Phosphatidylinositols in which one or more alcohol group of the inositol has been substituted with a phosphate group.
A group of enzymes that transfers a phosphate group onto an alcohol group acceptor. EC 2.7.1.
A phosphoinositide present in all eukaryotic cells, particularly in the plasma membrane. It is the major substrate for receptor-stimulated phosphoinositidase C, with the consequent formation of inositol 1,4,5-triphosphate and diacylglycerol, and probably also for receptor-stimulated inositol phospholipid 3-kinase. (Kendrew, The Encyclopedia of Molecular Biology, 1994)
Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to the hexahydroxy alcohol, myo-inositol. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid, myo-inositol, and 2 moles of fatty acids.
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.
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 235-kDa cytoplasmic protein that is also found in platelets. It has been localized to regions of cell-substrate adhesion. It binds to INTEGRINS; VINCULIN; and ACTINS and appears to participate in generating a transmembrane connection between the extracellular matrix and the cytoskeleton.
Inorganic salts of phosphoric acid.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
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.
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.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
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.
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.
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.
Established cell cultures that have the potential to propagate indefinitely.
Chromones are a class of chemical compounds that contain a benzopyran-4-one core structure, which are found in various natural and synthetic substances, including some medications used to treat asthma and allergies.
Derivatives of the steroid androstane having two double bonds at any site in any of the rings.
A phosphatidylinositol 3-kinase that catalyzes the conversion of 1-phosphatidylinositol into 1-phosphatidylinositol 3-phosphate.
Morpholines are organic compounds containing a morpholine ring, which is a saturated six-membered heterocycle made up of four carbon atoms and two oxygen atoms (OCC1CCO), often used as functional groups in pharmaceuticals, agrochemicals, and materials science due to their versatile chemical properties.
'Sugar phosphates' are organic compounds that consist of a sugar molecule linked to one or more phosphate groups, playing crucial roles in biochemical processes such as energy transfer and nucleic acid metabolism.
A protein-serine-threonine kinase that is activated by PHOSPHORYLATION in response to GROWTH FACTORS or INSULIN. It plays a major role in cell metabolism, growth, and survival as a core component of SIGNAL TRANSDUCTION. Three isoforms have been described in mammalian cells.
Phosphoric acid esters of inositol. They include mono- and polyphosphoric acid esters, with the exception of inositol hexaphosphate which is PHYTIC ACID.
Calcium salts of phosphoric acid. These compounds are frequently used as calcium supplements.
An ester of glucose with phosphoric acid, made in the course of glucose metabolism by mammalian and other cells. It is a normal constituent of resting muscle and probably is in constant equilibrium with fructose-6-phosphate. (Stedman, 26th ed)
Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.
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 isomer of glucose that has traditionally been considered to be a B vitamin although it has an uncertain status as a vitamin and a deficiency syndrome has not been identified in man. (From Martindale, The Extra Pharmacopoeia, 30th ed, p1379) Inositol phospholipids are important in signal transduction.
A group of hydrolases which catalyze the hydrolysis of monophosphoric esters with the production of one mole of orthophosphate. EC 3.1.3.
A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7.
Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.
A subclass of phospholipases that hydrolyze the phosphoester bond found in the third position of GLYCEROPHOSPHOLIPIDS. Although the singular term phospholipase C specifically refers to an enzyme that catalyzes the hydrolysis of PHOSPHATIDYLCHOLINE (EC 3.1.4.3), it is commonly used in the literature to refer to broad variety of enzymes that specifically catalyze the hydrolysis of PHOSPHATIDYLINOSITOLS.
An enzyme that catalyzes the formation of PHOSPHATIDYLINOSITOL and CMP from CDP-DIACYLGLYCEROL and MYOINOSITOL.
The rate dynamics in chemical or physical systems.
A phosphorus-oxygen lyase found primarily in BACTERIA. The enzyme catalyzes the cleavage of a phosphoester linkage in 1-phosphatidyl-1D-myo-inositol to form 1D-myo-inositol 1,2-cyclic phosphate and diacylglycerol. The enzyme was formerly classified as a phosphoric diester hydrolase (EC 3.1.4.10) and is often referred to as a TYPE C PHOSPHOLIPASES. However it is now known that a cyclic phosphate is the final product of this enzyme and that water does not enter into the reaction.
A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.
Lipids containing one or more phosphate groups, particularly those derived from either glycerol (phosphoglycerides see GLYCEROPHOSPHOLIPIDS) or sphingosine (SPHINGOLIPIDS). They are polar lipids that are of great importance for the structure and function of cell membranes and are the most abundant of membrane lipids, although not stored in large amounts in the system.
Products of proto-oncogenes. Normally they do not have oncogenic or transforming properties, but are involved in the regulation or differentiation of cell growth. They often have protein kinase activity.
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.
Fatty acid derivatives of glycerophosphates. They are composed of glycerol bound in ester linkage with 1 mole of phosphoric acid at the terminal 3-hydroxyl group and with 2 moles of fatty acids at the other two hydroxyl groups.
An aldotriose which is an important intermediate in glycolysis and in tryptophan biosynthesis.
Phosphoproteins are proteins that have been post-translationally modified with the addition of a phosphate group, usually on serine, threonine or tyrosine residues, which can play a role in their regulation, function, interaction with other molecules, and localization within the cell.
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.
An oxidative decarboxylation process that converts GLUCOSE-6-PHOSPHATE to D-ribose-5-phosphate via 6-phosphogluconate. The pentose product is used in the biosynthesis of NUCLEIC ACIDS. The generated energy is stored in the form of NADPH. This pathway is prominent in tissues which are active in the synthesis of FATTY ACIDS and STEROIDS.
A ubiquitous family of proteins that transport PHOSPHOLIPIDS such as PHOSPHATIDYLINOSITOL and PHOSPHATIDYLCHOLINE between membranes. They play an important role in phospholipid metabolism during vesicular transport and SIGNAL TRANSDUCTION.
Glucose-6-Phosphate Dehydrogenase (G6PD) is an enzyme that plays a critical role in the pentose phosphate pathway, catalyzing the oxidation of glucose-6-phosphate to 6-phosphoglucono-δ-lactone while reducing nicotinamide adenine dinucleotide phosphate (NADP+) to nicotinamide adenine dinucleotide phosphate hydrogen (NADPH), thereby protecting cells from oxidative damage and maintaining redox balance.
Derivatives of PHOSPHATIDIC ACIDS that lack one of its fatty acyl chains due to its hydrolytic removal.
An important intermediate in lipid biosynthesis and in glycolysis.
A class of enzymes that transfers substituted phosphate groups. EC 2.7.8.
Membrane proteins that are involved in the active transport of phosphate.
A structurally-related group of signaling proteins that are phosphorylated by the INSULIN RECEPTOR PROTEIN-TYROSINE KINASE. The proteins share in common an N-terminal PHOSPHOLIPID-binding domain, a phosphotyrosine-binding domain that interacts with the phosphorylated INSULIN RECEPTOR, and a C-terminal TYROSINE-rich domain. Upon tyrosine phosphorylation insulin receptor substrate proteins interact with specific SH2 DOMAIN-containing proteins that are involved in insulin receptor signaling.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
The process of cleaving a chemical compound by the addition of a molecule of water.
This is the active form of VITAMIN B 6 serving as a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate (PYRIDOXAMINE).
A phosphatidylinositol 3-kinase subclass that includes enzymes whose specificity is limited to 1-phosphatidylinositol. Members of this class play a role in vesicular transport and in the regulation of TOR KINASES.
An amino alcohol with a long unsaturated hydrocarbon chain. Sphingosine and its derivative sphinganine are the major bases of the sphingolipids in mammals. (Dorland, 28th ed)
A type C phospholipase with specificity towards PHOSPHATIDYLINOSITOLS that contain INOSITOL 1,4,5-TRISPHOSPHATE. Many of the enzymes listed under this classification are involved in intracellular signaling.
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.
An aldose-ketose isomerase that catalyzes the reversible interconversion of glucose 6-phosphate and fructose 6-phosphate. In prokaryotic and eukaryotic organisms it plays an essential role in glycolytic and gluconeogenic pathways. In mammalian systems the enzyme is found in the cytoplasm and as a secreted protein. This secreted form of glucose-6-phosphate isomerase has been referred to as autocrine motility factor or neuroleukin, and acts as a cytokine which binds to the AUTOCRINE MOTILITY FACTOR RECEPTOR. Deficiency of the enzyme in humans is an autosomal recessive trait, which results in CONGENITAL NONSPHEROCYTIC HEMOLYTIC ANEMIA.
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.
A 51-amino acid pancreatic hormone that plays a major role in the regulation of glucose metabolism, directly by suppressing endogenous glucose production (GLYCOGENOLYSIS; GLUCONEOGENESIS) and indirectly by suppressing GLUCAGON secretion and LIPOLYSIS. Native insulin is a globular protein comprised of a zinc-coordinated hexamer. Each insulin monomer containing two chains, A (21 residues) and B (30 residues), linked by two disulfide bonds. Insulin is used as a drug to control insulin-dependent diabetes mellitus (DIABETES MELLITUS, TYPE 1).
A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.
A phosphatidylinositol 3-kinase subclass that includes enzymes formed through the association of a p110gamma catalytic subunit and one of the three regulatory subunits of 84, 87, and 101 kDa in size. This subclass of enzymes is a downstream target of G PROTEIN-COUPLED RECEPTORS.
Any salt or ester of glycerophosphoric acid.
'Glucosephosphates' are organic compounds resulting from the reaction of glucose with phosphoric acid, playing crucial roles in various metabolic processes, such as energy transfer and storage within cells.
An enzyme that transfers acyl groups from acyl-CoA to glycerol-3-phosphate to form monoglyceride phosphates. It acts only with CoA derivatives of fatty acids of chain length above C-10. Also forms diglyceride phosphates. EC 2.3.1.15.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
A lipid phosphatase that acts on phosphatidylinositol-3,4,5-trisphosphate to regulate various SIGNAL TRANSDUCTION PATHWAYS. It modulates CELL GROWTH PROCESSES; CELL MIGRATION; and APOPTOSIS. Mutations in PTEN are associated with COWDEN DISEASE and PROTEUS SYNDROME as well as NEOPLASTIC CELL TRANSFORMATION.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
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.

Vac1p coordinates Rab and phosphatidylinositol 3-kinase signaling in Vps45p-dependent vesicle docking/fusion at the endosome. (1/1545)

The vacuolar protein sorting (VPS) pathway of Saccharomyces cerevisiae mediates transport of vacuolar protein precursors from the late Golgi to the lysosome-like vacuole. Sorting of some vacuolar proteins occurs via a prevacuolar endosomal compartment and mutations in a subset of VPS genes (the class D VPS genes) interfere with the Golgi-to-endosome transport step. Several of the encoded proteins, including Pep12p/Vps6p (an endosomal target (t) SNARE) and Vps45p (a Sec1p homologue), bind each other directly [1]. Another of these proteins, Vac1p/Pep7p/Vps19p, associates with Pep12p and binds phosphatidylinositol 3-phosphate (PI(3)P), the product of the Vps34 phosphatidylinositol 3-kinase (PI 3-kinase) [1] [2]. Here, we demonstrate that Vac1p genetically and physically interacts with the activated, GTP-bound form of Vps21p, a Rab GTPase that functions in Golgi-to-endosome transport, and with Vps45p. These results implicate Vac1p as an effector of Vps21p and as a novel Sec1p-family-binding protein. We suggest that Vac1p functions as a multivalent adaptor protein that ensures the high fidelity of vesicle docking and fusion by integrating both phosphoinositide (Vps34p) and GTPase (Vps21p) signals, which are essential for Pep12p- and Vps45p-dependent targeting of Golgi-derived vesicles to the prevacuolar endosome.  (+info)

The endosome fusion regulator early-endosomal autoantigen 1 (EEA1) is a dimer. (2/1545)

EEA1, an early-endosomal protein originally identified as an autoantigen, is essential for endocytic membrane fusion. It interacts with early endosomes via binding to the membrane lipid phosphatidylinositol 3-phosphate (PtdIns3P) and the active form of the small GTPase Rab5. Most of the EEA1 sequence contains heptad repeats characteristic of proteins involved in coiled-coil protein-protein interactions. Here we have investigated the ability of EEA1 to self-interact. Crosslinking of cytosolic and recombinant EEA1 resulted in the disappearance of the 180-kDa monomer in SDS/PAGE and the strong appearance of a approximately 350-kDa crosslinked product. Glycerol gradient centrifugation experiments indicated that native EEA1 had the same hydrodynamic properties as the approximately 350-kDa crosslinked complex. Two-hybrid analysis indicated that N- and C-terminal fragments of EEA1 can interact with themselves, but not with each other, suggesting that EEA1 forms parallel coiled-coil dimers. The ability of the C-terminus of EEA1 to dimerize correlates with its ability to bind to Rab5 and early endosomes, whereas its binding to PtdIns3P is independent of dimerization. These data enable us to propose a model for the quaternary structure of EEA1.  (+info)

Identification of the ras GTPase-activating protein GAP1(m) as a phosphatidylinositol-3,4,5-trisphosphate-binding protein in vivo. (3/1545)

GAP1(m) is a member of the GAP1 family of Ras GTPase-activating proteins (GAPs) [1]. In vitro, it has been shown to bind inositol 1, 3,4,5-tetrakisphosphate (IP4), the water-soluble inositol head group of the lipid second messenger phosphatidylinositol 3,4, 5-trisphosphate (PIP3) [2] [3]. This has led to the suggestion that GAP1(m) might function as a PIP3 receptor in vivo [4]. Here, using rat pheochromocytoma PC12 cells transiently transfected with a plasmid expressing a chimera of green fluorescent protein fused to GAP1(m) (GFP-GAP1(m)), we show that epidermal growth factor (EGF) induces a rapid (less than 60 seconds) recruitment of GFP-GAP1(m) from the cytosol to the plasma membrane. This recruitment required a functional GAP1(m) pleckstrin homology (PH) domain, because a specific point mutation (R629C) in the PH domain that inhibits IP4 binding in vitro [5] totally blocked EGF-induced GAP1(m) translocation. Furthermore, the membrane translocation was dependent on PI 3-kinase, and the time course of translocation paralleled the rate by which EGF stimulates the generation of plasma membrane PIP3 [6]. Significantly, the PIP3-induced recruitment of GAP1(m) did not appear to result in any detectable enhancement in its basal Ras GAP activity. From these results, we conclude that GAP1(m) binds PIP3 in vivo, and it is recruited to the plasma membrane, but does not appear to be activated, following agonist stimulation of PI 3-kinase.  (+info)

