Acid Phosphatase: An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.2.Phosphoprotein Phosphatases: A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992)TartratesProtein Tyrosine Phosphatases: An enzyme group that specifically dephosphorylates phosphotyrosyl residues in selected proteins. Together with PROTEIN-TYROSINE KINASE, it regulates tyrosine phosphorylation and dephosphorylation in cellular signal transduction and may play a role in cell growth control and carcinogenesis.Protein Phosphatase 2: A phosphoprotein phosphatase subtype that is comprised of a catalytic subunit and two different regulatory subunits. At least two genes encode isoforms of the protein phosphatase catalytic subunit, while several isoforms of regulatory subunits exist due to the presence of multiple genes and the alternative splicing of their mRNAs. Protein phosphatase 2 acts on a broad variety of cellular proteins and may play a role as a regulator of intracellular signaling processes.Protein Phosphatase 1: A eukayrotic protein serine-threonine phosphatase subtype that dephosphorylates a wide variety of cellular proteins. The enzyme is comprised of a catalytic subunit and regulatory subunit. Several isoforms of the protein phosphatase catalytic subunit exist due to the presence of multiple genes and the alternative splicing of their mRNAs. A large number of proteins have been shown to act as regulatory subunits for this enzyme. Many of the regulatory subunits have additional cellular functions.Phosphoric Monoester Hydrolases: A group of hydrolases which catalyze the hydrolysis of monophosphoric esters with the production of one mole of orthophosphate. EC 3.1.3.Glucose-6-Phosphatase: An enzyme that catalyzes the conversion of D-glucose 6-phosphate and water to D-glucose and orthophosphate. EC 3.1.3.9.Lysosomes: A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured. Such rupture is supposed to be under metabolic (hormonal) control. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)Isoenzymes: Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.Phosphatidate Phosphatase: A phosphomonoesterase involved in the synthesis of triacylglycerols. It catalyzes the hydrolysis of phosphatidates with the formation of diacylglycerols and orthophosphate. EC 3.1.3.4.Histocytochemistry: Study of intracellular distribution of chemicals, reaction sites, enzymes, etc., by means of staining reactions, radioactive isotope uptake, selective metal distribution in electron microscopy, or other methods.Prostate: A gland in males that surrounds the neck of the URINARY BLADDER and the URETHRA. It secretes a substance that liquefies coagulated semen. It is situated in the pelvic cavity behind the lower part of the PUBIC SYMPHYSIS, above the deep layer of the triangular ligament, and rests upon the RECTUM.Osteoclasts: A large multinuclear cell associated with the BONE RESORPTION. An odontoclast, also called cementoclast, is cytomorphologically the same as an osteoclast and is involved in CEMENTUM resorption.Phosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.Molecular Sequence Data: 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.Dual-Specificity Phosphatases: A sub-class of protein tyrosine phosphatases that contain an additional phosphatase activity which cleaves phosphate ester bonds on SERINE or THREONINE residues that are located on the same protein.Protein Tyrosine Phosphatase, Non-Receptor Type 11: A subtype of non-receptor protein tyrosine phosphatases that contain two SRC HOMOLOGY DOMAINS. Mutations in the gene for protein tyrosine phosphatase, non-receptor type 11 are associated with NOONAN SYNDROME.cdc25 Phosphatases: A subclass of dual specificity phosphatases that play a role in the progression of the CELL CYCLE. They dephosphorylate and activate CYCLIN-DEPENDENT KINASES.Protein Tyrosine Phosphatase, Non-Receptor Type 1: A subtype of non-receptor protein tyrosine phosphatases that includes two distinctive targeting motifs; an N-terminal motif specific for the INSULIN RECEPTOR, and a C-terminal motif specific for the SH3 domain containing proteins. This subtype includes a hydrophobic domain which localizes it to the ENDOPLASMIC RETICULUM.Amino Acid Sequence: 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.Phosphates: Inorganic salts of phosphoric acid.Protein Tyrosine Phosphatase, Non-Receptor Type 6: A Src-homology domain-containing protein tyrosine phosphatase found in the CYTOSOL of hematopoietic cells. It plays a role in signal transduction by dephosphorylating signaling proteins that are activated or inactivated by PROTEIN-TYROSINE KINASES.Okadaic Acid: A specific inhibitor of phosphoserine/threonine protein phosphatase 1 and 2a. It is also a potent tumor promoter. (Thromb Res 1992;67(4):345-54 & Cancer Res 1993;53(2):239-41)Myosin-Light-Chain Phosphatase: A phosphoprotein phosphatase that is specific for MYOSIN LIGHT CHAINS. It is composed of three subunits, which include a catalytic subunit, a myosin binding subunit, and a third subunit of unknown function.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Kinetics: The rate dynamics in chemical or physical systems.Alkaline Phosphatase: An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.1.Protein Tyrosine Phosphatases, Non-Receptor: A subcategory of protein tyrosine phosphatases that occur in the CYTOPLASM. Many of the proteins in this category play a role in intracellular signal transduction.Phosphorylase Phosphatase: An enzyme that deactivates glycogen phosphorylase a by releasing inorganic phosphate and phosphorylase b, the inactive form. EC 3.1.3.17.Bone Resorption: Bone loss due to osteoclastic activity.GlucuronidaseHydrogen-Ion Concentration: The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Receptor-Like Protein Tyrosine Phosphatases, Class 2: A subclass of receptor-like protein tryosine phosphatases that contain multiple extracellular immunoglobulin G-like domains and fibronectin type III-like domains. An additional memprin-A5-mu domain is found on some members of this subclass.Ethers, Cyclic: Compounds of the general formula R-O-R arranged in a ring or crown formation.Dual Specificity Phosphatase 1: A dual specificity phosphatase subtype that plays a role in intracellular signal transduction by inactivating MITOGEN-ACTIVATED PROTEIN KINASES. It has specificity for P38 MITOGEN-ACTIVATED PROTEIN KINASES and JNK MITOGEN-ACTIVATED PROTEIN KINASES.RANK Ligand: A transmembrane protein belonging to the tumor necrosis factor superfamily that specifically binds RECEPTOR ACTIVATOR OF NUCLEAR FACTOR-KAPPA B and OSTEOPROTEGERIN. It plays an important role in regulating OSTEOCLAST differentiation and activation.Microscopy, Electron: Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.4-Nitrophenylphosphatase: An enzyme that catalyzes the hydrolysis of nitrophenyl phosphates to nitrophenols. At acid pH it is probably ACID PHOSPHATASE (EC 3.1.3.2); at alkaline pH it is probably ALKALINE PHOSPHATASE (EC 3.1.3.1). EC 3.1.3.41.Thymolphthalein: Used as a pH indicator and as a reagent for blood after decolorizing the alkaline solution by boiling with zinc dust.