptor interacts with several prominent proteins in the postsynaptic density, including calcium/calmodulin-dependent protein kinase II (CaMKII). (caltech.edu)

Calcium/calmodulin-dependent protein kinase II (CaMKII) - the main protein of the postsynaptic density - is a Ca 2 + /calmodulin-activated dodecameric enzyme. (eunaonascideoculos.com)

Inhibition of glutamate release was blocked by removing extracellular calcium and by treatment with the vacuolar-type H+-ATPase inhibitor bafilomycin A1, which prevents the uptake and storage of glutamate in vesicles. (bvsalud.org)

Calcium/calmodulin-dependent protein kinase type IV is an enzyme that in humans is encoded by the CAMK4 gene. (wikipedia.org)
This enzyme is also sometimes dependent on CALCIUM. (bvsalud.org)

Molecular docking also revealed that cynarin formed a hydrogen bond with the P/Q-type Ca2+ channel, indicating a mechanism of action involving Ca2+ influx inhibition. (bvsalud.org)
NCS1 takes part in neuron differentiation through inhibition of the activity of N-type voltage-gated calcium channel. (prospecbio.com)
Furthermore, inhibition of the lipid kinase activity of PI3-kinase led only to a slight inhibition of cell survival. (ku.dk)

Molecular and Cellular Neuroscience, 25 (4). (cshl.edu)
Acts as a 'third messenger' substrate of protein kinase C-mediated molecular cascades during synaptic development and remodeling. (embl.de)

Neuronal Calcium Sensor 1 213 a.a. (prospecbio.com)
NCS1 is part of the neuronal calcium sensor gene family, which encode calcium-binding proteins expressed primarily in neurons. (prospecbio.com)

The prooncoprotein EWS binds calmodulin and is phosphorylated by protein kinase C through an IQ domain. (embl.de)
Here we report that EWS, a nuclear RNA-binding prooncoprotein, contains an IQ domain, is phosphorylated by protein kinase C, and interacts with calmodulin. (embl.de)

A further chapter discusses how surface membrane G-protein receptors in C. albicans and other fungi transmit external stimuli through 2 major protein kinase cascades. (cdc.gov)

A cell-penetrant peptide blocking C9ORF72-repeat RNA nuclear export reduces the neurotoxic effects of dipeptide repeat proteins. (le.ac.uk)

The autoantigens include glutamic acid decarboxylase 65 (GAD65), voltage-gated Ca 2+ channel (VGCC), metabotropic glutamate receptor type 1 (mGluR1), and glutamate receptor delta (GluRdelta). (springer.com)
To determine the function of these interactions, we derived transgenic mice expressing a ligand-activated carboxy-terminal NR2B fragment (cNR2B) by fusing this fragment to a tamoxifen (TAM)-dependent mutant of the estrogen receptor ligand-binding domain LBD(G521R). (caltech.edu)

NCS1 regulates GRK1 and substitutes for calmodulin. (prospecbio.com)

The presence of auto-antibodies that target synaptic machinery proteins was documented recently in immune-mediated cerebellar ataxias. (springer.com)

These data suggest that PKC may regulate interactions of EWS and other RNA-binding proteins with their RNA targets and that IQ domains may provide a regulatory link between Ca2+ signal transduction pathways and RNA processing. (embl.de)
Calmodulin (CaM) is recognized as a major calcium sensor and orchestrator of regulatory events through its interaction with a diverse group of cellular proteins. (embl.de)

Although ventricular cardiomyocytes express inositol 1,4,5-trisphosphate [Ins(1,4,5) P 3 ] receptors, it is unclear how these Ca 2+ channels contribute to the effects of Gq-coupled agonists. (biologists.com)
The endothelin-1-mediated spontaneous Ca 2+ transients were abolished by application of 2-aminoethoxydiphenyl borate (2-APB), an antagonist of Ins(1,4,5) P 3 receptors. (biologists.com)
Among these diverse features, it should be acknowledged that auto-antibodies toward glutamate receptors, GABA receptors, and K + channel-related proteins are preferentially found in autoimmune limbic encephalitis but not in IMCAs [ 10 ] (Table 1 ). (springer.com)

Intro The flux of water across biological Chlorpheniramine maleate membranes is definitely facilitated by transmembrane protein channels called aquaporins (AQPs). (idplink.net)

Yeast-form-specific genes identified in Histoplasma capsulatum function in calcium/calmodulin signaling pathways and sulphur metabolism. (cdc.gov)

Early steps in this transition are complex, with at least 2 signaling pathways identified: 1 stops yeast growth and another, with a heat shock protein 70-type profile, initiates the assembly of proteins necessary for mycelial growth. (cdc.gov)
Calcium-dependent signaling pathways and heat shock protein expression regulate dimorphism in Paracoccidioides brasiliensis and have broad implications for other pathogens. (cdc.gov)