Identification of multiple phosphoinositide-specific phospholipases D as new regulatory enzymes for phosphatidylinositol 3,4, 5-trisphosphate. (4/1545)

In the course of delineating the regulatory mechanism underlying phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) metabolism, we have discovered three distinct phosphoinositide-specific phospholipase D (PI-PLD) isozymes from rat brain, tentatively designated as PI-PLDa, PI-PLDb, and PI-PLDc. These enzymes convert [3H]PI(3,4,5)P3 to generate a novel inositol phosphate, D-myo-[3H]inositol 3,4,5-trisphosphate ([3H]Ins(3,4,5)P3) and phosphatidic acid. These isozymes are predominantly associated with the cytosol, a notable difference from phosphatidylcholine PLDs. They are partially purified by a three-step procedure consisting of DEAE, heparin, and Sephacryl S-200 chromatography. PI-PLDa and PI-PLDb display a high degree of substrate specificity for PI(3,4, 5)P3, with a relative potency of PI(3,4,5)P3 >> phosphatidylinositol 3-phosphate (PI(3)P) or phosphatidylinositol 4-phosphate (PI(4)P) > phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) > phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2). In contrast, PI-PLDc preferentially utilizes PI(3)P as substrate, followed by, in sequence, PI(3,4,5)P3, PI(4)P, PI(3,4)P2, and PI(4,5)P2. Both PI(3, 4)P2 and PI(4,5)P2 are poor substrates for all three isozymes, indicating that the regulatory mechanisms underlying these phosphoinositides are different from that of PI(3,4,5)P3. None of these enzymes reacts with phosphatidylcholine, phosphatidylserine, or phosphatidylethanolamine. All three PI-PLDs are Ca2+-dependent. Among them, PI-PLDb and PI-PLDc show maximum activities within a sub-microM range (0.3 and 0.9 microM Ca2+, respectively), whereas PI-PLDa exhibits an optimal [Ca2+] at 20 microM. In contrast to PC-PLD, Mg2+ has no significant effect on the enzyme activity. All three enzymes require sodium deoxycholate for optimal activities; other detergents examined including Triton X-100 and Nonidet P-40 are, however, inhibitory. In addition, PI(4,5)P2 stimulates these isozymes in a dose-dependent manner. Enhancement in the enzyme activity is noted only when the molar ratio of PI(4,5)P2 to PI(3,4, 5)P3 is between 1:1 and 2:1.  (+info)

Pertussis toxin-sensitive and insensitive intracellular signalling pathways in undifferentiated 3T3-L1 cells stimulated by insulin converge with phosphatidylinositol 3-kinase upstream of the Ras mitogen-activated protein kinase cascade. (5/1545)

We have previously reported that pertussis toxin (PTX)-sensitive GTP binding protein (G-protein) and phosphatidylinositol 3-kinase (PI 3-K) are involved in adipocyte differentiation of 3T3-L1 cells induced by insulin/dexamethasone/methylisobutyl xanthine. The aim of this study was to examine the effect of PTX on the tyrosine kinase cascade stimulated by insulin acting through insulin-like growth factor-I (IGF-I) receptors in undifferentiated 3T3-L1 cells. A high level of mitogen-activated protein kinase (MAPK) activation was sustained for up to 4 h after insulin treatment, and mobility shifted and tyrosine phosphorylated MAPK was also detected. MAPK kinase activity measured by the incorporation of 32P into kinase-negative recombinant MAPK was enhanced by insulin treatment. We previously discovered that insulin activates Ras and that this is mediated by wortmannin-sensitive PI 3-K. Tyrosine-phosphorylation of IRS-1 and Shc also occurred in response to insulin. Subsequently, we investigated the effects of PTX on the activation of these proteins by insulin. Interestingly, treating 3T3-L1 cells with PTX attenuates the activation by insulin of both the Ras-MAPK cascade and PI 3-K. In contrast, neither tyrosine-phosphorylation of IRS-1 and Shc nor the interaction between IRS-1 and PI 3-K is sensitive to PTX. However, activation of the Ras-MAPK cascade and tyrosine-phosphorylation of Shc by epidermal growth factor are insensitive to PTX. These results indicate that there is another pathway which regulates PI 3-K and Ras-MAPK, independent of the pathway mediated by IGF-I receptor kinase. These findings suggest that in 3T3-L1 fibroblasts, PTX-sensitive G-proteins cross-talk with the Ras-MAPK pathway via PI 3-K by insulin acting via IGF-I receptors.  (+info)

Effects of phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 4-phosphate on a Na+-gated nonselective cation channel. (6/1545)

Olfactory receptor neurons in the lobster express a nonselective cation channel that is activated by intracellular Na+ and carries a substantial part of the depolarizing receptor current. Here, we show that phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] and phosphatidylinositol 4-phosphate [PI(4)P] applied to the intracellular face of cell-free patches activate the channel in the absence of Na+ and that antibodies against the respective phospholipids irreversibly inhibit the evoked activity. Further, we show that applying PI(4,5)P2 or PI(4)P in the presence of Na+ decreases the concentration of Na+ required to activate the channel from an EC50 of 74 to 22 mM for PI(4,5)P2 and to 29 mM for PI(4)P, respectively. Na+-gated channel activity was irreversibly inhibited by monoclonal antibodies against PI(4,5)P2 and PI(4)P in patches never exposed to exogenous phosphatidylinositols, suggesting that endogenous inositol phospholipids are required for the activation of the channel by intracellular Na+. Our findings suggest that PI(4,5)P2 and/or PI(4)P may serve as intracellular signaling molecules in these primary sensory neurons and provide a general mechanism to explain how the sensitivity of Na+-gated channels to Na+ could be much greater in intact cells than in excised membrane patches.  (+info)

Identification of protein kinase B (PKB) as a phosphatidylinositol 3,4,5-trisphosphate binding protein in Dictyostelium discoideum. (7/1545)

We have searched for phosphatidylinositol (PI)-3,4,5-trisphosphate (PIP3) binding proteins in Dictyostelium discoideum using beads bearing a PIP3 analogue, PIP3-APB. One of the binding proteins with a molecular mass of 55 kDa was purified and its amino acid sequence was partially analyzed. Database searches showed that the analyzed sequence was identical to that of protein kinase B (PKB) of D. discoideum. The specific activity of D. discoideum PKB, when expressed together with constitutively active PI-3 kinase in mammalian cells, was elevated by about three-fold, suggesting that PKB could also act downstream of PI-3 kinase in Dictyostelium cells.  (+info)

A phosphotransferase that generates phosphatidylinositol 4-phosphate (PtdIns-4-P) from phosphatidylinositol and lipid A in Rhizobium leguminosarum. A membrane-bound enzyme linking lipid a and ptdins-4-p biosynthesis. (8/1545)

Membranes of Rhizobium leguminosarum contain a 3-deoxy-D-manno-octulosonic acid (Kdo)-activated lipid A 4'-phosphatase required for generating the unusual phosphate-deficient lipid A found in this organism. The enzyme has been solubilized with Triton X-100 and purified 80-fold. As shown by co-purification and thermal inactivation studies, the 4'-phosphatase catalyzes not only the hydrolysis of (Kdo)2-[4'-32P]lipid IVA but also the transfer the 4'-phosphate of Kdo2-[4'-32P]lipid IVA to the inositol headgroup of phosphatidylinositol (PtdIns) to generate PtdIns-4-P. Like the 4'-phosphatase, the phosphotransferase activity is not present in Escherichia coli, Rhizobium meliloti, or the nodulation-defective mutant 24AR of R. leguminosarum. The specific activity for the phosphotransferase reaction is about 2 times higher than that of the 4'-phosphatase. The phosphotransferase assay conditions are similar to those used for PtdIns kinases, except that ATP and Mg2+ are omitted. The apparent Km for PtdIns is approximately 500 microM versus 20-100 microM for most PtdIns kinases, but the phosphotransferase specific activity in crude cell extracts is higher than that of most PtdIns kinases. The phosphotransferase is absolutely specific for the 4-position of PtdIns and is highly selective for PtdIns as the acceptor. The 4'-phosphatase/phosphotransferase can be eluted from heparin- or Cibacron blue-agarose with PtdIns. A phosphoenzyme intermediate may account for the dual function of this enzyme, since a single 32P-labeled protein species (Mr approximately 68,000) can be trapped and visualized by SDS gel electrophoresis of enzyme preparations incubated with Kdo2-[4'-32P]lipid IVA. Although PtdIns is not detected in cultures of R. leguminosarum/etli (CE3), PtdIns may be synthesized during nodulation or supplied by plant membranes, given that soybean PtdIns is an excellent phosphate acceptor. A bacterial enzyme for generating PtdIns-4-P and a direct link between lipid A and PtdIns-4-P biosynthesis have not been reported previously.  (+info)

Phosphatidylinositol phosphates (PIPs) are a family of lipid molecules that play crucial roles as secondary messengers in intracellular signaling pathways. They are formed by the phosphorylation of the hydroxyl group on the inositol ring of phosphatidylinositol (PI), a fundamental component of cell membranes.

There are seven main types of PIPs, classified based on the number and position of phosphate groups attached to the inositol ring:

1. Phosphatidylinositol 4-monophosphate (PI4P) - one phosphate group at the 4th position
2. Phosphatidylinositol 5-monophosphate (PI5P) - one phosphate group at the 5th position
3. Phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2) - two phosphate groups at the 3rd and 4th positions
4. Phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) - two phosphate groups at the 3rd and 5th positions
5. Phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] - two phosphate groups at the 4th and 5th positions
6. Phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3] - three phosphate groups at the 3rd, 4th, and 5th positions
7. Phosphatidylinositol 3-phosphate (PI3P) - one phosphate group at the 3rd position

These PIPs are involved in various cellular processes such as membrane trafficking, cytoskeleton organization, cell survival, and metabolism. Dysregulation of PIP metabolism has been implicated in several diseases, including cancer, diabetes, and neurological disorders.

Phosphatidylinositol 4,5-Diphosphate (PIP2) is a phospholipid molecule that plays a crucial role as a secondary messenger in various cell signaling pathways. It is a constituent of the inner leaflet of the plasma membrane and is formed by the phosphorylation of Phosphatidylinositol 4-Phosphate (PIP) at the 5th position of the inositol ring by enzyme Phosphoinositide kinase.

PIP2 is involved in several cellular processes, including regulation of ion channels, cytoskeleton dynamics, and membrane trafficking. It also acts as a substrate for the generation of two important secondary messengers, Inositol 1,4,5-Trisphosphate (IP3) and Diacylglycerol (DAG), which are produced by the action of Phospholipase C enzyme in response to various extracellular signals. These second messengers then mediate a variety of cellular responses such as calcium mobilization, gene expression, and cell proliferation.

Phosphatidylinositols (PIs) are a type of phospholipid that are abundant in the cell membrane. They contain a glycerol backbone, two fatty acid chains, and a head group consisting of myo-inositol, a cyclic sugar molecule, linked to a phosphate group.

Phosphatidylinositols can be phosphorylated at one or more of the hydroxyl groups on the inositol ring, forming various phosphoinositides (PtdInsPs) with different functions. These signaling molecules play crucial roles in regulating cellular processes such as membrane trafficking, cytoskeletal organization, and signal transduction pathways that control cell growth, differentiation, and survival.

Phosphatidylinositol 4,5-bisphosphate (PIP2) is a prominent phosphoinositide involved in the regulation of ion channels, enzymes, and cytoskeletal proteins. Upon activation of certain receptors, PIP2 can be cleaved by the enzyme phospholipase C into diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (InsP3), which act as second messengers to trigger downstream signaling events.

1-Phosphatidylinositol 4-Kinase (PI4K) is a type of enzyme that belongs to the family of kinases, which are enzymes that transfer phosphate groups from high-energy donor molecules to specific target proteins or lipids in the cell. PI4K specifically phosphorylates the 4th position on the inositol ring of phosphatidylinositol (PI), a type of phospholipid found in the cell membrane, converting it to phosphatidylinositol 4-phosphate (PI4P).

PI4K has several isoforms, including PI4K alpha, beta, gamma, and delta, which are located in different cellular compartments and play distinct roles. For example, PI4K alpha and beta are primarily involved in vesicle trafficking and Golgi function, while PI4K gamma and delta are associated with the plasma membrane and regulate ion channels and other signaling pathways.

PI4P, the product of PI4K activity, is an important signaling molecule that regulates various cellular processes, including membrane trafficking, cytoskeleton organization, and protein sorting. Dysregulation of PI4K and its downstream pathways has been implicated in several human diseases, such as cancer, neurodegeneration, and viral infection.

Phosphatidylinositol 3-Kinases (PI3Ks) are a family of enzymes that play a crucial role in intracellular signal transduction. They phosphorylate the 3-hydroxyl group of the inositol ring in phosphatidylinositol and its derivatives, which results in the production of second messengers that regulate various cellular processes such as cell growth, proliferation, differentiation, motility, and survival.

PI3Ks are divided into three classes based on their structure and substrate specificity. Class I PI3Ks are further subdivided into two categories: class IA and class IB. Class IA PI3Ks are heterodimers consisting of a catalytic subunit (p110α, p110β, or p110δ) and a regulatory subunit (p85α, p85β, p55γ, or p50γ). They are primarily activated by receptor tyrosine kinases and G protein-coupled receptors. Class IB PI3Ks consist of a catalytic subunit (p110γ) and a regulatory subunit (p101 or p84/87). They are mainly activated by G protein-coupled receptors.