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.NitrophenolsBone and Bones: A specialized CONNECTIVE TISSUE that is the main constituent of the SKELETON. The principle cellular component of bone is comprised of OSTEOBLASTS; OSTEOCYTES; and OSTEOCLASTS, while FIBRILLAR COLLAGENS and hydroxyapatite crystals form the BONE MATRIX.EsterasesVanadates: Oxyvanadium ions in various states of oxidation. They act primarily as ion transport inhibitors due to their inhibition of Na(+)-, K(+)-, and Ca(+)-ATPase transport systems. They also have insulin-like action, positive inotropic action on cardiac ventricular muscle, and other metabolic effects.Hydrolases: Any member of the class of enzymes that catalyze the cleavage of the substrate and the addition of water to the resulting molecules, e.g., ESTERASES, glycosidases (GLYCOSIDE HYDROLASES), lipases, NUCLEOTIDASES, peptidases (PEPTIDE HYDROLASES), and phosphatases (PHOSPHORIC MONOESTER HYDROLASES). EC 3.Hexosaminidases: Enzymes that catalyze the hydrolysis of N-acylhexosamine residues in N-acylhexosamides. Hexosaminidases also act on GLUCOSIDES; GALACTOSIDES; and several OLIGOSACCHARIDES.Receptor-Like Protein Tyrosine Phosphatases, Class 3: A subclass of receptor-like protein tryosine phosphatases that contain a single cytosolic protein tyrosine phosphate domain and multiple extracellular fibronectin III-like domains.Enzyme Repression: The interference in synthesis of an enzyme due to the elevated level of an effector substance, usually a metabolite, whose presence would cause depression of the gene responsible for enzyme synthesis.Molecular Weight: The sum of the weight of all the atoms in a molecule.Organophosphorus Compounds: Organic compounds that contain phosphorus as an integral part of the molecule. Included under this heading is broad array of synthetic compounds that are used as PESTICIDES and DRUGS.Semen: The thick, yellowish-white, viscid fluid secretion of male reproductive organs discharged upon ejaculation. In addition to reproductive organ secretions, it contains SPERMATOZOA and their nutrient plasma.Signal Transduction: 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.Arylsulfatases: Enzymes that catalyze the hydrolysis of a phenol sulfate to yield a phenol and sulfate. Arylsulfatase A, B, and C have been separated. A deficiency of arylsulfatases is one of the causes of metachromatic leukodystrophy (LEUKODYSTROPHY, METACHROMATIC). EC 3.1.6.1.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Cells, Cultured: 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.Receptor-Like Protein Tyrosine Phosphatases, Class 4: A subclass of receptor-like protein tryosine phosphatases that contain short highly glycosylated extracellular domains and two active cytosolic protein tyrosine phosphatase domains.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Mitogen-Activated Protein Kinase Phosphatases: A subcategory of phosphohydrolases that are specific for MITOGEN-ACTIVATED PROTEIN KINASES. They play a role in the inactivation of the MAP KINASE SIGNALING SYSTEM.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Enzyme Activation: 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.Nucleotidases: A class of enzymes that catalyze the conversion of a nucleotide and water to a nucleoside and orthophosphate. EC 3.1.3.-.Organophosphates: Carbon-containing phosphoric acid derivatives. Included under this heading are compounds that have CARBON atoms bound to one or more OXYGEN atoms of the P(=O)(O)3 structure. Note that several specific classes of endogenous phosphorus-containing compounds such as NUCLEOTIDES; PHOSPHOLIPIDS; and PHOSPHOPROTEINS are listed elsewhere.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Mutation: 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.Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.Thiamine Pyrophosphatase: An enzyme that hydrolyzes thiamine pyrophosphate to thiamine monophosphate plus inorganic phosphate. EC 3.6.1.-.Enzyme Inhibitors: Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.Organoids: An organization of cells into an organ-like structure. Organoids can be generated in culture. They are also found in certain neoplasms.Dual Specificity Phosphatase 6: A dual specificity phosphatase subtype that plays a role in intracellular signal transduction by inactivating MITOGEN-ACTIVATED PROTEIN KINASES. It has specificity for EXTRACELLULAR SIGNAL-REGULATED MAP KINASES and is primarily localized to the CYTOSOL.Protein Tyrosine Phosphatase, Non-Receptor Type 2: A subtype of non-receptor protein tyrosine phosphatase that is closely-related to PROTEIN TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE 1. Alternative splicing of the mRNA for this phosphatase results in the production at two gene products, one of which includes a C-terminal nuclear localization domain that may be involved in the transport of the protein to the CELL NUCLEUS. Although initially referred to as T-cell protein tyrosine phosphatase the expression of this subtype occurs widely.Oxazoles: Five-membered heterocyclic ring structures containing an oxygen in the 1-position and a nitrogen in the 3-position, in distinction from ISOXAZOLES where they are at the 1,2 positions.Prostatic Neoplasms: Tumors or cancer of the PROSTATE.Metalloproteins: Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed)SH2 Domain-Containing Protein Tyrosine Phosphatases: A subcategory of protein tyrosine phosphatases that contain SH2 type SRC HOMOLOGY DOMAINS. Many of the proteins in this class are recruited to specific cellular targets such as a cell surface receptor complexes via their SH2 domain.Leucyl Aminopeptidase: A zinc containing enzyme of the hydrolase class that catalyzes the removal of the N-terminal amino acid from most L-peptides, particularly those with N-terminal leucine residues but not those with N-terminal lysine or arginine residues. This occurs in tissue cell cytosol, with high activity in the duodenum, liver, and kidney. The activity of this enzyme is commonly assayed using a leucine arylamide chromogenic substrate such as leucyl beta-naphthylamide.Calcineurin: A CALCIUM and CALMODULIN-dependent serine/threonine protein phosphatase that is composed of the calcineurin A catalytic subunit and the calcineurin B regulatory subunit. Calcineurin has been shown to dephosphorylate a number of phosphoproteins including HISTONES; MYOSIN LIGHT CHAIN; and the regulatory subunits of CAMP-DEPENDENT PROTEIN KINASES. It is involved in the regulation of signal transduction and is the target of an important class of immunophilin-immunosuppressive drug complexes.6-Phytase: An enzyme that catalyzes the conversion of myo-inositol hexakisphosphate and water to 1L-myo-inositol 1,2,3,4,5-pentakisphosphate and orthophosphate. EC 3.1.3.26.Macrophages: The relatively long-lived phagocytic cell of mammalian tissues that are derived from blood MONOCYTES. Main types are PERITONEAL MACROPHAGES; ALVEOLAR MACROPHAGES; HISTIOCYTES; KUPFFER CELLS of the liver; and OSTEOCLASTS. They may further differentiate within chronic inflammatory lesions to EPITHELIOID CELLS or may fuse to form FOREIGN BODY GIANT CELLS or LANGHANS GIANT CELLS. (from The Dictionary of Cell Biology, Lackie and Dow, 3rd ed.)Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Acetylglucosaminidase: A beta-N-Acetylhexosaminidase that catalyzes the hydrolysis of terminal, non-reducing 2-acetamido-2-deoxy-beta-glucose residues in chitobiose and higher analogs as well as in glycoproteins. Has been used widely in structural studies on bacterial cell walls and in the study of diseases such as MUCOLIPIDOSIS and various inflammatory disorders of muscle and connective tissue.Subcellular Fractions: Components of a cell produced by various separation techniques which, though they disrupt the delicate anatomy of a cell, preserve the structure and physiology of its functioning constituents for biochemical and ultrastructural analysis. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p163)Cathepsins: A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.Escherichia: A genus of gram-negative, facultatively anaerobic, rod-shaped bacteria whose organisms occur in the lower part of the intestine of warm-blooded animals. The species are either nonpathogenic or opportunistic pathogens.Protein Binding: 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.Cathepsin K: A cysteine protease that is highly expressed in OSTEOCLASTS and plays an essential role in BONE RESORPTION as a potent EXTRACELLULAR MATRIX-degrading enzyme.Clinical Enzyme Tests: Analyses for a specific enzyme activity, or of the level of a specific enzyme that is used to assess health and disease risk, for early detection of disease or disease prediction, diagnosis, and change in disease status.Recombinant Proteins: Proteins prepared by recombinant DNA technology.PTEN Phosphohydrolase: 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.Cell Differentiation: Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.Time Factors: Elements of limited time intervals, contributing to particular results or situations.Glycogen-Synthase-D Phosphatase: An enzyme that catalyzes the conversion of phosphorylated, inactive glycogen synthase D to active dephosphoglycogen synthase I. EC 3.1.3.42.Gene Expression Regulation, Enzymologic: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.Golgi Apparatus: A stack of flattened vesicles that functions in posttranslational processing and sorting of proteins, receiving them from the rough ENDOPLASMIC RETICULUM and directing them to secretory vesicles, LYSOSOMES, or the CELL MEMBRANE. The movement of proteins takes place by transfer vesicles that bud off from the rough endoplasmic reticulum or Golgi apparatus and fuse with the Golgi, lysosomes or cell membrane. (From Glick, Glossary of Biochemistry and Molecular Biology, 1990)Receptor Activator of Nuclear Factor-kappa B: A tumor necrosis factor receptor family member that is specific for RANK LIGAND and plays a role in bone homeostasis by regulating osteoclastogenesis. It is also expressed on DENDRITIC CELLS where it plays a role in regulating dendritic cell survival. Signaling by the activated receptor occurs through its association with TNF RECEPTOR-ASSOCIATED FACTORS.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Microcystins: Cyclic heptapeptides found in MICROCYSTIS and other CYANOBACTERIA. Hepatotoxic and carcinogenic effects have been noted. They are sometimes called cyanotoxins, which should not be confused with chemicals containing a cyano group (CN) which are toxic.Chromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.Rabbits: The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.Recombinant Fusion Proteins: Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.Tyrosine: A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.Receptor-Like Protein Tyrosine Phosphatases, Class 5: A subclass of receptor-like protein tryosine phosphatases that contain an extracellular fibronectin III-like domain along with a carbonic anhydrase-like domain.Vacuoles: Any spaces or cavities within a cell. They may function in digestion, storage, secretion, or excretion.Cattle: Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.Intracellular Signaling Peptides and Proteins: Proteins and peptides that are involved in SIGNAL TRANSDUCTION within the cell. Included here are peptides and proteins that regulate the activity of TRANSCRIPTION FACTORS and cellular processes in response to signals from CELL SURFACE RECEPTORS. Intracellular signaling peptide and proteins may be part of an enzymatic signaling cascade or act through binding to and modifying the action of other signaling factors.Osteocalcin: Vitamin K-dependent calcium-binding protein synthesized by OSTEOBLASTS and found primarily in BONES. Serum osteocalcin measurements provide a noninvasive specific marker of bone metabolism. The protein contains three residues of the amino acid gamma-carboxyglutamic acid (Gla), which, in the presence of CALCIUM, promotes binding to HYDROXYAPATITE and subsequent accumulation in BONE MATRIX.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Pyruvate Dehydrogenase (Lipoamide)-Phosphatase: (Pyruvate dehydrogenase (lipoamide))-phosphate phosphohydrolase. A mitochondrial enzyme that catalyzes the hydrolytic removal of a phosphate on a specific seryl hydroxyl group of pyruvate dehydrogenase, reactivating the enzyme complex. EC 3.1.3.43.Glycoproteins: Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.Cantharidin: A toxic compound, isolated from the Spanish fly or blistering beetle (Lytta (Cantharis) vesicatoria) and other insects. It is a potent and specific inhibitor of protein phosphatases 1 (PP1) and 2A (PP2A). This compound can produce severe skin inflammation, and is extremely toxic if ingested orally.RNA, Messenger: RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.Cytoplasmic Granules: Condensed areas of cellular material that may be bounded by a membrane.Protein Kinases: A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.Proteins: Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.Protein Tyrosine Phosphatase, Non-Receptor Type 12: A subtype of non-receptor protein tyrosine phosphatases that is characterized by the presence of a N-terminal catalytic domain and a large C-terminal domain that is enriched in PROLINE, GLUTAMIC ACID, SERINE, and THREONINE residues (PEST sequences). The phosphatase subtype is ubiquitously expressed and implicated in the regulation of a variety of biological processes such as CELL MOVEMENT; CYTOKINESIS; focal adhesion disassembly; and LYMPHOCYTE ACTIVATION.Dual Specificity Phosphatase 3: A dual specificity phosphatase subtype that plays a role in intracellular signal transduction by inactivating MITOGEN-ACTIVATED PROTEIN KINASES. It has specificity for EXTRACELLULAR SIGNAL-REGULATED MAP KINASES.Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.PeroxidasesOsteoblasts: Bone-forming cells which secrete an EXTRACELLULAR MATRIX. HYDROXYAPATITE crystals are then deposited into the matrix to form bone.Sequence Alignment: The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.Receptor-Like Protein Tyrosine Phosphatases: A subcategory of protein tyrosine phosphatases that are bound to the cell membrane. They contain cytoplasmic tyrosine phosphatase domains and extracellular protein domains that may play a role in cell-cell interactions by interacting with EXTRACELLULAR MATRIX components. They are considered receptor-like proteins in that they appear to lack specific ligands.Phosphorus: A non-metal element that has the atomic symbol P, atomic number 15, and atomic weight 31. It is an essential element that takes part in a broad variety of biochemical reactions.Morganella morganii: A species of MORGANELLA formerly classified as a Proteus species. It is found in the feces of humans, dogs, other mammals, and reptiles. (From Bergey's Manual of Determinative Bacteriology, 9th ed)Phenolphthaleins: A family of 3,3-bis(p-hydroxyphenyl)phthalides. They are used as CATHARTICS, indicators, and COLORING AGENTS.Phosphotyrosine: An amino acid that occurs in endogenous proteins. Tyrosine phosphorylation and dephosphorylation plays a role in cellular signal transduction and possibly in cell growth control and carcinogenesis.Cell Biology: The study of the structure, behavior, growth, reproduction, and pathology of cells; and the function and chemistry of cellular components.Osteoprotegerin: A secreted member of the TNF receptor superfamily that negatively regulates osteoclastogenesis. It is a soluble decoy receptor of RANK LIGAND that inhibits both CELL DIFFERENTIATION and function of OSTEOCLASTS by inhibiting the interaction between RANK LIGAND and RECEPTOR ACTIVATOR OF NUCLEAR FACTOR-KAPPA B.Chromatography, Ion Exchange: Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.Leukemia, Hairy Cell: A neoplastic disease of the lymphoreticular cells which is considered to be a rare type of chronic leukemia; it is characterized by an insidious onset, splenomegaly, anemia, granulocytopenia, thrombocytopenia, little or no lymphadenopathy, and the presence of "hairy" or "flagellated" cells in the blood and bone marrow.