Sequence motifs for calmodulin recognition. (embl.de)
Although considerable sequence diversity is observed among the different binding regions, these three classes of recognition motifs exist for many of the known CaM binding proteins. (embl.de)

NCS1 stimulates PI4KB kinase activity and participates in long-term synaptic plasticity through its interaction with PICK1. (prospecbio.com)

Short calmodulin-binding motif containing conserved Ile and Gln residues. (embl.de)
A modified version of the IQ motif as a consensus for Ca2+-independent binding and two related motifs for Ca2+-dependent binding, termed 18-14 and 1-5-10 based on the position of conserved hydrophobic residues, are proposed. (embl.de)

Ras GTPase-activating-like protein IQGAP1. (embl.de)
IQGAP1 contains 4 IQ motifs. (embl.de)

We find that in patDp/+ mice delay eyeblink conditioning-a form of cerebellum-dependent motor learning-is impaired, and observe deregulation of a putative cellular mechanism for motor learning, long-term depression (LTD) at parallel fibre-Purkinje cell synapses. (nature.com)

AQP5 translocation offers been shown to be affected by cAMP inside a PKA-dependent manner, with exposure to elevated intracellular cAMP levels causing a short-term (moments) decrease in AQP5 membrane large quantity whereas long-term (8 hours) exposure increased total AQP5 protein [15]. (idplink.net)

In humans, thirteen members of the AQP family (AQP0-12), with delicate functional differences, are indicated with different tissue-specific and time-dependent profiles [3]. (idplink.net)
Heart relaxation also stands out as an active process, dependent on the energetic output and on specific ion and enzymatic actions, with the role of sodium channel being outstanding in the functional process. (bvsalud.org)

The purpose of this study was to evaluate the effect of cynarin, a caffeoylquinic acid derivative in artichoke, on glutamate release elicited by 4-aminopyridine (4-AP) in rat cortical nerve terminals (synaptosomes). (bvsalud.org)
We observed that cynarin decreased 4-aminopyridine-elicited glutamate release, which was prevented by the removal of external free Ca2+ with ethylene glycol bis (ß-aminoethyl ether)-N,N,N,N-tetraacetic acid (EGTA) or the blockade of P/Q-type calcium channels with ω-agatoxin IVA. (bvsalud.org)
Additionally, the inhibitory effect of cynarin on glutamate release is associated with a change in the available synaptic vesicles, as cynarin decreased 4-AP-elicited FM1-43 release or hypertonic sucrose-evoked glutamate release from synaptosomes. (bvsalud.org)
We observed that mangiferin produced a concentration-dependent reduction in the release of glutamate elicited by 4-aminopyridine with an IC50 value of 25 µM. (bvsalud.org)
In addition, antagonism of Ca2+/calmodulin-dependent kinase II (CaMKII) and protein kinase A (PKA) counteracted mangiferin's effect on glutamate release. (bvsalud.org)

These types of well-designed versions https://www.selleckchem.com/products/selonsertib-gs-4997.html included the effects involving GWAS-identified steer SNPs in CCR6/FGFR1OP. (dihydroartemisinininhibitor.com)

However, mutation of this binding site had little effect on the PI3-kinase activity in the cells, suggesting that c-Kit/D816V-mediated cell survival is dependent on PI3-kinase but not its kinase activity. (ku.dk)

lt;div class="textblock">PI3-kinase has a crucial role in transformation mediated by the oncogenic c-Kit mutant D816V. (ku.dk)
Knockdown of the predominant PI3-kinase isoform p110δ in c-Kit/D816V-expressing Ba/F3 cells led to reduced cell transformation both in vitro and in vivo without affecting the overall PI3-kinase activity. (ku.dk)
This suggests that p110δ has a lipid-kinase-independent role in c-Kit/D816V-mediated cell transformation. (ku.dk)
Taken together, our results demonstrate an important lipid-kinase-independent role of p110δ in c-Kit/D816V-mediated cell transformation. (ku.dk)

Activation of the LBD(G521R)-cNR2B transgenic protein in mice leads to the disruption of CaMKII/NR2B interactions at synapses. (caltech.edu)

Immunohistochemistry showed increased expression involving CCR6 protein inside the livers regarding people using PBC in comparison to that relating to a non-diseased handle. (dihydroartemisinininhibitor.com)

Lead absorption is augmented in the presence of iron, zinc, and calcium deficiency. (medscape.com)

Because CaM can bind with high affinity to a relatively small alpha-helical region of many proteins, success in clearly defining the essential elements of CaM binding motifs seems feasible and should provide a means of identifying CaM binding proteins. (embl.de)
Three recognition motifs for CaM interaction are discussed in the context of experimental investigations of a variety of CaM target proteins. (embl.de)