Dysregulation of PI3K signaling has been implicated in various human diseases, including cancer, diabetes, and autoimmune disorders. Therefore, PI3Ks have emerged as important targets for drug development in these areas.

I'm sorry for any confusion, but "Talin" is not a medical term that I am aware of. Talin is actually a protein involved in cell-matrix and cell-cell adhesion, acting as a crucial component in connecting the intracellular cytoskeleton to the extracellular matrix. It might be used in scientific or biology research contexts, but it's not a term typically found in medical textbooks or patient-related medical definitions. If you have any questions about medical conditions or terms, I would be happy to help with those!

Phosphates, in a medical context, refer to the salts or esters of phosphoric acid. Phosphates play crucial roles in various biological processes within the human body. They are essential components of bones and teeth, where they combine with calcium to form hydroxyapatite crystals. Phosphates also participate in energy transfer reactions as phosphate groups attached to adenosine diphosphate (ADP) and adenosine triphosphate (ATP). Additionally, they contribute to buffer systems that help maintain normal pH levels in the body.

Abnormal levels of phosphates in the blood can indicate certain medical conditions. High phosphate levels (hyperphosphatemia) may be associated with kidney dysfunction, hyperparathyroidism, or excessive intake of phosphate-containing products. Low phosphate levels (hypophosphatemia) might result from malnutrition, vitamin D deficiency, or certain diseases affecting the small intestine or kidneys. Both hypophosphatemia and hyperphosphatemia can have significant impacts on various organ systems and may require medical intervention.

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

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

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

Phosphorylation is the process of adding a phosphate group (a molecule consisting of one phosphorus atom and four oxygen atoms) to a protein or other organic molecule, which is usually done by enzymes called kinases. This post-translational modification can change the function, localization, or activity of the target molecule, playing a crucial role in various cellular processes such as signal transduction, metabolism, and regulation of gene expression. Phosphorylation is reversible, and the removal of the phosphate group is facilitated by enzymes called phosphatases.

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

Signal transduction is the process by which a cell converts an extracellular signal, such as a hormone or neurotransmitter, into an intracellular response. This involves a series of molecular events that transmit the signal from the cell surface to the interior of the cell, ultimately resulting in changes in gene expression, protein activity, or metabolism.

The process typically begins with the binding of the extracellular signal to a receptor located on the cell membrane. This binding event activates the receptor, which then triggers a cascade of intracellular signaling molecules, such as second messengers, protein kinases, and ion channels. These molecules amplify and propagate the signal, ultimately leading to the activation or inhibition of specific cellular responses.

Signal transduction pathways are highly regulated and can be modulated by various factors, including other signaling molecules, post-translational modifications, and feedback mechanisms. Dysregulation of these pathways has been implicated in a variety of diseases, including cancer, diabetes, and neurological disorders.

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

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

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

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

Chromones are a type of chemical compound that contain a benzopyran ring, which is a structural component made up of a benzene ring fused to a pyran ring. They can be found in various plants and have been used in medicine for their anti-inflammatory, antimicrobial, and antitussive (cough suppressant) properties. Some chromones are also known to have estrogenic activity and have been studied for their potential use in hormone replacement therapy. Additionally, some synthetic chromones have been developed as drugs for the treatment of asthma and other respiratory disorders.

Androstadienes are a class of steroid hormones that are derived from androstenedione, which is a weak male sex hormone. Androstadienes include various compounds such as androstadiene-3,17-dione and androstanedione, which are intermediate products in the biosynthesis of more potent androgens like testosterone and dihydrotestosterone.

Androstadienes are present in both males and females but are found in higher concentrations in men. They can be detected in various bodily fluids, including blood, urine, sweat, and semen. In addition to their role in steroid hormone synthesis, androstadienes have been studied for their potential use as biomarkers of physiological processes and disease states.

It's worth noting that androstadienes are sometimes referred to as "androstenes" in the literature, although this term can also refer to other related compounds.

Phosphatidylinositol 3-Kinase (PI3K) is an intracellular lipid kinase that phosphorylates the 3-hydroxyl group of the inositol ring of phosphatidylinositol and its phosphorylated derivatives, converting PIP2 (phosphatidylinositol 4,5-bisphosphate) to PIP3 (phosphatidylinositol 3,4,5-trisphosphate). This enzyme plays a crucial role in various cellular functions such as cell growth, proliferation, differentiation, motility, survival, and intracellular trafficking. PI3Ks are classified into three classes (I, II, and III) based on their structure, regulation, and substrate specificity. Class I PI3Ks are further divided into two subclasses (IA and IB), which are involved in signal transduction downstream of receptor tyrosine kinases and G protein-coupled receptors. Dysregulation of PI3K signaling has been implicated in various human diseases, including cancer, diabetes, and autoimmune disorders.

I'm sorry for any confusion, but "Morpholines" is not a medical term. It is a chemical term that refers to a class of heterocyclic organic compounds containing one nitrogen atom and one oxygen atom in the ring. They are widely used as intermediates in the synthesis of various pharmaceuticals, agrochemicals, and dyes. If you have any questions about a medical issue or term, I'd be happy to try to help answer those for you!

Sugar phosphates are organic compounds that play crucial roles in various biological processes, particularly in the field of genetics and molecular biology. They are formed by the attachment of a phosphate group to a sugar molecule, most commonly to the 5-carbon sugar ribose or deoxyribose.

In genetics, sugar phosphates form the backbone of nucleic acids, such as DNA and RNA. In DNA, the sugar phosphate backbone consists of alternating deoxyribose (a sugar) and phosphate groups, linked together by covalent bonds between the 5' carbon atom of one sugar molecule and the 3' carbon atom of another sugar molecule. This forms a long, twisted ladder-like structure known as a double helix.

Similarly, in RNA, the sugar phosphate backbone is formed by ribose (a sugar) and phosphate groups, creating a single-stranded structure that can fold back on itself to form complex shapes. These sugar phosphate backbones provide structural support for the nucleic acids and help to protect the genetic information stored within them.

Sugar phosphates also play important roles in energy metabolism, as they are involved in the formation and breakdown of high-energy compounds such as ATP (adenosine triphosphate) and GTP (guanosine triphosphate). These molecules serve as energy currency for cells, storing and releasing energy as needed to power various cellular processes.

Protein-kinase B, also known as AKT, is a group of intracellular proteins that play a crucial role in various cellular processes such as glucose metabolism, apoptosis, cell proliferation, transcription, and cell migration. The AKT family includes three isoforms: AKT1, AKT2, and AKT3, which are encoded by the genes PKBalpha, PKBbeta, and PKBgamma, respectively.

Proto-oncogene proteins c-AKT refer to the normal, non-mutated forms of these proteins that are involved in the regulation of cell growth and survival under physiological conditions. However, when these genes are mutated or overexpressed, they can become oncogenes, leading to uncontrolled cell growth and cancer development.

Activation of c-AKT occurs through a signaling cascade that begins with the binding of extracellular ligands such as insulin-like growth factor 1 (IGF-1) or epidermal growth factor (EGF) to their respective receptors on the cell surface. This triggers a series of phosphorylation events that ultimately lead to the activation of c-AKT, which then phosphorylates downstream targets involved in various cellular processes.

In summary, proto-oncogene proteins c-AKT are normal intracellular proteins that play essential roles in regulating cell growth and survival under physiological conditions. However, their dysregulation can contribute to cancer development and progression.

Inositol phosphates are a family of molecules that consist of an inositol ring, which is a six-carbon heterocyclic compound, linked to one or more phosphate groups. These molecules play important roles as intracellular signaling intermediates and are involved in various cellular processes such as cell growth, differentiation, and metabolism.

Inositol hexakisphosphate (IP6), also known as phytic acid, is a form of inositol phosphate that is found in plant-based foods. IP6 has the ability to bind to minerals such as calcium, magnesium, and iron, which can reduce their bioavailability in the body.

Inositol phosphates have been implicated in several diseases, including cancer, diabetes, and neurodegenerative disorders. For example, altered levels of certain inositol phosphates have been observed in cancer cells, suggesting that they may play a role in tumor growth and progression. Additionally, mutations in enzymes involved in the metabolism of inositol phosphates have been associated with several genetic diseases.

Calcium phosphates are a group of minerals that are important components of bones and teeth. They are also found in some foods and are used in dietary supplements and medical applications. Chemically, calcium phosphates are salts of calcium and phosphoric acid, and they exist in various forms, including hydroxyapatite, which is the primary mineral component of bone tissue. Other forms of calcium phosphates include monocalcium phosphate, dicalcium phosphate, and tricalcium phosphate, which are used as food additives and dietary supplements. Calcium phosphates are important for maintaining strong bones and teeth, and they also play a role in various physiological processes, such as nerve impulse transmission and muscle contraction.

Glucose-6-phosphate (G6P) is a vital intermediate compound in the metabolism of glucose, which is a simple sugar that serves as a primary source of energy for living organisms. G6P plays a critical role in both glycolysis and gluconeogenesis pathways, contributing to the regulation of blood glucose levels and energy production within cells.

In biochemistry, glucose-6-phosphate is defined as:

A hexose sugar phosphate ester formed by the phosphorylation of glucose at the 6th carbon atom by ATP in a reaction catalyzed by the enzyme hexokinase or glucokinase. This reaction is the first step in both glycolysis and glucose storage (glycogen synthesis) processes, ensuring that glucose can be effectively utilized for energy production or stored for later use.

G6P serves as a crucial metabolic branch point, leading to various pathways such as:

1. Glycolysis: In the presence of sufficient ATP and NAD+ levels, G6P is further metabolized through glycolysis to generate pyruvate, which enters the citric acid cycle for additional energy production in the form of ATP, NADH, and FADH2.
2. Gluconeogenesis: During periods of low blood glucose levels, G6P can be synthesized back into glucose through the gluconeogenesis pathway, primarily occurring in the liver and kidneys. This process helps maintain stable blood glucose concentrations and provides energy to cells when dietary intake is insufficient.
3. Pentose phosphate pathway (PPP): A portion of G6P can be shunted into the PPP, an alternative metabolic route that generates NADPH, ribose-5-phosphate for nucleotide synthesis, and erythrose-4-phosphate for aromatic amino acid production. The PPP is essential in maintaining redox balance within cells and supporting biosynthetic processes.

Overall, glucose-6-phosphate plays a critical role as a central metabolic intermediate, connecting various pathways to regulate energy homeostasis, redox balance, and biosynthesis in response to cellular demands and environmental cues.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is an enzyme that plays a crucial role in the metabolic pathway of glycolysis. Its primary function is to convert glyceraldehyde-3-phosphate (a triose sugar phosphate) into D-glycerate 1,3-bisphosphate, while also converting nicotinamide adenine dinucleotide (NAD+) into its reduced form NADH. This reaction is essential for the production of energy in the form of adenosine triphosphate (ATP) during cellular respiration. GAPDH has also been implicated in various non-metabolic processes, including DNA replication, repair, and transcription regulation, due to its ability to interact with different proteins and nucleic acids.

Enzyme activation refers to the process by which an enzyme becomes biologically active and capable of carrying out its specific chemical or biological reaction. This is often achieved through various post-translational modifications, such as proteolytic cleavage, phosphorylation, or addition of cofactors or prosthetic groups to the enzyme molecule. These modifications can change the conformation or structure of the enzyme, exposing or creating a binding site for the substrate and allowing the enzymatic reaction to occur.

For example, in the case of proteolytic cleavage, an inactive precursor enzyme, known as a zymogen, is cleaved into its active form by a specific protease. This is seen in enzymes such as trypsin and chymotrypsin, which are initially produced in the pancreas as inactive precursors called trypsinogen and chymotrypsinogen, respectively. Once they reach the small intestine, they are activated by enteropeptidase, a protease that cleaves a specific peptide bond, releasing the active enzyme.

Phosphorylation is another common mechanism of enzyme activation, where a phosphate group is added to a specific serine, threonine, or tyrosine residue on the enzyme by a protein kinase. This modification can alter the conformation of the enzyme and create a binding site for the substrate, allowing the enzymatic reaction to occur.

Enzyme activation is a crucial process in many biological pathways, as it allows for precise control over when and where specific reactions take place. It also provides a mechanism for regulating enzyme activity in response to various signals and stimuli, such as hormones, neurotransmitters, or changes in the intracellular environment.

Inositol is not considered a true "vitamin" because it can be created by the body from glucose. However, it is an important nutrient and is sometimes referred to as vitamin B8. It is a type of sugar alcohol that is found in both animals and plants. Inositol is involved in various biological processes, including:

1. Signal transduction: Inositol phospholipids are key components of cell membranes and play a crucial role in intracellular signaling pathways. They act as secondary messengers in response to hormones, neurotransmitters, and growth factors.
2. Insulin sensitivity: Inositol and its derivatives, such as myo-inositol and D-chiro-inositol, are involved in insulin signal transduction. Abnormalities in inositol metabolism have been linked to insulin resistance and conditions like polycystic ovary syndrome (PCOS).
3. Cerebral and ocular functions: Inositol is essential for the proper functioning of neurons and has been implicated in various neurological and psychiatric disorders, such as depression, anxiety, and bipolar disorder. It also plays a role in maintaining eye health.
4. Lipid metabolism: Inositol participates in the breakdown and transport of fats within the body.
5. Gene expression: Inositol and its derivatives are involved in regulating gene expression through epigenetic modifications.

Inositol can be found in various foods, including fruits, beans, grains, nuts, and vegetables. It is also available as a dietary supplement for those who wish to increase their intake.

Phosphoric monoester hydrolases are a class of enzymes that catalyze the hydrolysis of phosphoric monoesters into alcohol and phosphate. This class of enzymes includes several specific enzymes, such as phosphatases and nucleotidases, which play important roles in various biological processes, including metabolism, signal transduction, and regulation of cellular processes.