SLC7A7 Lysosomal acid phosphatase deficiency; 200950; ACP2 Lysyl hydroxylase 3 deficiency; 612394; PLOD3 Machado-Joseph disease ... FREM1 Bile acid malabsorption, primary; 613291; SLC10A2 Bile acid synthesis defect, congenital, 2; 235555; AKR1D1 Bile acid ... SBDS Sialic acid storage disorder, infantile; 269920; SLC17A5 Sialidosis, type I; 256550; NEU1 Sialidosis, type II; 256550; ... DLAT Pyruvate dehydrogenase phosphatase deficiency; 608782; PDP1 Pyruvate kinase deficiency; 266200; PKLR Rabson-Mendenhall ...
Phosphatidate phosphatase PPAPDC1A also known as phosphatidic acid phosphatase type 2 domain containing 1A is an enzyme that in ... phosphatidic acid phosphatase type 2 domain containing 1A". Takeuchi M, Harigai M, Momohara S, Ball E, Abe J, Furuichi K, ... PPAPDC1A has phosphatidate phosphatase activity. GRCh38: Ensembl release 89: ENSG00000203805 - Ensembl, May 2017 GRCm38: ... representatives of a novel type of mammalian phosphatidate phosphatase". Gene. 399 (2): 174-80. doi:10.1016/j.gene.2007.05.009 ...
In the case of Provenge, this disease related protein is prostatic acid phosphatase and the signalling component is GM-CSF. ... October 2008). "Prostatic acid phosphatase is an ectonucleotidase and suppresses pain by generating adenosine". Neuron. 60 (1 ... Disclosed are a novel prostatic acid phosphatase and corresponding coding region derived from mouse. Also disclosed is a method ... Erbas H, Erten O, Irfanoglu ME (December 2007). "Prostatic acid phosphatase in breast cyst fluid". The Malaysian Journal of ...
These granules can contain acid phosphatase. Acid phosphatase is only found in larger secretory granules, 400 to 900 nm in ... This acid phosphatase is also present in the Golgi apparatus of the chief cell. However, the Golgi apparatus areas associated ... Chief cells in parathyroid adenomas also display acid phosphatase activity. It is a benign tumor of the gland that requires ... Shannon, W. Allen; Roth, Sanford I. (1974-12-01). "An Ultrastructural Study of Acid Phosphatase Activity in Normal, Adenomatous ...
Brightwell R, Tappel AL (1968). "Lysosomal acid pyrophosphatase and acid phosphatase". Arch. Biochem. Biophys. 124 (1): 333-43 ... This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing ...
... uric acid lithiasis; acute uric acid nephropathy; neoplastic disease and myeloproliferative disease with high cell turnover ... glucose 6-phosphatase including glycogen storage disease; phosphoribosyl pyrophosphate synthetase, phosphoribosyl pyrophosphate ... resulting in the production of uric acid, the product of human purine metabolism. In addition to blocking uric acid production ... It is specifically used to prevent gout, prevent specific types of kidney stones, and for the high uric acid levels that can ...
Carbohydrates are utilised to generate energy, whilst amino acids and fatty acids are involved in the synthesis of ... Such transporter molecules include schistosome alkaline phosphatase (SmAP) and cathepsin B, which may be important in nutrient ... They obtain amino acids from host blood through a mechanism of haemoglobin degradation, which remains unresolved but is ... Schistosomes are in direct contact with host blood, a rich source of amino acids, and they therefore do not require penetrative ...
This permits characterization of osteoclasts by their staining for high expression of tartrate resistant acid phosphatase (TRAP ... These vacuoles include lysosomes filled with acid phosphatase. ... Energy-dependent acid transport was verified and the postulated ... Attachment to the bone matrix is facilitated by integrin receptors, such as αvβ3, via the specific amino acid motif Arg-Gly-Asp ... The osteoclast disassembles and digests the composite of hydrated protein and mineral at a molecular level by secreting acid ...
Richardson CC, Lehman IR, Kornberg A (January 1964). "A Deoxyribonucleic Acid Phosphatase-Exonuclease from Escherichia coli. II ... Linxweiler W, Hörz W (August 1982). "Sequence specificity of exonuclease III from E. coli". Nucleic Acids Res. 10 (16): 4845-59 ... phosphatase and AP-endonuclease activities. Temperature, salt concentration and the ratio of enzyme to DNA greatly affect ...
"Entrez Gene: PPAP2B phosphatidic acid phosphatase type 2B". "PLPP3 - Phospholipid phosphatase 3 - Homo sapiens (Human) - PLPP3 ... Lipid phosphate phosphohydrolase 3 (LPP3), also known as phospholipid phosphatase 3 (PLPP3) and phosphatidic acid phosphatase ... Ishikawa T, Kai M, Wada I, Kanoh H (April 2000). "Cell surface activities of the human type 2b phosphatidic acid phosphatase". ... Ishikawa T, Kai M, Wada I, Kanoh H (April 2000). "Cell surface activities of the human type 2b phosphatidic acid phosphatase". ...