Sperm surface protein Sp17. (embl.de)

Moreover, developmental elimination of surplus climbing fibres-a model for activity-dependent synaptic pruning-is impaired. (nature.com)
Using insights from a co-crystal structure of a 3,5-bis(arylamino)-4H-1,2,6-thiadiazin-4-one bound to calcium/calmodulin-dependent protein kinase kinase 2 (CaMKK2), several analogues were identified with micromolar activity through targeted displacement of bound water molecules in the active site. (diamond.ac.uk)

We demonstrate for the first time that 4H-1,2,6-thiadiazin-4-one (TDZ) can function as a chemotype for the design of ATP-competitive kinase inhibitors. (diamond.ac.uk)
Many investigations have focused on defining the region of interaction between CaM and its cellular targets and the action of CaM on target protein function. (embl.de)

Anatomy6

Organisms5

Chemicals and Drugs63

Analytical, Diagnostic and Therapeutic Techniques and Equipment4

Phenomena and Processes18

Information Science3

Differential effects of a calcineurin inhibitor on glutamate-induced phosphorylation of Ca2+/calmodulin-dependent protein kinases in cultured rat hippocampal neurons. (1/181)

Inhibition of the Ca2+/calmodulin-dependent protein kinase I cascade by cAMP-dependent protein kinase. (2/181)

Substrate recognition by Ca2+/Calmodulin-dependent protein kinase kinase. Role of the arg-pro-rich insert domain. (3/181)

The retinoblastoma susceptibility gene product/Sp1 signalling pathway is modulated by Ca2+/calmodulin kinases II and IV activity. (4/181)

A late phase of cerebellar long-term depression requires activation of CaMKIV and CREB. (5/181)

Ca(2+)-dependent gene expression mediated by MEF2 transcription factors. (6/181)

Activation of orphan receptor-mediated transcription by Ca(2+)/calmodulin-dependent protein kinase IV. (7/181)

Ca(2+)/calmodulin-dependent protein kinase IV is expressed in spermatids and targeted to chromatin and the nuclear matrix. (8/181)

Calcium-Calmodulin-Dependent Protein Kinase Type 2

Calcium-Calmodulin-Dependent Protein Kinases

Calmodulin

Cyclic GMP-Dependent Protein Kinase Type I

Cyclic GMP-Dependent Protein Kinase Type II

Calcium-Calmodulin-Dependent Protein Kinase Type 4

Protein Kinases

Phosphorylation

Cyclic GMP-Dependent Protein Kinases

Calcium

Cyclic AMP-Dependent Protein Kinase Type II

Protein Kinase C

Cyclic AMP-Dependent Protein Kinases

Calcium-Calmodulin-Dependent Protein Kinase Type 1

Benzylamines

Enzyme Activation

Cyclic AMP

Molecular Sequence Data

Isoenzymes

Calcium Signaling

Amino Acid Sequence

Cyclic AMP-Dependent Protein Kinase RIalpha Subunit

Kinetics

Signal Transduction

Protein Kinase Inhibitors

Cyclic AMP-Dependent Protein Kinase Type I

Cyclic GMP

Cells, Cultured

Protein-Serine-Threonine Kinases

Protein Binding

Enzyme Inhibitors

Cell Line

Sporothrix

Calmodulin-Binding Proteins

Phosphotransferases (Alcohol Group Acceptor)

Binding Sites

Mitogen-Activated Protein Kinases

Paramecium tetraurelia

Sulfonamides

Calcium-Binding Proteins

1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine

Trifluoperazine

MAP Kinase Signaling System

Cattle

Myosin-Light-Chain Kinase

Phosphatidylinositol 3-Kinases

p38 Mitogen-Activated Protein Kinases

Base Sequence

eIF-2 Kinase

Protein Structure, Tertiary

Tetradecanoylphorbol Acetate

Protein Kinase C-alpha

Substrate Specificity

Pyruvate Kinase

Mitogen-Activated Protein Kinase 1

Calcium Channels

Death-Associated Protein Kinases

Cyclic AMP-Dependent Protein Kinase Catalytic Subunits

Mutation

Sequence Homology, Amino Acid

Rats, Sprague-Dawley

Blotting, Western

Transfection

Mycelium

Phosphoprotein Phosphatases

Mitogen-Activated Protein Kinase Kinases

Mitogen-Activated Protein Kinase 3

Recombinant Proteins

Protein Kinase C-delta

Isoquinolines

Adenosine Triphosphate

JNK Mitogen-Activated Protein Kinases

Peptide T

Serine

Phosphoproteins

Nucleotides, Cyclic

Egtazic Acid

Molecular Weight

AMP-Activated Protein Kinases

RNA, Messenger