Phosphoric monoester hydrolases are classified under the EC number 3.1.3 by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB). The enzymes in this class share a common mechanism of action, which involves the nucleophilic attack on the phosphorus atom of the substrate by a serine or cysteine residue in the active site of the enzyme. This results in the formation of a covalent intermediate, which is then hydrolyzed to release the products.

Phosphoric monoester hydrolases are important therapeutic targets for the development of drugs that can modulate their activity. For example, inhibitors of phosphoric monoester hydrolases have been developed as potential treatments for various diseases, including cancer, neurodegenerative disorders, and infectious diseases.

Phosphotransferases are a group of enzymes that catalyze the transfer of a phosphate group from a donor molecule to an acceptor molecule. This reaction is essential for various cellular processes, including energy metabolism, signal transduction, and biosynthesis.

The systematic name for this group of enzymes is phosphotransferase, which is derived from the general reaction they catalyze: D-donor + A-acceptor = D-donor minus phosphate + A-phosphate. The donor molecule can be a variety of compounds, such as ATP or a phosphorylated protein, while the acceptor molecule is typically a compound that becomes phosphorylated during the reaction.

Phosphotransferases are classified into several subgroups based on the type of donor and acceptor molecules they act upon. For example, kinases are a subgroup of phosphotransferases that transfer a phosphate group from ATP to a protein or other organic compound. Phosphatases, another subgroup, remove phosphate groups from molecules by transferring them to water.

Overall, phosphotransferases play a critical role in regulating many cellular functions and are important targets for drug development in various diseases, including cancer and neurological disorders.

Enzyme inhibitors are substances that bind to an enzyme and decrease its activity, preventing it from catalyzing a chemical reaction in the body. They can work by several mechanisms, including blocking the active site where the substrate binds, or binding to another site on the enzyme to change its shape and prevent substrate binding. Enzyme inhibitors are often used as drugs to treat various medical conditions, such as high blood pressure, abnormal heart rhythms, and bacterial infections. They can also be found naturally in some foods and plants, and can be used in research to understand enzyme function and regulation.

Type C phospholipases, also known as group CIA phospholipases or patatin-like phospholipase domain containing proteins (PNPLAs), are a subclass of phospholipases that specifically hydrolyze the sn-2 ester bond of glycerophospholipids. They belong to the PNPLA family, which includes nine members (PNPLA1-9) with diverse functions in lipid metabolism and cell signaling.

Type C phospholipases contain a patatin domain, which is a conserved region of approximately 240 amino acids that exhibits lipase and acyltransferase activities. These enzymes are primarily involved in the regulation of triglyceride metabolism, membrane remodeling, and cell signaling pathways.

PNPLA1 (adiponutrin) is mainly expressed in the liver and adipose tissue, where it plays a role in lipid droplet homeostasis and triglyceride hydrolysis. PNPLA2 (ATGL or desnutrin) is a key regulator of triglyceride metabolism, responsible for the initial step of triacylglycerol hydrolysis in adipose tissue and other tissues.

PNPLA3 (calcium-independent phospholipase A2 epsilon or iPLA2ε) is involved in membrane remodeling, arachidonic acid release, and cell signaling pathways. Mutations in PNPLA3 have been associated with an increased risk of developing nonalcoholic fatty liver disease (NAFLD), alcoholic liver disease, and hepatic steatosis.

PNPLA4 (lipase maturation factor 1 or LMF1) is involved in the intracellular processing and trafficking of lipases, such as pancreatic lipase and hepatic lipase. PNPLA5 ( Mozart1 or GSPML) has been implicated in membrane trafficking and cell signaling pathways.

PNPLA6 (neuropathy target esterase or NTE) is primarily expressed in the brain, where it plays a role in maintaining neuronal integrity by regulating lipid metabolism. Mutations in PNPLA6 have been associated with neuropathy and cognitive impairment.

PNPLA7 (adiponutrin or ADPN) has been implicated in lipid droplet formation, triacylglycerol hydrolysis, and cell signaling pathways. Mutations in PNPLA7 have been associated with an increased risk of developing NAFLD and hepatic steatosis.

PNPLA8 (diglyceride lipase or DGLα) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA9 (calcium-independent phospholipase A2 gamma or iPLA2γ) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA10 (calcium-independent phospholipase A2 delta or iPLA2δ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA11 (calcium-independent phospholipase A2 epsilon or iPLA2ε) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA12 (calcium-independent phospholipase A2 zeta or iPLA2ζ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA13 (calcium-independent phospholipase A2 eta or iPLA2η) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA14 (calcium-independent phospholipase A2 theta or iPLA2θ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA15 (calcium-independent phospholipase A2 iota or iPLA2ι) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA16 (calcium-independent phospholipase A2 kappa or iPLA2κ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA17 (calcium-independent phospholipase A2 lambda or iPLA2λ) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA18 (calcium-independent phospholipase A2 mu or iPLA2μ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA19 (calcium-independent phospholipase A2 nu or iPLA2ν) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA20 (calcium-independent phospholipase A2 xi or iPLA2ξ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA21 (calcium-independent phospholipase A2 omicron or iPLA2ο) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA22 (calcium-independent phospholipase A2 pi or iPLA2π) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA23 (calcium-independent phospholipase A2 rho or iPLA2ρ) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA24 (calcium-independent phospholipase A2 sigma or iPLA2σ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA25 (calcium-independent phospholipase A2 tau or iPLA2τ) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA26 (calcium-independent phospholipase A2 upsilon or iPLA2υ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA27 (calcium-independent phospholipase A2 phi or iPLA2φ) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA28 (calcium-independent phospholipase A2 chi or iPLA2χ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA29 (calcium-independent phospholipase A2 psi or iPLA2ψ) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA30 (calcium-independent phospholipase A2 omega or iPLA2ω) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA31 (calcium-independent phospholipase A2 pi or iPLA2π) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA32 (calcium-independent phospholipase A2 rho or iPLA2ρ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA33 (calcium-independent phospholipase A2 sigma or iPLA2σ) has been implicated in membrane remodeling, ar

CDP-diacylglycerol-inositol 3-phosphatidyltransferase is an enzyme that plays a role in the synthesis of phosphatidylinositol (PI) lipids, which are important components of cell membranes and also serve as secondary messengers in intracellular signaling pathways.

The enzyme catalyzes the transfer of a phosphate group from CDP-diacylglycerol to the 3-hydroxyl position of inositol, resulting in the formation of phosphatidylinositol 3-phosphate (PI3P). PI3P is a key signaling molecule that regulates various cellular processes, including membrane trafficking, autophagy, and inflammation.

CDP-diacylglycerol-inositol 3-phosphatidyltransferase is also known as phosphatidylinositol 3-kinase (PI3K) or type II PI3K, and it is distinct from the class I PI3Ks that are involved in growth factor signaling and oncogenesis. Mutations in CDP-diacylglycerol-inositol 3-phosphatidyltransferase have been implicated in various diseases, including cancer, neurodevelopmental disorders, and autoimmune diseases.

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

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

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

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

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

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

Phosphatidylinositol Diacylglycerol-Lyase is an enzyme that plays a crucial role in the breakdown and metabolism of certain lipids known as phosphoinositides. These are important components of cell membranes and are involved in various cellular processes such as signal transduction.

The systematic name for this enzyme is 1-phosphatidyl-1D-myo-inositol-3,4-bisphosphate D-3-phosphoinositide phospholipase C. Its function is to cleave 1,2-diacylglycerol and inositol 1,3,4,5-tetrakisphosphate from 1-phosphatidyl-1D-myo-inositol-3,4-bisphosphate. This reaction is a key step in the phosphoinositide signaling pathway, which is involved in regulating various cellular functions such as cell growth, differentiation, and metabolism.

Defects in this enzyme have been associated with certain diseases, including neurological disorders and cancer. Therefore, understanding its function and regulation is an important area of research in biology and medicine.

Protein-Serine-Threonine Kinases (PSTKs) are a type of protein kinase that catalyzes the transfer of a phosphate group from ATP to the hydroxyl side chains of serine or threonine residues on target proteins. This phosphorylation process plays a crucial role in various cellular signaling pathways, including regulation of metabolism, gene expression, cell cycle progression, and apoptosis. PSTKs are involved in many physiological and pathological processes, and their dysregulation has been implicated in several diseases, such as cancer, diabetes, and neurodegenerative disorders.

Phospholipids are a major class of lipids that consist of a hydrophilic (water-attracting) head and two hydrophobic (water-repelling) tails. The head is composed of a phosphate group, which is often bound to an organic molecule such as choline, ethanolamine, serine or inositol. The tails are made up of two fatty acid chains.

Phospholipids are a key component of cell membranes and play a crucial role in maintaining the structural integrity and function of the cell. They form a lipid bilayer, with the hydrophilic heads facing outwards and the hydrophobic tails facing inwards, creating a barrier that separates the interior of the cell from the outside environment.

Phospholipids are also involved in various cellular processes such as signal transduction, intracellular trafficking, and protein function regulation. Additionally, they serve as emulsifiers in the digestive system, helping to break down fats in the diet.

Proto-oncogene proteins are normal cellular proteins that play crucial roles in various cellular processes, such as signal transduction, cell cycle regulation, and apoptosis (programmed cell death). They are involved in the regulation of cell growth, differentiation, and survival under physiological conditions.

When proto-oncogene proteins undergo mutations or aberrations in their expression levels, they can transform into oncogenic forms, leading to uncontrolled cell growth and division. These altered proteins are then referred to as oncogene products or oncoproteins. Oncogenic mutations can occur due to various factors, including genetic predisposition, environmental exposures, and aging.

Examples of proto-oncogene proteins include:

1. Ras proteins: Involved in signal transduction pathways that regulate cell growth and differentiation. Activating mutations in Ras genes are found in various human cancers.
2. Myc proteins: Regulate gene expression related to cell cycle progression, apoptosis, and metabolism. Overexpression of Myc proteins is associated with several types of cancer.
3. EGFR (Epidermal Growth Factor Receptor): A transmembrane receptor tyrosine kinase that regulates cell proliferation, survival, and differentiation. Mutations or overexpression of EGFR are linked to various malignancies, such as lung cancer and glioblastoma.
4. Src family kinases: Intracellular tyrosine kinases that regulate signal transduction pathways involved in cell proliferation, survival, and migration. Dysregulation of Src family kinases is implicated in several types of cancer.
5. Abl kinases: Cytoplasmic tyrosine kinases that regulate various cellular processes, including cell growth, differentiation, and stress responses. Aberrant activation of Abl kinases, as seen in chronic myelogenous leukemia (CML), leads to uncontrolled cell proliferation.

Understanding the roles of proto-oncogene proteins and their dysregulation in cancer development is essential for developing targeted cancer therapies that aim to inhibit or modulate these aberrant signaling pathways.

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

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

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

Phosphatidic acids (PAs) are a type of phospholipid that are essential components of cell membranes. They are composed of a glycerol backbone linked to two fatty acid chains and a phosphate group. The phosphate group is esterified to another molecule, usually either serine, inositol, or choline, forming different types of phosphatidic acids.

PAs are particularly important as they serve as key regulators of many cellular processes, including signal transduction, membrane trafficking, and autophagy. They can act as signaling molecules by binding to and activating specific proteins, such as the enzyme phospholipase D, which generates second messengers involved in various signaling pathways.

PAs are also important intermediates in the synthesis of other phospholipids, such as phosphatidylcholine, phosphatidylethanolamine, and phosphatidylinositol. They are produced by the enzyme diacylglycerol kinase (DGK), which adds a phosphate group to diacylglycerol (DAG) to form PA.

Abnormal levels of PAs have been implicated in various diseases, including cancer, diabetes, and neurological disorders. Therefore, understanding the regulation and function of PAs is an active area of research with potential therapeutic implications.

Glyceraldehyde 3-phosphate (G3P) is a crucial intermediate in both glycolysis and gluconeogenesis metabolic pathways. It is an triose sugar phosphate, which means it contains three carbon atoms and has a phosphate group attached to it.

In the glycolysis process, G3P is produced during the third step of the process from the molecule dihydroxyacetone phosphate (DHAP) via the enzyme triosephosphate isomerase. In the following steps, G3P is converted into 1,3-bisphosphoglycerate, which eventually leads to the production of ATP and NADH.

In gluconeogenesis, G3P is produced from the reverse reaction of the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase, using the molecule dihydroxyacetone phosphate (DHAP) as a starting point. G3P is then converted into glucose-6-phosphate, which can be further metabolized or released from the cell.

It's important to note that Glyceraldehyde 3-Phosphate plays a key role in energy production and carbohydrate metabolism.

Phosphoproteins are proteins that have been post-translationally modified by the addition of a phosphate group (-PO3H2) onto specific amino acid residues, most commonly serine, threonine, or tyrosine. This process is known as phosphorylation and is mediated by enzymes called kinases. Phosphoproteins play crucial roles in various cellular processes such as signal transduction, cell cycle regulation, metabolism, and gene expression. The addition or removal of a phosphate group can activate or inhibit the function of a protein, thereby serving as a switch to control its activity. Phosphoproteins can be detected and quantified using techniques such as Western blotting, mass spectrometry, and immunofluorescence.

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

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

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

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

The Pentose Phosphate Pathway (also known as the Hexose Monophosphate Shunt or HMP Shunt) is a metabolic pathway that runs parallel to glycolysis. It serves two major functions:

1. Providing reducing equivalents in the form of NADPH for reductive biosynthesis and detoxification processes.
2. Generating ribose-5-phosphate, a pentose sugar used in the synthesis of nucleotides and nucleic acids (DNA and RNA).

This pathway begins with the oxidation of glucose-6-phosphate to form 6-phosphogluconolactone, catalyzed by the enzyme glucose-6-phosphate dehydrogenase. The resulting NADPH is used in various anabolic reactions and antioxidant defense systems.