Lysosomal acid phosphatase is an enzyme that in humans is encoded by the ACP2 gene. Lysosomal acid phosphatase is composed of ... and is chemically and genetically distinct from red cell acid phosphatase. Lysosomal acid phosphatase 2 is a member of a family ... Radzun HJ, Parwaresch MR (1981). "Isoelectric focusing pattern of acid phosphatase and acid esterase in human blood cells, ... "Entrez Gene: ACP2 acid phosphatase 2, lysosomal". Human ACP2 genome location and ACP2 gene details page in the UCSC Genome ...
Dullard dephosphorylates the mammalian phospatidic acid phosphatase, lipid. Dullard participates in a unique phosphatase ... which include phosphatase activity and protein serine/threonine phosphatase activity. This gene is relatively small and only ... Dullard is a member of DXDX(T/V) phosphatase family. It was shown in 2002 to be a potential regulator of neural tube ... contains 244 amino acids. Dullard protein or CTDnep1 encodes a protein serine/threonine phosphatase and dephosphoroylates LPIN1 ...
"Entrez Gene: RNGTT RNA guanylyltransferase and 5'-phosphatase". Yue Z, Maldonado E, Pillutla R, et al. (1998). "Mammalian ... Nucleic Acids Res. 26 (7): 1700-6. doi:10.1093/nar/26.7.1700. PMC 147440 . PMID 9512541. " ...
Richardson, C.C.; Lehman, I.R.; Kornberg, A. (1964). "A deoxyribonucleic acid phosphatase-exonuclease from Escherichia coli. II ... Richardson, C.C.; Kornberg, A. (1964). "A deoxyribonucleic acid phosphatase-exonuclease from Escherichia coli. I. Purification ... of the enzyme and characterization of the phosphatase activity". J. Biol. Chem. 239: 242-250. PMID 14114850. ...
Yasbin, R; Sawicki, J; MacIntyre, RJ (1978). "A developmental study of acid phosphatase-1 in Drosophila melanogaster". Dev Biol ... Sawicki, J; MacIntyre, RJ (1977). "Synthesis of ovarian acid phosphatase in Drosophila melanogaster". Dev Biol. 60 (1): 1-13. ... level of maternally derived enzyme and determination of the time of paternal gene expression for acid phosphatase-1 in ...
Lipid phosphate phosphohydrolase 1 also known as phosphatidic acid phosphatase 2a is an enzyme that in humans is encoded by the ... Ulrix W, Swinnen JV, Heyns W, Verhoeven G (1998). "Identification of the phosphatidic acid phosphatase type 2a isozyme as an ... "Entrez Gene: PPAP2A phosphatidic acid phosphatase type 2A". Kanoh H, Kai M, Wada I (1999). "Molecular characterization of the ... Hooks SB, Ragan SP, Lynch KR (1998). "Identification of a novel human phosphatidic acid phosphatase type 2 isoform". FEBS Lett ...
... histidine acid phosphatases (HAPS), β-propeller phytases, purple acid phosphatases, and most recently, protein tyrosine ... Zhang ZY (2003). "Mechanistic studies on protein tyrosine phosphatases". Prog. Nucleic Acid Res. Mol. Biol. 73: 171-220. doi: ... Phytic acid and its metabolites have several important roles in seeds and grains, most notably, phytic acid functions as a ... As such, phytases, which hydrolyze phytic acid and its metabolites, also have important roles. Phytic acid and its metabolites ...
Nucleic Acids Res. 26 (16): 3854-61. doi:10.1093/nar/26.16.3854. PMC 147779 . PMID 9685505. Theis-Febvre N, Filhol O, Froment C ... Cazales M, Cochet C, Monsarrat B, Ducommun B, Baldin V (January 2003). "Protein kinase CK2 regulates CDC25B phosphatase ... Nucleic Acids Res. 19 (25): 7125-9. doi:10.1093/nar/19.25.7125. PMC 332535 . PMID 1766873. "Entrez Gene: CSNK2A1 casein kinase ... Nucleic Acids Res. 23 (14): 2593-9. doi:10.1093/nar/23.14.2593. PMC 307079 . PMID 7651819. ole-MoiYoi OK (1995). "Casein kinase ...
Here they secrete promastigote secretory gel (PSG), which is composed of soluble acid phosphatase and phosphoglycoprotein. ... Bates, PA; Dwyer, DM (1987). "Biosynthesis and secretion of acid phosphatase by Leishmania donovani promastigotes". Molecular ...
2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415-8. doi:10.1093/nar/gkj139. PMC 1347501 . ... 2006). "Shugoshin collaborates with protein phosphatase 2A to protect cohesin". Nature. 441 (7089): 46-52. doi:10.1038/ ... "Shugoshin collaborates with protein phosphatase 2A to protect cohesin". Nature. 441 (7089): 46-52. doi:10.1038/nature04663. ...
Buschbeck M, Eickhoff J, Sommer MN, Ullrich A (Aug 2002). "Phosphotyrosine-specific phosphatase PTP-SL regulates the ERK5 ... Nucleic Acids Res. 26 (20): 4771-7. doi:10.1093/nar/26.20.4771. PMC 147902 . PMID 9753748. Kato Y, Tapping RI, Huang S, Watson ... Nucleic Acids Res. 26 (20): 4771-7. doi:10.1093/nar/26.20.4771. PMC 147902 . PMID 9753748. ...
Kishi F, Matsuura S, Kajii T (1989). "Nucleotide sequence of the human liver-type alkaline phosphatase cDNA". Nucleic Acids Res ... Alkaline phosphatase, tissue-nonspecific isozyme is an enzyme that in humans is encoded by the ALPL gene. There are at least ... The exact physiological function of the alkaline phosphatases is not known. A proposed function of this form of the enzyme is ... Khandwala HM, Mumm S, Whyte MP (2007). "Low serum alkaline phosphatase activity and pathologic fracture: case report and brief ...
Its acid dissociation constant pKa is 5.0 at 20 °C. Tolbutamide Tolazamide Glyburide Glipizide Dinnendahl, V.; Fricke, U., eds ... It also markedly raises the serum level of alkaline phosphatase.[citation needed] Chlorpropamide is a white crystalline powder ...
The site contains 3 crucial amino acids (2 histidines and 1 glutamic acid ) that are involved in the phosphatase reaction. ... Re-localisation to the mitochondria does not require TIGAR's phosphatase domain. Instead 4 amino acids at the C-terminal end of ... and use molecules from respiratory pathways to synthesise amino acids and nucleic acids to maintain rapid growth. In Glioma, a ... The bis-phosphatase-like active site of TIGAR is positively charged, and catalyses the removal of phosphate groups from other ...
Wan, H.; Horvath, C. (1975-11-20). "Behavior of soluble and immobilized acid phosphatase in hydro-organic media". Biochimica et ...
... (EC 3.1.3.2, acid phosphomonoesterase, phosphomonoesterase, glycerophosphatase, acid monophosphatase, acid phosphohydrolase, acid phosphomonoester hydrolase, uteroferrin, acid nucleoside diphosphate phosphatase, orthophosphoric-monoester phosphohydrolase (acid optimum)) is a phosphatase, a type of enzyme, used to free attached phosphoryl groups from other molecules during digestion. It can be further classified as a phosphomonoesterase. Acid phosphatase is stored in lysosomes and functions when these fuse with endosomes, which are acidified while they function; therefore, it has an acid pH optimum. This enzyme is ...
விலங்கு உயிரணுக்களின் நுண்ணுறுப்புகளுள் ஒன்றான இலைசோசோம்கள் (lysosome) கழிவுப் பொருட்ளையும் தீங்கு விளைவிக்கும் நோய்க்கிருமிகளையும் செரிக்கும் இன்றியமையாத வேலையைச் செய்கின்றன. தாவரங்களிலும் பூஞ்சைகளிலும் இலைசோசோம்கள் இல்லை. இப்பணியை வெற்றிடப்பைகள் செய்கின்றன. இலைசோசோம் ஒரே ஒரு உறை மட்டுமே உடையது. இவ் உறைக்குள் பல வலிமையான நொதிகள் காணப்படும். இவை இந்த உறையை விட்டு வெளியே ...
... (PSP)[1] is a form of phosphoprotein phosphatase that acts upon phosphorylated serine/threonine residues. Serine and threonine phosphates are stable under physiological conditions, so a phosphatase enzyme has to remove the phosphate to reverse the regulation signal. Ser/Thr-specific protein phosphatases are regulated partly by their location within the cell and by specific inhibitor proteins. Serine and threonine are amino acids which have similar side-chain compositions that contain a hydroxyl group and thus can be phosphorylated by enzymes called serine/threonine protein kinases. The addition of the phosphate group can be reversed by enzymes called serine/threonine phosphatases. The addition and removal of phosphate groups regulates many cellular pathways involved in cell proliferation, programmed cell death (apoptosis), embryonic development, and cell differentiation. ...
... (CaN) is a calcium and calmodulin dependent serine/threonine protein phosphatase (also known as protein phosphatase 3, and calcium-dependent serine-threonine phosphatase). It activates the T cells of the immune system and can be blocked by drugs. Calcineurin activates nuclear factor of activated T cell, cytoplasmic (NFATc), a transcription factor, by dephosphorylating it. The activated NFATc is then translocated into the nucleus, where it upregulates the expression of interleukin 2 (IL-2), which, in turn, stimulates the growth and differentiation of T cell response. Calcineurin is the target of a class of drugs called calcineurin inhibitors, which includes cyclosporin, voclosporin, pimecrolimus and tacrolimus. Calcineurin is a heterodimer of a 61-kD calmodulin-binding catalytic subunit, calcineurin A and a 19-kD Ca2+-binding regulatory subunit, calcineurin B. There are three isozymes of the catalytic subunit, each encoded by a separate gene (PPP3CA, ...
A protein phosphatase is a phosphatase enzyme that removes a phosphate group from the phosphorylated amino acid residue of its substrate protein. Protein phosphorylation is one of the most common forms of reversible protein posttranslational modification (PTM), with up to 30% of all proteins being phosphorylated at any given time. Protein kinases (PKs) are the effectors of phosphorylation and catalyse the transfer of a γ-phosphate from ATP to specific amino acids on proteins. Several hundred PKs exist in mammals and are classified into distinct super-families. Proteins are phosphorylated predominantly on Ser, Thr and Tyr residues, which account for 79.3, 16.9 and 3.8% respectively of the phosphoproteome, at least in mammals. In contrast, protein phosphatases (PPs) are the primary effectors of dephosphorylation and can be grouped into three main classes based on sequence, structure and ...
Although a clear consensus has not been reached, a large number of scientists adhere to a substrate-transport model to account for the catalytic properties of glucose 6-phosphatase. In this model, glucose 6-phosphatase has a low degree of selectivity. The transfer of the glucose 6-phosphate is carried out by a transporter protein (T1) and the endoplasmic reticulum (ER) contains structures allowing the exit of the phosphate group (T2) and glucose (T3).[6] Glucose 6-phosphatase consists of 357 amino acids, and is anchored to the endoplasmic reticulum (ER) by nine transmembrane helices. Its N-terminal and active site are found on the lumen side of the ER and its C-terminus projects into the cytoplasm. Due to its tight association to the ER, the exact structure of glucose 6-phosphatase remains unknown. However, sequence alignment has shown that glucose 6-phosphatase is structurally similar to ...
... (EC 3.1.3.2, acid phosphomonoesterase, phosphomonoesterase, glycerophosphatase, acid monophosphatase, acid phosphohydrolase, acid phosphomonoester hydrolase, uteroferrin, acid nucleoside diphosphate phosphatase, orthophosphoric-monoester phosphohydrolase (acid optimum)) is a phosphatase, a type of enzyme, used to free attached phosphoryl groups from other molecules during digestion. It can be further classified as a phosphomonoesterase. Acid phosphatase is stored in lysosomes and functions when these fuse with endosomes, which are acidified while they function; therefore, it has an acid pH optimum. This enzyme is ...
Calcineurin subunit B type 2 is a protein that in humans is encoded by the PPP3R2 gene. Among its related pathways are MAPK signaling pathway and GPCR pathway. GO annotations related to this gene include calcium ion binding. An important paralog of this gene is CHP1. GRCh38: Ensembl release 89: ENSG00000188386 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000028310 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". Liu L, Zhang J, Yuan J, Dang Y, Yang C, Chen X, Xu J, Yu L (May 2005). "Characterization of a human regulatory subunit of protein phosphatase 3 gene (PPP3RL) expressed specifically in testis". Mol Biol Rep. 32 (1): 41-5. doi:10.1007/s11033-004-4250-4. PMID 15865209. "Entrez Gene: PPP3R2 protein phosphatase 3 (formerly 2B), regulatory subunit B, beta isoform". "PathCards :: MAPK signaling pathway Pathway and related pathways". pathcards.genecards.org. Retrieved 2015-09-08. "PathCards :: GPCR Pathway Pathway and related pathways". ...
... tetrahydrate, also known as Rochelle salt, is a double salt of tartaric acid first prepared (in about 1675) by an apothecary, Pierre Seignette, of La Rochelle, France. Potassium sodium tartrate and monopotassium phosphate were the first materials discovered to exhibit piezoelectricity.[3] This property led to its extensive use in "crystal" gramophone (phono) pick-ups, microphones and earpieces during the post-World War II consumer electronics boom of the mid-20th Century. Such transducers had an exceptionally high output with typical pick-up cartridge outputs as much as 2 volts or more. Rochelle salt is deliquescent so any transducers based on the material deteriorated if stored in damp conditions. It has been used medicinally as a laxative. It has also been used in the process of silvering mirrors. It is an ingredient of Fehling's solution (reagent for reducing sugars). It is used in electroplating, in electronics and piezoelectricity, and as a combustion accelerator ...