The Pentose Phosphate Pathway also includes a series of reactions called the non-oxidative branch, which interconverts various sugars to meet cellular needs for different types of monosaccharides. These conversions are facilitated by several enzymes including transketolase and transaldolase.

Phospholipid transfer proteins (PLTPs) are a group of proteins found in the bloodstream that play a crucial role in the distribution and metabolism of phospholipids, which are key components of cell membranes. These proteins facilitate the transfer of phospholipids between different lipoprotein particles, such as high-density lipoproteins (HDL) and low-density lipoproteins (LDL), in a process known as non-vesicular lipid transport.

PLTPs can also modulate the size, composition, and function of these lipoprotein particles, which has implications for lipid metabolism, inflammation, and atherosclerosis. Additionally, PLTPs have been implicated in various physiological processes, including cell signaling, membrane trafficking, and host defense mechanisms.

It is worth noting that while PLTPs are important regulators of lipid metabolism, their precise role in human health and disease is still an area of active research.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), also known as Glucosephosphate Dehydrogenase, is an enzyme that plays a crucial role in cellular metabolism, particularly in the glycolytic pathway. It catalyzes the conversion of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (1,3-BPG), while also converting nicotinamide adenine dinucleotide (NAD+) to its reduced form NADH. This reaction is essential for the production of energy in the form of adenosine triphosphate (ATP) during cellular respiration. GAPDH has been widely used as a housekeeping gene in molecular biology research due to its consistent expression across various tissues and cells, although recent studies have shown that its expression can vary under certain conditions.

Lysophospholipids are a type of glycerophospholipid, which is a major component of cell membranes. They are characterized by having only one fatty acid chain attached to the glycerol backbone, as opposed to two in regular phospholipids. This results in a more polar and charged molecule, which can play important roles in cell signaling and regulation.

Lysophospholipids can be derived from the breakdown of regular phospholipids through the action of enzymes such as phospholipase A1 or A2. They can also be synthesized de novo in the cell. Some lysophospholipids, such as lysophosphatidic acid (LPA) and sphingosine-1-phosphate (S1P), have been found to act as signaling molecules that bind to specific G protein-coupled receptors and regulate various cellular processes, including proliferation, survival, and migration.

Abnormal levels of lysophospholipids have been implicated in several diseases, such as cancer, inflammation, and neurological disorders. Therefore, understanding the biology of lysophospholipids has important implications for developing new therapeutic strategies.

Dihydroxyacetone Phosphate (DHAP) is a 3-carbon organic compound that plays a crucial role in the metabolic pathway called glycolysis. It is an intermediate molecule formed during the conversion of glucose into pyruvate, which ultimately produces energy in the form of ATP.

In the glycolytic process, DHAP is produced from glyceraldehyde 3-phosphate (G3P) in a reaction catalyzed by the enzyme triose phosphate isomerase. Then, DHAP is converted back to G3P in a subsequent step, which prepares it for further processing in the glycolytic pathway. This reversible conversion of DHAP and G3P helps maintain the equilibrium of the glycolytic process.

Apart from its role in energy metabolism, DHAP is also involved in other biochemical processes, such as the synthesis of glucose during gluconeogenesis and the formation of lipids in the liver.

Phosphate transport proteins are membrane-bound proteins responsible for the active transport of phosphate ions across cell membranes. They play a crucial role in maintaining appropriate phosphate concentrations within cells and between intracellular compartments, which is essential for various biological processes such as energy metabolism, signal transduction, and bone formation.

These proteins utilize the energy derived from ATP hydrolysis or other sources to move phosphate ions against their concentration gradient, thereby facilitating cellular uptake of phosphate even when extracellular concentrations are low. Phosphate transport proteins can be classified based on their structure, function, and localization into different types, including sodium-dependent and sodium-independent transporters, secondary active transporters, and channels.

Dysregulation of phosphate transport proteins has been implicated in several pathological conditions, such as renal Fanconi syndrome, tumoral calcinosis, and hypophosphatemic rickets. Therefore, understanding the molecular mechanisms underlying phosphate transport protein function is essential for developing targeted therapies to treat these disorders.

Insulin Receptor Substrate (IRS) proteins are a family of cytoplasmic signaling proteins that play a crucial role in the insulin signaling pathway. There are four main isoforms in humans, namely IRS-1, IRS-2, IRS-3, and IRS-4, which contain several conserved domains for interacting with various signaling molecules.

When insulin binds to its receptor, the intracellular tyrosine kinase domain of the receptor becomes activated and phosphorylates specific tyrosine residues on IRS proteins. This leads to the recruitment and activation of downstream effectors, such as PI3K and Grb2/SOS, which ultimately result in metabolic responses (e.g., glucose uptake, glycogen synthesis) and mitogenic responses (e.g., cell proliferation, differentiation).

Dysregulation of the IRS-mediated insulin signaling pathway has been implicated in several pathological conditions, including insulin resistance, type 2 diabetes, and certain types of cancer.

Isoenzymes, also known as isoforms, are multiple forms of an enzyme that catalyze the same chemical reaction but differ in their amino acid sequence, structure, and/or kinetic properties. They are encoded by different genes or alternative splicing of the same gene. Isoenzymes can be found in various tissues and organs, and they play a crucial role in biological processes such as metabolism, detoxification, and cell signaling. Measurement of isoenzyme levels in body fluids (such as blood) can provide valuable diagnostic information for certain medical conditions, including tissue damage, inflammation, and various diseases.

Hydrolysis is a chemical process, not a medical one. However, it is relevant to medicine and biology.

Hydrolysis is the breakdown of a chemical compound due to its reaction with water, often resulting in the formation of two or more simpler compounds. In the context of physiology and medicine, hydrolysis is a crucial process in various biological reactions, such as the digestion of food molecules like proteins, carbohydrates, and fats. Enzymes called hydrolases catalyze these hydrolysis reactions to speed up the breakdown process in the body.

Pyridoxal phosphate (PLP) is the active form of vitamin B6 and functions as a cofactor in various enzymatic reactions in the human body. It plays a crucial role in the metabolism of amino acids, carbohydrates, lipids, and neurotransmitters. Pyridoxal phosphate is involved in more than 140 different enzyme-catalyzed reactions, making it one of the most versatile cofactors in human biochemistry.

As a cofactor, pyridoxal phosphate helps enzymes carry out their functions by facilitating chemical transformations in substrates (the molecules on which enzymes act). In particular, PLP is essential for transamination, decarboxylation, racemization, and elimination reactions involving amino acids. These processes are vital for the synthesis and degradation of amino acids, neurotransmitters, hemoglobin, and other crucial molecules in the body.

Pyridoxal phosphate is formed from the conversion of pyridoxal (a form of vitamin B6) by the enzyme pyridoxal kinase, using ATP as a phosphate donor. The human body obtains vitamin B6 through dietary sources such as whole grains, legumes, vegetables, nuts, and animal products like poultry, fish, and pork. It is essential to maintain adequate levels of pyridoxal phosphate for optimal enzymatic function and overall health.

Class III phosphatidylinositol 3-kinases (PI3Ks) are a subclass of the PI3K family, which are enzymes that play a crucial role in intracellular signaling pathways involved in various cellular processes such as cell growth, proliferation, differentiation, and survival.

Class III PI3Ks, also known as Vps34-like kinases, specifically phosphorylate the 3-hydroxyl group of the invariant position D-3 of the inositol ring of phosphatidylinositol (PI) to produce phosphatidylinositol 3-phosphate (PI3P). This lipid second messenger is involved in various cellular functions, including vesicle trafficking and autophagy.

Class III PI3Ks are composed of a catalytic subunit, Vps34, and a regulatory subunit, Vps15, which are both required for their activity. Mutations or dysregulation of Class III PI3Ks have been implicated in various human diseases, including cancer, neurodegenerative disorders, and infectious diseases.

Sphingosine is not a medical term per se, but rather a biological compound with importance in the field of medicine. It is a type of sphingolipid, a class of lipids that are crucial components of cell membranes. Sphingosine itself is a secondary alcohol with an amino group and two long-chain hydrocarbons.

Medically, sphingosine is significant due to its role as a precursor in the synthesis of other sphingolipids, such as ceramides, sphingomyelins, and gangliosides, which are involved in various cellular processes like signal transduction, cell growth, differentiation, and apoptosis (programmed cell death).

Moreover, sphingosine-1-phosphate (S1P), a derivative of sphingosine, is an important bioactive lipid mediator that regulates various physiological functions, including immune response, vascular maturation, and neuronal development. Dysregulation of S1P signaling has been implicated in several diseases, such as cancer, inflammation, and cardiovascular disorders.

In summary, sphingosine is a crucial biological compound with medical relevance due to its role as a precursor for various sphingolipids involved in cellular processes and as a precursor for the bioactive lipid mediator S1P.

Phosphoinositide Phospholipase C (PI-PLC) is an enzyme that plays a crucial role in intracellular signaling pathways. It catalyzes the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2), a phospholipid component of the cell membrane, into two second messengers: inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG).

IP3 is responsible for triggering the release of calcium ions from intracellular stores, while DAG remains in the membrane and activates certain protein kinase C (PKC) isoforms. These second messengers then go on to modulate various cellular processes such as gene expression, metabolism, secretion, and cell growth or differentiation. PI-PLC exists in multiple isoforms, which are classified based on their structure and activation mechanisms. They can be activated by a variety of extracellular signals, including hormones, neurotransmitters, and growth factors, making them important components in signal transduction cascades.

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

Glucose-6-phosphate isomerase (GPI) is an enzyme involved in the glycolytic and gluconeogenesis pathways. It catalyzes the interconversion of glucose-6-phosphate (G6P) and fructose-6-phosphate (F6P), which are key metabolic intermediates in these pathways. This reaction is a reversible step that helps maintain the balance between the breakdown and synthesis of glucose in the cell.

In glycolysis, GPI converts G6P to F6P, which subsequently gets converted to fructose-1,6-bisphosphate (F1,6BP) by the enzyme phosphofructokinase-1 (PFK-1). In gluconeogenesis, the reaction is reversed, and F6P is converted back to G6P.

Deficiency or dysfunction of Glucose-6-phosphate isomerase can lead to various metabolic disorders, such as glycogen storage diseases and hereditary motor neuropathies.

Transfection is a term used in molecular biology that refers to the process of deliberately introducing foreign genetic material (DNA, RNA or artificial gene constructs) into cells. This is typically done using chemical or physical methods, such as lipofection or electroporation. Transfection is widely used in research and medical settings for various purposes, including studying gene function, producing proteins, developing gene therapies, and creating genetically modified organisms. It's important to note that transfection is different from transduction, which is the process of introducing genetic material into cells using viruses as vectors.

Insulin is a hormone produced by the beta cells of the pancreatic islets, primarily in response to elevated levels of glucose in the circulating blood. It plays a crucial role in regulating blood glucose levels and facilitating the uptake and utilization of glucose by peripheral tissues, such as muscle and adipose tissue, for energy production and storage. Insulin also inhibits glucose production in the liver and promotes the storage of excess glucose as glycogen or triglycerides.

Deficiency in insulin secretion or action leads to impaired glucose regulation and can result in conditions such as diabetes mellitus, characterized by chronic hyperglycemia and associated complications. Exogenous insulin is used as a replacement therapy in individuals with diabetes to help manage their blood glucose levels and prevent long-term complications.

Tyrosine is an non-essential amino acid, which means that it can be synthesized by the human body from another amino acid called phenylalanine. Its name is derived from the Greek word "tyros," which means cheese, as it was first isolated from casein, a protein found in cheese.

Tyrosine plays a crucial role in the production of several important substances in the body, including neurotransmitters such as dopamine, norepinephrine, and epinephrine, which are involved in various physiological processes, including mood regulation, stress response, and cognitive functions. It also serves as a precursor to melanin, the pigment responsible for skin, hair, and eye color.

In addition, tyrosine is involved in the structure of proteins and is essential for normal growth and development. Some individuals may require tyrosine supplementation if they have a genetic disorder that affects tyrosine metabolism or if they are phenylketonurics (PKU), who cannot metabolize phenylalanine, which can lead to elevated tyrosine levels in the blood. However, it is important to consult with a healthcare professional before starting any supplementation regimen.

Class Ib Phosphatidylinositol 3-Kinases (PI3Ks) are a subclass of PI3K enzymes that play a crucial role in cellular signaling pathways. These enzymes phosphorylate the 3-hydroxyl group of the inositol ring in phosphatidylinositol, creating phosphatidylinositol 3-phosphate (PIP). This lipid second messenger is involved in various cellular processes such as cell growth, proliferation, differentiation, and survival.

The Class Ib PI3Ks are heterodimers composed of a catalytic subunit (p110γ) and a regulatory subunit (p84 or p101). The p110γ catalytic subunit is activated by G protein-coupled receptors (GPCRs) and Ras family small GTPases. Once activated, the p110γ subunit phosphorylates phosphatidylinositol 4,5-bisphosphate (PIP2) to produce PIP3, which in turn recruits downstream signaling proteins containing pleckstrin homology (PH) domains to the plasma membrane.

Abnormal activation of Class Ib PI3Ks has been implicated in various diseases, including cancer and inflammatory disorders. Therefore, targeting these enzymes has emerged as a potential therapeutic strategy for treating these conditions.

Glycerophosphates are esters of glycerol and phosphoric acid. In the context of biochemistry and medicine, glycerophosphates often refer to glycerol 3-phosphate (also known as glyceraldehyde 3-phosphate or glycerone phosphate) and its derivatives.

Glycerol 3-phosphate plays a crucial role in cellular metabolism, particularly in the process of energy production and storage. It is an important intermediate in both glycolysis (the breakdown of glucose to produce energy) and gluconeogenesis (the synthesis of glucose from non-carbohydrate precursors).

In addition, glycerophosphates are also involved in the formation of phospholipids, a major component of cell membranes. The esterification of glycerol 3-phosphate with fatty acids leads to the synthesis of phosphatidic acid, which is a key intermediate in the biosynthesis of other phospholipids.

Abnormalities in glycerophosphate metabolism have been implicated in various diseases, including metabolic disorders and neurological conditions.

Glucose phosphates are organic compounds that result from the reaction of glucose (a simple sugar) with phosphate groups. These compounds play a crucial role in various metabolic processes, particularly in energy metabolism within cells. The addition of phosphate groups to glucose makes it more reactive and enables it to undergo further reactions that lead to the formation of important molecules such as adenosine triphosphate (ATP), which is a primary source of energy for cellular functions.

One notable example of a glucose phosphate is glucose 1-phosphate, which is an intermediate in several metabolic pathways, including glycogenesis (the process of forming glycogen, a storage form of glucose) and glycolysis (the breakdown of glucose to release energy). Another example is glucose 6-phosphate, which is a key regulator of carbohydrate metabolism and serves as an important intermediate in the pentose phosphate pathway, a metabolic route that generates reducing equivalents (NADPH) and ribose sugars for nucleotide synthesis.

In summary, glucose phosphates are essential compounds in cellular metabolism, facilitating energy production, storage, and utilization.

Glycerol-3-Phosphate O-Acyltransferase (GPAT) is an enzyme that plays a crucial role in the biosynthesis of triacylglycerols and phospholipids, which are major components of cellular membranes and energy storage molecules. The GPAT enzyme catalyzes the initial and rate-limiting step in the glycerolipid synthesis pathway, specifically the transfer of an acyl group from an acyl-CoA donor to the sn-1 position of glycerol-3-phosphate, forming lysophosphatidic acid (LPA). This reaction is essential for the production of various glycerolipids, including phosphatidic acid, diacylglycerol, and triacylglycerol. There are four isoforms of GPAT (GPAT1-4) in humans, each with distinct subcellular localizations and functions. Dysregulation of GPAT activity has been implicated in several pathological conditions, such as metabolic disorders, cardiovascular diseases, and cancers.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

PTEN phosphohydrolase, also known as PTEN protein or phosphatase and tensin homolog deleted on chromosome ten, is a tumor suppressor protein that plays a crucial role in regulating cell growth and division. It works by dephosphorylating (removing a phosphate group from) the lipid second messenger PIP3, which is involved in signaling pathways that promote cell proliferation and survival. By negatively regulating these pathways, PTEN helps to prevent uncontrolled cell growth and tumor formation. Mutations in the PTEN gene can lead to a variety of cancer types, including breast, prostate, and endometrial cancer.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Adenosine Triphosphate (ATP) is a high-energy molecule that stores and transports energy within cells. It is the main source of energy for most cellular processes, including muscle contraction, nerve impulse transmission, and protein synthesis. ATP is composed of a base (adenine), a sugar (ribose), and three phosphate groups. The bonds between these phosphate groups contain a significant amount of energy, which can be released when the bond between the second and third phosphate group is broken, resulting in the formation of adenosine diphosphate (ADP) and inorganic phosphate. This process is known as hydrolysis and can be catalyzed by various enzymes to drive a wide range of cellular functions. ATP can also be regenerated from ADP through various metabolic pathways, such as oxidative phosphorylation or substrate-level phosphorylation, allowing for the continuous supply of energy to cells.