... (Na2C4H4O6) is used as an emulsifier and a binding agent in food products such as jellies, margarine, and sausage casings. As a food additive, it is known by the E number E335. Because its crystal structure captures a very precise amount of water, it is also a common primary standard for Karl Fischer titration, a common technique to assay water content. ...
... (3-nitropropanoic acid, BPA, 3-NPA, C3H5NO4) is a mycotoxin, a potent mitochondrial inhibitor, toxic to humans. It is produced by a number of fungi, and found widely in food, in sugar cane, as well as Japanese fungally fermented staples miso, soy sauce, katsuobushi, and some traditional Chinese medicines. It can be caused by extreme weather, stressed crop growth conditions, as well as storage conditions (like moisture), which can give a further rise under global warming conditions. It is found that 3-nitropropionic acid is a mitochondrial toxin and produces striatal alterations in rats similar to those observed in the brain of Huntington's disease patients, and administration of the cannabinoid receptor agonist WIN55212-2 to rats for six consecutive days, before the 3-NPA injection, exerted preventive effects on all alterations elicited by the toxin, like mitochondrial dysfunction and lipid peroxidation, by activation of the CB1 ...
In chemistry, a racemic mixture, or racemate /reɪˈsimeɪt/, is one that has equal amounts of left- and right-handed enantiomers of a chiral molecule. The first known racemic mixture was racemic acid, which Louis Pasteur found to be a mixture of the two enantiomeric isomers of tartaric acid. A sample with only a single enantiomer is an enantiomerically pure, enantiopure or homochiral compound. From racemic acid found in grapes; from Latin racemus, meaning a bunch of grapes. A racemic mixture is denoted by the prefix (±)- or dl- (for sugars the prefix dl- may be used), indicating an equal (1:1) mixture of dextro and levo isomers. Also the prefix rac- (or racem-) or the symbols RS and SR (all in italic letters) are used. If the ratio is not 1:1 (or is not known), the prefix (+)/(−), d/l- or d/l- (with a slash) is used instead. The usage of d and l is strongly discouraged by IUPAC. A racemate is optically ...
6, is added to the egg whites before the denaturation process. Cream of tartar is an acid that is used to help stabilize and coagulate the proteins, which aids in a stronger protein network to trap air for the foam formation. Cream of tartar has a low pH to help bring the proteins near their isoelectric point to allow them to be denatured easier. The isoelectric point is a specific pH where a molecule, in this case protein, has no net electrical charge. The electrical charge on a protein would normally hold the protein together in its coiled clump.[10]. The cream of tartar also acts as a catalase affecting the sugar structure. Sugar/sucrose used in meringue is a crystal structure made up of glucose and fructose. Cream of tartar inverts the sugar during the baking process, meaning the sugar is split into two parts containing glucose and fructose. This prevents the sugar from recrystallizing and giving the meringue a gritty, undesirable texture.[11]. Sugar is the final ...
High sensitivity ELISA kit for detection of Prostatic Acid Phosphatase/ACPP. Backed by our 100% Guarantee. ... Human Prostatic Acid Phosphatase/ACPP ELISA Kit (Colorimetric). ... Prostatic Acid Phosphatase/ACPP ELISA Kit. * Prostatic Acid ... Additional Prostatic Acid Phosphatase/ACPP Products. Prostatic Acid Phosphatase/ACPP KA1911 * Prostatic Acid Phosphatase/ACPP ... Home » Prostatic Acid Phosphatase/ACPP » Prostatic Acid Phosphatase/ACPP ELISA Kits » Human Prostatic Acid Phosphatase/ACPP ...
... side effects of tartrate resistant acid phosphatase test and more. ... Tartrate resistant acid phosphatase test, treatment, preventions, precautions, risk factors, procedure, results, complications ... Tartrate Resistant Acid Phosphatase Test is a comprehensive medical test which aims at measuring the level of acid phosphatase ... This test is also known as Type 5b acid phosphatase test.. Purpose of theTest. Your physician may suggest you to go for the ...
Although prostate-specific acid phosphatase is not a cancer-specific enzyme, we conclude that its measurement may be of ... Comparison of enzyme-linked immunosorbent assay and radioimmunoassay for prostate-specific acid phosphatase in prostatic ... Comparison of enzyme-linked immunosorbent assay and radioimmunoassay for prostate-specific acid phosphatase in prostatic ... Comparison of enzyme-linked immunosorbent assay and radioimmunoassay for prostate-specific acid phosphatase in prostatic ...
NMP inhibited RANKL-induced tartrate-resistant acid phosphatase activity and the formation of tartrate-resistant acid ... NMP inhibited RANKL-induced tartrate-resistant acid phosphatase activity and the formation of tartrate-resistant acid ... phosphatase-positive multinucleated cells. The RANKL-induced expression of NFATc1 (nuclear factor of activated T cells, ... phosphatase-positive multinucleated cells. The RANKL-induced expression of NFATc1 (nuclear factor of activated T cells, ...
Testicular acid phosphatase Tissue acid phosphatase, or Lysosomal acid phosphatase Alkaline phosphatase Henneberry, M.O.; Engel ... is Acid-Phosphatase negative , T-ALL ( originating instead from T Lymphocytes ) is acid-phosphatase positive . Acid phosphatase ... Acid phosphatase (EC 3.1.3.2, acid phosphomonoesterase, phosphomonoesterase, glycerophosphatase, acid monophosphatase, acid ... Minkin, Cedrick (1982). "Bone Acid Phosphatase: Tartrate-resistant Acid Phosphatase as a Marker of Osteoclast Function". ...
Prostatic acid phosphatase (PAP), also prostatic specific acid phosphatase (PSAP), is an enzyme produced by the prostate. It ... "Prostatic acid phosphatase in serum of patients with prostatic cancer is a specific phosphotyrosine acid phosphatase". Clin. ... "Human prostatic acid phosphatase: cDNA cloning, gene mapping and protein sequence homology with lysosomal acid phosphatase". ... "Nucleotide sequence of human prostatic acid phosphatase determined from a full-length cDNA clone". Nucleic Acids Res. 18 (16): ...
... ,ARUP Laboratories is a national reference laboratory and a worldwide leader in innovative ... Acid Phosphatase, Prostatic. 2. Acid Phosphatase, Total, Serum. 3. Alkaline Phosphatase, Bone Specific. 4. Alkaline Phosphatase ... Tartrate Resistant Acid Phosphatase Stain. 6. Chemically Resistant Sealing Mat for 384-well Plate. 7. Chemically Resistant ...