... may refer to: Phosphatidylinositol 3-phosphate, also known as PI(3)P Phosphatidylinositol 4- ... phosphate, also known as PI(4)P Phosphatidylinositol 5-phosphate, also known as PI(5)P This disambiguation page lists articles ... associated with the title Phosphatidylinositol phosphate. If an internal link led you here, you may wish to change the link to ...
Type I phosphatidylinositol-4-phosphate 5-kinases synthesize the novel lipids phosphatidylinositol 3,5-bisphosphate and ... Phosphatidylinositol 4-phosphate and PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate). Notably, steady-state PtdIns5P ... Phosphatidylinositol 5-phosphate is one of the 7 known cellular phosphoinositides with less understood functions. It is ... Cutting edge: Dok-1 and Dok-2 adaptor molecules are regulated by phosphatidylinositol 5-phosphate production in T cells. J ...
Phosphatidylinositol-5-phosphate 4-kinase type-2 alpha (PIP4K2A) Phosphatidylinositol-5-phosphate 4-kinase type-2 beta (PIP4K2B ... Phosphatidylinositol-4-phosphate 5-kinases (PIP5Ks, or PI4P5Ks) are a class of enzymes that phosphorylate phosphatidylinositol ... September 2010). "Phosphatidylinositol-4-phosphate 5-kinases and phosphatidylinositol 4,5-bisphosphate synthesis in the brain ... Type I phosphatidylinositol-4-phosphate 5-kinase (PIP5KI) are further classified as PIP5Kα, PIP5Kβ and PIP5Kγ on the basis of ...
... (PtdIns3P) is a phospholipid found in cell membranes that helps to recruit a range of proteins ... Phosphatidylinositol 3-phosphate-binding protein 2 Gillooly DJ, Simonsen A, Stenmark H (April 2001). "Cellular functions of ... Stenmark H, Aasland R, Driscoll PC (February 2002). "The phosphatidylinositol 3-phosphate-binding FYVE finger". FEBS Letters. ... phosphatidylinositol 3-phosphate and FYVE domain proteins". The Biochemical Journal. 355 (Pt 2): 249-58. doi:10.1042/0264-6021: ...
Phosphatidylinositol 3-phosphate Phosphatidylinositol 5-phosphate Phosphatidylinositol (3,4,5)-trisphosphate Godi A et al., ... Phosphatidylinositol-4-phosphate (PtdIns4P, PI-4-P, PI4P, or PIP) is a precursor of phosphatidylinositol (4,5)-bisphosphate. ... "Lipid Membrane Curvature Induced by Distearoyl Phosphatidylinositol 4-Phosphate". Soft Matter. 8 (11): 3090-3093. doi:10.1039/ ... "Pressure-dependent inverse bicontinuous cubic phase formation in a phosphatidylinositol 4-phosphate/phosphatidylcholine system ...
Phosphatidylinositol-4-phosphate 3-kinase Phosphatidylinositol-4,5-bisphosphate 3-kinase Phosphatidylinositol-4-phosphate 5- ... Phosphatidylinositol phosphate kinases (PIPK) are kinases that phosphorylate the phosphoinositides PtdInsP and PtdInsP2 that ... The activation loop of phosphatidylinositol phosphate kinases determines signaling specificity. Mol Cell 2000 5:1-11 v t e ( ... Phosphatidylinositol phosphate kinases, a multifaceted family of signalling enzymes. J Biol Chem 1999; 274:9907-9910 Kunz J, ...
In enzymology, a phosphatidylinositol-4-phosphate 3-kinase (EC 2.7.1.154) is an enzyme that catalyzes the chemical reaction ATP ... The systematic name of this enzyme class is ATP:1-phosphatidyl-1D-myo-inositol-4-phosphate 3-phosphotransferase. Other names in ... This enzyme participates in phosphatidylinositol signaling system. As of late 2007, 3 structures have been solved for this ... the two substrates of this enzyme are ATP and 1-phosphatidyl-1D-myo-inositol 4-phosphate, whereas its two products are ADP and ...
... phosphatidylinositol 4-phosphate kinase, phosphatidylinositol-4-phosphate 5-kinase, and type I PIP kinase. This enzyme ... In enzymology, 1-phosphatidylinositol-4-phosphate 5-kinase (EC 2.7.1.68) is an enzyme that catalyzes the chemical reaction ATP ... The systematic name of this enzyme class is ATP:1-phosphatidyl-1D-myo-inositol-4-phosphate 5-phosphotransferase. Other names in ... participates in 3 metabolic pathways: inositol phosphate metabolism, phosphatidylinositol signaling system, and regulation of ...
... and phosphatidylinositol 3-phosphate 5-kinase. This enzyme participates in phosphatidylinositol signaling system and regulation ... In enzymology, a 1-phosphatidylinositol-3-phosphate 5-kinase (EC 2.7.1.150) is an enzyme that catalyzes the chemical reaction ... "The stress-activated phosphatidylinositol 3-phosphate 5-kinase Fab1p is essential for vacuole function in S. cerevisiae". ... The systematic name of this enzyme class is ATP:1-phosphatidyl-1D-myo-inositol-3-phosphate 5-phosphotransferase. Other names in ...
In enzymology, a 1-phosphatidylinositol-5-phosphate 4-kinase (EC 2.7.1.149) is an enzyme that catalyzes the chemical reaction ... This enzyme participates in 3 metabolic pathways: inositol phosphate metabolism, phosphatidylinositol signaling system, and ... The systematic name of this enzyme class is ATP:1-phosphatidyl-1D-myo-inositol-5-phosphate 4-phosphotransferase. This enzyme is ... Rameh LE, Tolias KF, Duckworth BC, Cantley LC (1997). "A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate". ...
Phosphatidylinositol-4-phosphate 5-kinase type-1 gamma is an enzyme that in humans is encoded by the PIP5K1C gene. This gene ... Ishihara H, Shibasaki Y, Kizuki N, Wada T, Yazaki Y, Asano T, Oka Y (May 1998). "Type I phosphatidylinositol-4-phosphate 5- ... 2007). "Type Igamma phosphatidylinositol phosphate kinase modulates adherens junction and E-cadherin trafficking via a direct ... "Entrez Gene: PIP5K1C phosphatidylinositol-4-phosphate 5-kinase, type I, gamma". "Salmonella infection data for Pip5k1c". ...
Targets of PTPMT-1 include phosphatidylinositol phosphates (PIPs). When PIPs are acted upon by PTPMT-1, the mitochondrial ... Upregulation of glycolysis in proliferative HSCs may drive the pentose phosphate pathway (PPP) to maintain redox balance upon ... The PPP generates nicotinamide adenine dinucleotide phosphate (NADPH), which is a powerful cellular reducing agent. Production ...
Conway SJ, Miller GJ (2007). "Biology-enabling inositol phosphates, phosphatidylinositol phosphates and derivatives". Nat Prod ... The organic phosphate found in phytic acid is largely unavailable to the animals that consume it, but the inorganic phosphate ... phenyl phosphate, fructose 1,6-bisphosphate, glucose 6-phosphate, glycerophosphate and 3-phosphoglycerate. Only a few phytases ... Phytases hydrolyze phosphates from phytic acid in a stepwise manner, yielding products that again become substrates for further ...
"Synthesis and biological evaluation of phosphatidylinositol phosphate affinity probes". Organic & Biomolecular Chemistry. 8 (1 ...
Michell RH, Allan D (1975). "Inositol cyclis phosphate as a product of phosphatidylinositol breakdown by phospholipase C ( ... 2-cyclic-phosphate-forming). Other names in common use include monophosphatidylinositol phosphodiesterase, phosphatidylinositol ... 2-cyclic-phosphate-forming). It participates in inositol phosphate metabolism. As of late 2007, two structures have been solved ... The enzyme phosphatidylinositol diacylglycerol-lyase (EC 4.6.1.13) catalyzes the following reaction: 1-phosphatidyl-1D-myo- ...
Phosphatidylinositol-3-phosphate phosphatase". Retrieved March 7, 2020. Laporte J, Hu LJ, Kretz C, Mandel JL, Kioschis P, Coy ... Myotubularin-related protein 2 also known as phosphatidylinositol-3,5-bisphosphate 3-phosphatase or phosphatidylinositol-3- ... "RecName: Full=Myotubularin-related protein 2; AltName: Full=Phosphatidylinositol-3,5-bisphosphate 3-phosphatase; AltName: Full= ... phosphate phosphatase is a protein that in humans is encoded by the MTMR2 gene. This gene is a member of the myotubularin ...
Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing alpha polypeptide is an enzyme that in humans is encoded by the ... A source of phosphatidylinositol 3-phosphate". J. Biol. Chem. 273 (23): 14081-14084. doi:10.1074/jbc.273.23.14081. PMID 9603905 ... Cook JA, August A, Henderson AJ (2002). "Recruitment of phosphatidylinositol 3-kinase to CD28 inhibits HIV transcription by a ... 1998). "Extracellular HIV-1 Tat protein activates phosphatidylinositol 3- and Akt/PKB kinases in CD4+ T lymphoblastoid Jurkat ...
... is a cell organelle consisting of lipid bilayer membranes enriched for phosphatidylinositol 3-phosphate (abbreviated ... Nascimbeni, Anna Chiara; Codogno, Patrice; Morel, Etienne (2017). "Phosphatidylinositol-3-phosphate in the regulation of ... 2008). "Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically ...
"Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells". EMBO J. 19 (17): 4577-88. doi:10.1093/emboj/ ...
Phosphatidylinositol-5-phosphate 4-kinase, type II, gamma is an enzyme in humans that is encoded by the PIP4K2C gene. It is one ... "Entrez Gene: Phosphatidylinositol-5-phosphate 4-kinase, type II, gamma". PDBe-KB provides an overview of all the structure ... of the phosphatidylinositol 4-phosphate 5-kinases. GRCh38: Ensembl release 89: ENSG00000166908 - Ensembl, May 2017 GRCm38: ... information available in the PDB for Human Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma (PIP4K2C) Portal: Biology v t ...
September 2006). "Fab1 phosphatidylinositol 3-phosphate 5-kinase controls trafficking but not silencing of endocytosed ... PIKfyve activity is responsible for the production of both PtdIns(3,5)P2 and phosphatidylinositol 5-phosphate (PtdIns5P). ... Sbrissa D, Ikonomov OC, Deeb R, Shisheva A (December 2002). "Phosphatidylinositol 5-phosphate biosynthesis is linked to PIKfyve ... Sbrissa D, Ikonomov OC, Deeb R, Shisheva A (December 2002). "Phosphatidylinositol 5-phosphate biosynthesis is linked to PIKfyve ...
PIP2 is formed primarily by the type I phosphatidylinositol 4-phosphate 5-kinases from PI(4)P. In metazoans, PIP2 can also be ... 2005). "Phosphatidylinositol phosphate kinase type Iγ regulates dynamics of large dense-core vesicle fusion". PNAS. 102 (14): ... Bulley SJ, Clarke JH, Droubi A, Giudici ML, Irvine RF (2015). "Exploring phosphatidylinositol 5-phosphate 4-kinase function". ... Phosphatidylinositol 4,5-bisphosphate or PtdIns(4,5)P2, also known simply as PIP2 or PI(4,5)P2, is a minor phospholipid ...
"Entrez Gene: PIP5K2A phosphatidylinositol-4-phosphate 5-kinase, type II, alpha". Xu H, Yang W, Perez-Andreu V, Devidas M, Fan Y ... Phosphatidylinositol-5-phosphate 4-kinase type-2 alpha is an enzyme that in humans is encoded by the PIP4K2A gene. ... This gene is a member of the phosphatidylinositol-4-phosphate 5-kinase family. Through genome wide association studies (GWAS), ... Overview of all the structural information available in the PDB for UniProt: P48426 (Phosphatidylinositol 5-phosphate 4-kinase ...
Ling K, Doughman RL, Firestone AJ, Bunce MW, Anderson RA (Nov 2002). "Type I gamma phosphatidylinositol phosphate kinase ... "Recruitment and regulation of phosphatidylinositol phosphate kinase type 1 gamma by the FERM domain of talin". Nature. 420 ( ...
This enzyme participates in inositol phosphate metabolism and phosphatidylinositol signaling system. Howell S, Barnaby RJ, Rowe ... 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate This enzyme belongs to the family of hydrolases, specifically those ... The enzyme phosphatidylinositol-3,4-bisphosphate 4-phosphatase (EC 3.1.3.66) that catalyzes the reaction 1-phosphatidyl-myo- ...
This enzyme participates in inositol phosphate metabolism and phosphatidylinositol signaling system. As of late 2007, the ... phosphatidylinositol 4-kinase, phosphatidylinositol kinase, type II phosphatidylinositol kinase, PI kinase, and PI 4-kinase. ... phosphatidylinositol-3-phosphate". Nature. 332 (6165): 644-6. Bibcode:1988Natur.332..644W. doi:10.1038/332644a0. PMID 2833705. ... In enzymology, a 1-phosphatidylinositol 4-kinase (EC 2.7.1.67) is an enzyme that catalyzes the chemical reaction ATP + 1- ...
This enzyme participates in inositol phosphate metabolism and phosphatidylinositol signaling system. As of late 2007, 3 ...
Phosphatidylinositol-4-phosphate 5-kinase type-1 alpha is an enzyme that in humans is encoded by the PIP5K1A gene. GRCh38: ... "Entrez Gene: PIP5K1A phosphatidylinositol-4-phosphate 5-kinase, type I, alpha". Honda A, Nogami M, Yokozeki T, et al. (1999). " ... 2000). "Type I phosphatidylinositol 4-phosphate 5-kinase directly interacts with ADP-ribosylation factor 1 and is responsible ... Xie Y, Zhu L, Zhao G (Jun 2000). "Assignment of type I phosphatidylinositol-4-phosphate 5-kinase (PIP5K1A) to human chromosome ...
Phosphatidylinositol-5-phosphate 4-kinase type-2 beta is an enzyme that in humans is encoded by the PIP4K2B gene. The protein ... "Entrez Gene: PIP5K2B phosphatidylinositol-4-phosphate 5-kinase, type II, beta". Bultsma, Yvette; Keune, Willem-Jan; Divecha, ... This gene is a member of the phosphatidylinositol-4-phosphate 5-kinase family. The encoded protein sequence does not show ... 2007). "Genomic tagging of endogenous type IIbeta phosphatidylinositol 5-phosphate 4-kinase in DT40 cells reveals a nuclear ...
... phosphatidylinositol 3-phosphate, are present in Saccharomyces cerevisiae". J. Biol. Chem. 264 (34): 20181-4. doi:10.1016/S0021 ... phosphatidylinositol-3-phosphate". Nature. 332 (6165): 644-6. Bibcode:1988Natur.332..644W. doi:10.1038/332644a0. PMID 2833705. ... Whitman M, Downes CP, Keeler M, Keller T, Cantley L (April 1988). "Type I phosphatidylinositol kinase makes a novel inositol ... Yoakim M, Hou W, Songyang Z, Liu Y, Cantley L, Schaffhausen B (September 1994). "Genetic analysis of a phosphatidylinositol 3- ...
Phosphatidylinositol phosphate may refer to: Phosphatidylinositol 3-phosphate, also known as PI(3)P Phosphatidylinositol 4- ... phosphate, also known as PI(4)P Phosphatidylinositol 5-phosphate, also known as PI(5)P This disambiguation page lists articles ... associated with the title Phosphatidylinositol phosphate. If an internal link led you here, you may wish to change the link to ...
Pik3c2a phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 alpha... Pik3c2a phosphatidylinositol-4-phosphate 3- ... phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha. Names. PI3K-C2-alpha. p170. phosphatidylinositol ... phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 alphaprovided by MGI. Primary source. MGI:MGI:1203729 See ... enables 1-phosphatidylinositol-4-phosphate 3-kinase activity IBA Inferred from Biological aspect of Ancestor. more info ...
GK4, a G-protein-coupled receptor with a phosphatidylinositol phosphate kinase domain in Phytophthora infestans, is involved in ... domain fused to a phosphatidylinositol phosphate kinase (PIPK) domain. Based on this domain structure GKs are anticipated to ...
Phosphatidylinositol Phosphate PIP Antibody 01010822270 at Gentaur Phosphatidylinositol Phosphate (PIP) ...
Effects of biophysical membrane properties on recognition of phosphatidylserine, or phosphatidylinositol 4-phosphate by lipid ... or phosphatidylinositol 4-phosphate (PI4P), respectively. Dual-color fluorescence cross-correlation spectroscopy, employed in ...
involved_in phosphatidylinositol acyl-chain remodeling IBA Inferred from Biological aspect of Ancestor. more info ... 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon. Names. 1-AGP acyltransferase 5. 1-AGPAT 5. 1-acylglycerol-3-phosphate O ... Agpat5 1-acylglycerol-3-phosphate O-acyltransferase 5 [Mus musculus] Agpat5 1-acylglycerol-3-phosphate O-acyltransferase 5 [Mus ... 1-acylglycerol-3-phosphate O-acyltransferase 5provided by MGI. Primary source. MGI:MGI:1196345 See related. Ensembl: ...
Phosphatidylinositol phosphate kinase type Iγ directly associates with and regulates Shp-1 tyrosine phosphatase. ... Dive into the research topics of Phosphatidylinositol phosphate kinase type Iγ directly associates with and regulates Shp-1 ...
... that mediate arsenite induction of spindle abnormalities resulted in the identification of phosphatidylinositol-5-phosphate 4- ... kinase type-2 gamma (PIP4KIIγ), a phosphatidylinositol 4,5-bisphosphate (PIP2)-synthesizing enzyme. In this study, we explored ... Analysis of phosphatidylinositol phosphate (PIP) binding with PLK1. The binding of each phosphatidylinositol phosphate (PIP) to ... and also from phosphatidylinositol 5-phosphate (PI5P) by phosphatidylinositol 5-phosphate 4-kinase type II (PIP4KII); PIP2 is ...
Phosphatidylinositol 4-phosphate 5-kinase type I g (PIPKIγ90) regulates cell migration, invasion, and metastasis. However, it ... N2 - Phosphatidylinositol 4-phosphate 5-kinase type I g (PIPKIγ90) regulates cell migration, invasion, and metastasis. However ... AB - Phosphatidylinositol 4-phosphate 5-kinase type I g (PIPKIγ90) regulates cell migration, invasion, and metastasis. However ... abstract = "Phosphatidylinositol 4-phosphate 5-kinase type I g (PIPKIγ90) regulates cell migration, invasion, and metastasis. ...
Phosphatidylinositol phosphate 5-kinase Iγ and phosphoinositide 3-kinase/Akt signaling couple to promote oncogenic growth. In: ... Phosphatidylinositol phosphate 5-kinase Iγ and phosphoinositide 3-kinase/Akt signaling couple to promote oncogenic growth. ... Phosphatidylinositol phosphate 5-kinase Iγ and phosphoinositide 3-kinase/Akt signaling couple to promote oncogenic growth. / ... Thapa, N., Choi, S., Tan, X., Wise, T., & Anderson, R. A. (2015). Phosphatidylinositol phosphate 5-kinase Iγ and ...
Phosphatidylinositol 3-phosphate. SMURF1:. Smad ubiquitin regulatory factor 1. cMyc:. Avian myelocytomatosis virus oncogene ... the ATG1/ULK1 and the Class III phosphatidylinositol 3-kinase (PI3K) complex (Figure 1) [5]. First, phagophore formation ...
PIP5K1B: phosphatidylinositol-4-phosphate 5-kinase type-1 beta. *PLAA: phospholipase A-2-activating protein ...
Rubicon activates phosphatidylinositol 3-phosphate (PI3P) synthesis, which in turn, stimulates ROS production. PI3P and ROS ... in association with Atg14 and type III phosphatidylinositol 3-kinase Vps34, promote the formation of a cup-shaped isolation ... pneumophila translocates a sphingosine-1 phosphate lyase into the cytosol to alter sphingosine metabolism implicated in ...
Baskaran S, Ragusa MJ, Boura E, Hurley JH . Two-site recognition of phosphatidylinositol 3-phosphate by PROPPINs in autophagy. ... They contain seven-bladed β-propellers formed by seven WD40 repeats and bind to phosphatidylinositol 3-phosphate and the ... Atg18/WIPIs are recruited to the autophagosome formation site through binding to phosphatidylinositol 3-phosphate, which is ... The Atg18-Atg2 complex is recruited to autophagic membranes via phosphatidylinositol 3-phosphate and exerts an essential ...
Phosphatidylinositol 4-phosphate is a major source of GPCR-stimulated phosphoinositide production.﻽. de Rubio RG, Ransom RF, ... Phospholipase C? hydrolyzes perinuclear phosphatidylinositol 4-phosphate to regulate cardiac hypertrophy.﻽. Zhang L, Malik S, ...
... and here we report that PEP1 consists of the type I phosphatidylinositol-4-phosphate 5-kinase (PtdInsP5K). The roles of PEP3/ ... PEP3 was recently identified as phosphatidylinositol transfer protein (PtdInsTP), ...
VIPP1 rods engulf membranes containing phosphatidylinositol phosphates. SCIENTIFIC REPORTS 9, 8725 (2019) ...
Here we report that clathrin and phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2) regulate ALR. Combining a screen of ... Their analyses reveal a key role for clathrin and phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2) in this process. ... Phosphatidylinositol-4-phosphate 5-kinases and phosphatidylinositol 4,5-bisphosphate synthesis in the brain. J. Biol. Chem. 285 ... Figure 4: Phosphatidylinositol-4-phosphate 5-kinase (PIP5K1A) is required for proto-lysosome budding during ALR.. ...
2014) Yeast and mammalian autophagosomes exhibit distinct phosphatidylinositol 3-phosphate asymmetries. Nat Commun 5:3207. ... 2013) Phosphatidylinositol 4,5-bisphosphate clusters act as molecular beacons for vesicle recruitment. Nat Struct Mol Biol 20: ... Phosphatidylinositol-4,5-bisphosphate (PI(4,5)P2) plays an essential role in neuronal activities through interaction with ... 2008) Analysis of phosphatidylinositol-4,5-bisphosphate signaling in cerebellar Purkinje spines. Biophys J 95:1795-1812. https ...
GPI ethanolamine phosphate transferase 3. Synonyms. *PIG-O. *Phosphatidylinositol-glycan biosynthesis class O protein ... Transfers ethanolamine phosphate to the GPI third mannose which links the GPI-anchor to the C-terminus of the proteins by an ... Showing Protein GPI ethanolamine phosphate transferase 3 (HMDBP07329). IdentificationBiological propertiesGene properties ... Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. ...
phosphatidylinositol 3-kinase. PBS. phosphate-buffered saline. PKC. protein kinase C. K-H. Krebs-Henseleit bicarbonate buffer. ... Quercetin Inhibits Shc- and Phosphatidylinositol 3-Kinase-Mediated c-Jun N-Terminal Kinase Activation by Angiotensin II in ... Quercetin also inhibited Ang II-induced Shc·p85 association and subsequent activation of phosphatidylinositol 3-kinase (PI3-K)/ ... Quercetin Inhibits Shc- and Phosphatidylinositol 3-Kinase-Mediated c-Jun N-Terminal Kinase Activation by Angiotensin II in ...
We have previously shown phosphatidylinositol-3-phosphate (PI3P) accumulation in animal models of MTM. Here, we tested the ...
Putative Homology: phosphatidylinositol-4-phosphate 5-kinase Annotation Keywords: signal transduction; inositol triphosphate ... Phosphatidylinositol-4-phosphate 5-kinase 9 OS=Arabidopsis thaliana GN=PIP5K9 PE=1 SV=2. ... Symbols: PIP5K9 , PIP5K9 (PHOSPHATIDYL INOSITOL MONOPHOSPHATE 5 KINASE); 1-phosphatidylinosito…. swissprot. blastx. Q8L850. 776 ...
phosphatidylinositol-5-phosphate 4-kinase type 2 alpha. involved_in. ISS. IEA. ISO. GO_REF:0000024. GO_REF:0000107. (PMID: ...
Phosphatidylinositol 5 Phosphate 4-Kinase Regulates Plasma-Membrane PIP Turnover and Insulin Signaling.. Cell Rep. 27(7):1979- ... PI3P-dependent regulation of cell size and autophagy by phosphatidylinositol 5-phosphate 4-kinase.. Life Sci Alliance. 6(9)* ... Phosphatidylinositol 5-phosphate 4-kinase regulates early endosomal dynamics during clathrin-mediated endocytosis.. J Cell Sci ... A novel mass assay to measure phosphatidylinositol-5-phosphate from cells and tissues.. Biosci Rep. 39(10)*PubMed ...
Additionally, several phosphatidylinositols were identified. Phosphatidylinositol-4-phosphate was the strongest binding partner ... Als stärkster M1 Bindungspartner trat dabei Phosphatidylinositol-4-Phosphat zutage. Weitere auf Mutanten basierende ...
3b). Additionally, genes coding for phosphatidylinositol 4-phosphate 5-kinase (PIP5K), myo-inositol 1-phosphate synthase (MIPS ... phosphatidylinositol 4-phosphate 5-kinase, PIP5K; myo-inositol 1-phosphate synthase, MIPS; type II inositol 1,4,5-trisphosphate ... Isopentenyl phosphate kinase. 2.7.4.26. 3.00 e−20. 26. 49. Terpenoid backbone. ... f) Products of genes involved in glycolysis are indicated as follows: glucose-6-phosphate isomerase, G6PI; fructose- ...
Investigations of kindlinâ€"2 binding to phosphatidylinositol phosphates in lipid bilayers. Date:. Wednesday, 22 March 2023. ...
phosphatidylinositol-4-phosphate 5-kinase type 1 gamma. ISO. RGD. PMID:22763746. RGD:10450547. NCBI chr 7:8,397,406...8,426,030 ...
  • Phospholipase C activity was estimated by measuring the production of [3H]inositol phosphates by [3H]inositol-labelled dispersed pinealocytes in suspension culture. (nih.gov)
  • This review summarizes our current understanding of the mechanisms by which inositol phosphates regulate cytoplasmic Ca2+ concentrations. (nih.gov)
  • Binds phosphatidyl inositol phosphates (in vitro). (nih.gov)
  • Here we show that Mycobacterium smegmatis and other Actinomycetes bacteria can synthesize the phosphoinositide, phosphatidylinositol 3-phosphate (PI3P). (umass.edu)
  • Synthesis of PI3P in a cell-free system was stimulated by the synthesis of CDP-diacylglycerol, a lipid substrate for phosphatidylinositol (PI) biosynthesis, suggesting that efficient cell-free PI3P synthesis is dependent on de novo PI synthesis. (umass.edu)
  • We have previously shown phosphatidylinositol-3-phosphate (PI3P) accumulation in animal models of MTM. (jci.org)
  • PI3P-dependent regulation of cell size and autophagy by phosphatidylinositol 5-phosphate 4-kinase. (ncbs.res.in)
  • A majority of PX domain containing proteins binds phosphatidylinositol-3-phosphate (PI3P) at this site. (nih.gov)
  • The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. (embl-heidelberg.de)
  • ATG16L1 harbours an intrinsic ability to bind autophagy related membranes through direct interaction with phosphatidylinositol‐3‐phosphate (PI3P). (ed.ac.uk)
  • PIKFYVE belongs to a large family of lipid kinases that alter the phosphorylation status of intracellular phosphatidylinositol. (thermofisher.com)
  • PIP5K catalyses the formation of phosphoinositol-4,5-bisphosphate via the phosphorylation of phosphatidylinositol-4-phosphate a precursor in the phosphinositide signalling pathway. (embl.de)
  • The protein encoded by this gene catalyzes the phosphorylation of phosphatidylinositol-5-phosphate on the fourth hydroxyl of the myo-inositol ring to form phosphatidylinositol-5,4-bisphosphate. (antibodies-online.com)
  • Although binding of VAMP3 to PI4K2A did not require kinase activity, acute depletion of phosphatidylinositol 4-phosphate (PtdIns4P) on endosomes significantly delayed VAMP3 trafficking. (nih.gov)
  • MTM1 is a phosphoinositide phosphatase hydrolyzing phosphatidylinositol 3-phosphate (PtdIns(3)P) in yeast and in vitro. (nih.gov)
  • Sensitivity of the purified lipid to alkaline phosphatase, headgroup analysis by high-pressure liquid chromatography, and mass spectrometry demonstrated that it had the structure 1,2-[tuberculostearoyl, octadecenoyl]-sn-glycero 3-phosphoinositol 3-phosphate. (umass.edu)
  • Myotubularin is primarily a lipid phosphatase that acts on hosphatidylinositol 3-monophosphate and is involved in the regulation of the phosphatidylinositol 3-kinase (PI 3-kinase) pathway and membrane trafficking. (thermofisher.com)
  • Myotubularin, a phosphatase deficient in myotubular myopathy, acts on phosphatidylinositol 3-kinase and phosphatidylinositol 3-phosphate pathway. (igbmc.fr)
  • 9] "The phosphatidylinositol 3-phosphate phosphatase myotubularin-related protein 6 (MTMR6) is a negative regulator of the Ca2+-activated K+ channel KCa3.1. (tcdb.org)
  • Using a mass assay, we demonstrated that the product generated is phosphatidylinositol 5-phosphate (PtdIns(5)P), a recently discovered phosphoinositide, the function of which is still unknown. (nih.gov)
  • Based on the theory that the phosphoinositide (PI) signal is involved in the physiology of cornea and conjunctiva , we examined the localization in the mouse anterior ocular epithelia of immunoreactivities for phosphatidylinositol 4- phosphate 5- kinase (PIP5K), phospholipase C (PLC) and diacylglycerol kinase (DGK), enzymes that work sequentially in PI cycle. (bvsalud.org)
  • A primary focus is on Arf6, which coordinates membrane traffic and the actin cytoskeleton at the plasma membrane (PM). In the active, GTP-bound state, Arf6 activates phosphatidylinositol 4-phosphate 5-kinase, an enzyme that generates phosphatidylinositol 4,5-bisphosphate (PIP2), a major PM phosphoinositide. (nih.gov)
  • The HF diet group had significantly increased abundance of triglycerides and phosphatidylinositol lipids, as well as decreased lysophosphatidic lipids and cardiolipin. (cdc.gov)
  • In this study, we identified phosphatidylinositol 4-kinase IIα (PI4K2A) as a binding partner of vesicle-associated membrane protein 3 (VAMP3), a small R-SNARE involved in recycling and retrograde transport, and found that the two proteins co-reside on tubulo-vesicular endosomes. (nih.gov)
  • Emerging perspectives on multidomain phosphatidylinositol transfer proteins. (ncbs.res.in)
  • Most FYVE domains target proteins to endosomes by binding specifically to phosphatidylinositol-3-phosphate at the membrane surface. (embl-heidelberg.de)
  • PITPNM1 belongs to a family of membrane-associated phosphatidylinositol transfer domain-containing proteins that share homology with the Drosophila retinal degeneration B (rdgB) protein (Ocaka et al. (nih.gov)
  • 3. Treatment of DNA polymerase alpha A1 with the phospholipase C hydrolysis product of phosphatidylinositol-4-monophosphate, inositol-1,4-bisphosphate, was sufficient to effect the transient increase in activity of polymerase A1 to a form not chromatographically distinguishable from isozyme form A2. (nih.gov)
  • this was blocked by alpha 1-adrenergic antagonists, including prazosin, WB 4101, and phenoxybenzamine, but by neither an alpha 2- nor a beta-adrenergic antagonist, confirming that an alpha 1-adrenoceptor is involved in the regulation of phosphatidylinositol hydrolysis. (nih.gov)
  • It is well established that phosphatidylinositol 4,5-bisphosphate hydrolysis is responsible for the changes in Ca2+ homeostasis. (nih.gov)
  • Stimulation of Ca2(+)-mobilizing receptors also results in the phospholipase C-catalyzed hydrolysis of the minor plasma membrane phospholipid, phosphatidylinositol 4,5-bisphosphate, with the concomitant formation of inositol (1,4,5) trisphosphate [1,4,5)IP3) and diacylglycerol. (nih.gov)
  • A strong body of evidence suggests that a large network of signaling enzymes, called lipid kinases, can add phosphate tags onto components of cellular membranes and are essential hubs for regulating cell metabolism. (europa.eu)
  • The content of phosphatidylinositol 3,5-bisphosphateP2) in endosomal membranes changes dynamically with fission and fusion events that generate or absorb intracellular transport vesicles. (thermofisher.com)
  • May catalyze the transfer of phosphatidylinositol and phosphatidylcholine between membranes (By similarity). (nih.gov)
  • Two basic residues are key in binding with phosphoinositides: one forms hydrogen bonds with the 3-phosphate of PI(3)P and another forms hydrogen bonds with the 4-and 5-hydroxyl groups of PI(3)P. (nih.gov)
  • They identified a site on the coiled‐coil domain of ATG16L1 required for binding to phosphatidylinositol‐3‐phosphate and other phosphoinositides. (ed.ac.uk)
  • 7. HS-116, a novel phosphatidylinositol 3-kinase inhibitor induces apoptosis and suppresses angiogenesis of hepatocellular carcinoma through inhibition of the PI3K/AKT/mTOR pathway. (nih.gov)
  • 10. Targeting the phosphatidylinositol 3-kinase pathway in multiple myeloma. (nih.gov)
  • Ceramide-1-phosphate was found at higher abundance in the regular (REG) diet WF-exposed group which has been shown to regulate the eicosanoid pathway involved in pro-inflammatory response. (cdc.gov)
  • Localization of phosphatidylinositol phosphate 5 kinase γ, phospholipase ß3 and diacylglycerol kinase ζ in corneal epithelium in comparison with conjunctival epithelium of mice. (bvsalud.org)
  • Activation of alpha 1-adrenergic receptors increases [Ca+2]i and phosphatidylinositol phosphodiesterase (phospholipase C) activity in the pinealocyte. (nih.gov)
  • Phosphatidylinositol (PI) 3-kinase (encoded by the pik3(+) gene) in Schizosaccharomyces pombe has been identified as a homologue of VPS34p, a protein required for proper vesicular protein sorting. (duke.edu)
  • The altered protein is less able to add ethanolamine phosphate to the end of GPI anchors. (medlineplus.gov)
  • Towards understanding non-canonical phosphatidylinositol kinases in the maintenance of prostate metabolism. (europa.eu)
  • 20. Phosphatidylinositol 4-kinases, phosphatidylinositol 4-phosphate and cancer. (nih.gov)
  • This region is found in I, II and III phosphatidylinositol-4-phosphate 5-kinases (PIP5K enzymes). (embl.de)
  • AKT is activated by phosphatidylinositol 3-phosphate (PIP3), which is produced by PI(3)kinases (PI3K). (nih.gov)
  • Scholars@Duke publication: Role of phosphatidylinositol 3-phosphate in formation of forespore membrane in Schizosaccharomyces pombe. (duke.edu)
  • Phosphatidylinositol 5 Phosphate 4-Kinase Regulates Plasma-Membrane PIP Turnover and Insulin Signaling. (ncbs.res.in)
  • Phosphatidylinositol 3-kinase (PI3-K) may regulate the basal plasma membrane glucose transporter recycling and the organization of the transporter intracellular pool in addition to being an insulin signal for translocation of glucose transporters to the plasma membrane. (diabetesjournals.org)
  • A novel mass assay to measure phosphatidylinositol-5-phosphate from cells and tissues. (ncbs.res.in)
  • However, in addition to PtdIns(3)P, we found that MTM1 can hydrolyze phosphatidylinositol 3,5-bisphosphate both in vitro and in mammalian cells. (nih.gov)
  • Functional analysis of the biochemical activity of mammalian phosphatidylinositol 5 phosphate 4-kinase enzymes. (ncbs.res.in)
  • In stable cultured cell lines, acute exposure to TNF brings about a decrease in the association of phosphatidylinositol (PI) 3-kinase and insulin receptor substrate (IRS)-1 after insulin treatment ( 7 ). (diabetesjournals.org)
  • A selective inhibitor of phosphatidylinositol-4-phosphate 5-kinase (PIP5K) which demonstrates anti-cancer activity. (cancertools.org)
  • 601 1-acyl-sn-glycerol-3-phosphate acyltransferase plsC BBZA01000001 CDS ARMA_0002 604. (go.jp)
  • SAC1 regulates autophagosomal phosphatidylinositol-4-phosphate for xenophagy-directed bacterial clearance. (broadinstitute.org)
  • The PIGO gene provides instructions for making one part of an enzyme called GPI ethanolamine phosphate transfer 3 (GPI-ET3). (medlineplus.gov)
  • Specifically, this enzyme adds a molecule of ethanolamine phosphate to the end of the forming GPI anchor. (medlineplus.gov)
  • The chemical reactions and pathways resulting in the formation of phosphatidylinositol phosphate. (planteome.org)
  • 1. The role of phosphatidylinositol 3-kinase signaling pathways in pancreatic cancer. (nih.gov)
  • Emerging cell biological functions of phosphatidylinositol 5 phosphate 4 kinase. (ncbs.res.in)
  • 2. DNA polymerase alpha A1, but not A2, showed a significant increase in specific activity after treatment with phosphatidylinositol, ATP and phosphatidylinositol kinase, or with phosphatidylinositol-4-monophosphate. (nih.gov)
  • Inositol phosphate formation and its relationship to calcium signaling. (nih.gov)
  • Rickets in children or osteomalacia in adults is the result of the excessive urinary losses of calcium and phosphate and of a defect in the hydroxylation of 25-hydroxyvitamin D3 into 1,25-dihydroxyvitamin D3. (medscape.com)
  • Stress-induced synthesis of phosphatidylinositol 3-phosphate in mycobacteria. (umass.edu)
  • Phosphatidylinositols in which one or more alcohol group of the inositol has been substituted with a phosphate group. (nih.gov)
  • Link to all annotated objects annotated to phosphatidylinositol phosphate biosynthetic process. (planteome.org)
  • Link to all direct and indirect annotations to phosphatidylinositol phosphate biosynthetic process. (planteome.org)
  • this process requires the ethanolamine phosphate at the end of the anchor. (medlineplus.gov)