Arabidopsis thaliana mRNA for acid phosphatase-like protein, complete cds, clone... Arabidopsis thaliana mRNA for acid ... Arabidopsis thaliana mRNA for acid phosphatase-like protein, complete cds, clone: RAFL14-33-N06. GenBank: AK227764.1 ... phosphatase-like protein, complete cds, clone: RAFL14-33-N06. gi,110743823,dbj,AK227764.1, ...
Prostatic Acid Phosphatase - PAP. An enzyme produced by the prostate. It may be found in increased amounts in men who have ... Medical Word - Prostatic Acid Phosphatase. Ans : PAP. An enzyme produced by the prostate. It may be found in increased amounts ... Prostatic Acid Phosphatase - Glossary. Written & Compiled by Medindia Content Team. Medically Reviewed by The Medindia Medical ...
Buy our Recombinant human Acid Phosphatase protein. Ab87493 is an active full length protein produced in Escherichia coli and ... Recombinant human Acid Phosphatase protein. See all Acid Phosphatase proteins and peptides. ...
Assay Acid phosphatase activity in 1 hr 10 min in cell culture media, cell/tissue extracts, and biofluids with ab83367. For ... Acid phosphatases (AP) dephosphorylate phosphate groups from phosphate esters under acid conditions. Different acid phosphatase ... Acid phosphatases (AP) dephosphorylate phosphate groups from phosphate esters under acid conditions. Different acid phosphatase ... as a phosphatase substrate. They can be used to measure alkaline phosphatase, neutral phosphatase, and acid phosphatase ...
Characterization of a cell-wall acid phosphatase (PhoAp) in Aspergillus fumigatus.. Bernard M1, Mouyna I1, Dubreucq G1, ... It is also a phosphate-repressible acid phosphatase. The absence of PhoAp from a phosphate-rich medium was not associated with ... was an acid phosphatase (PhoAp) that was active on both phosphate monoesters and phosphate diesters. PhoAp is a ...
Tartrate resistant acid phosphatase (TRAP) is an enzyme expressed by subsets of macrophages and osteoclasts that exists either ...
Organ cultures of newborn mouse calvaria were used to test the hypothesis that tartrate-resistant acid phosphatase might serve ... Bone acid phosphatase: Tartrate-resistant acid phosphatase as a marker of osteoclast function. ... in vitro results in the release of tartrate-resistant acid phosphatase from osteoclasts and tartrate-sensitive acid phosphatase ... Yam, L. T.: Clinical significance of the human acid phosphatases. A review, Am. J. Med.56:604-616, 1974CrossRefPubMedGoogle ...
... nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to ... See also Velankar et al., Nucleic Acids Research 33, D262-265 (2005). ...
Testicular acid phosphataseImported. ,p>Information which has been imported from another database using automatic procedures.,/ ... Belongs to the histidine acid phosphatase family.SAAS annotation. Automatic assertion according to rulesi ... tr,F6WRF1,F6WRF1_MOUSE Testicular acid phosphatase (Fragment) OS=Mus musculus OX=10090 GN=Acp4 PE=3 SV=3 ... PS00616 HIS_ACID_PHOSPHAT_1, 1 hit. PS00778 HIS_ACID_PHOSPHAT_2, 1 hit. ...
... a reevaluation of the potential contribution of the prostatic acid phosphatase test seems timely. ... Prostatic acid phosphatase (PAP) emerged as the worlds first clinically useful tumor marker in the 1940s and 1950s. With the ... Prostatic Acid Phosphatase Timeline. In 1938, Gutman and Gutman reported increased levels of acid phosphatase in patients with ... Measuring Prostatic Acid Phosphatase. Acid phosphatases are a group of five ubiquitous tissue isoenzymes that hydrolyze organic ...
Acid-phosphatase test for semen definition at Dictionary.com, a free online dictionary with pronunciation, synonyms and ... acid phosphatase, acid-phosphatase test for semen, acid precipitation, acid radical, acid rain, acid reflux, acid-reflux test ... acid-phosphatase test for semen. acidophilic, acidophilus milk, acidosis, acid perfusion test, ... A screening test for detecting the presence of semen by determining acid phosphatase content. ...
Has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma (By similarity). ... A non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) ... Prostatic acid phosphataseAdd BLAST. 350. Amino acid modifications. Feature key. Position(s). DescriptionActions. Graphical ... "Site-directed mutagenesis of prostatic acid phosphatase. Catalytically important aspartic acid 258, substrate specificity, and ...
C. L. Araujo, I. B. Quintero, and A. Kipar, "Prostatic acid phosphatase is the main acid phosphatase with 5′-ectonucleotidase ... P. Vihko, I. Quintero, A. Rönkö et al., "Prostatic acid phosphatase (PAP) is pi(3)p-phosphatase and its inactivation leads to ... Consequences of the Lack of CD73 and Prostatic Acid Phosphatase in the Lymphoid Organs. Gennady G. Yegutkin,1,2 Kaisa Auvinen,1 ... I. B. Quintero, C. L. Araujo, A. E. Pulkka et al., "Prostatic acid phosphatase is not a prostate specific target," Cancer ...
"Acid Phosphatase" by people in Harvard Catalyst Profiles by year, and whether "Acid Phosphatase" was a major or minor topic of ... "Acid Phosphatase" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical Subject ... Below are the most recent publications written about "Acid Phosphatase" by people in Profiles. ... Below are MeSH descriptors whose meaning is more general than "Acid Phosphatase". ...
Prostatic acid phosphatase (PAP) has been investigated as the target of several antigen-specific anti-prostate tumor vaccines. ... CTL Prostatic acid phosphatase (PAP) HLA-A2 ELISPOT Epitope This is a preview of subscription content, log in to check access. ... Prostatic acid phosphatase (PAP) has been investigated as the target of several antigen-specific anti-prostate tumor vaccines. ... Wang Y, Harada M, Yano H, Ogasawara S, Takedatsu H, Arima Y, Matsueda S, Yamada A, Itoh K (2005) Prostatic acid phosphatase as ...
Acid and alkaline phosphatase were determined in 107 breast cancer patients to study their potential value in case of bone ... Acid Phosphatase / blood*. Alkaline Phosphatase / blood*. Bone Neoplasms / blood, diagnosis, enzymology, secondary*. Bone and ... 0/Isoenzymes; 0/Tumor Markers, Biological; EC 3.1.3.1/Alkaline Phosphatase; EC 3.1.3.2/Acid Phosphatase ... Tartrate resistant acid phosphatase (TR-ACP), and bone alkaline phosphatase (bone-ALP) were significantly higher in patients ...
... sialic acid storage disease pathway; FOUND IN cytosol (inferred); INTERACTS WITH aflatoxin B1; arsenous acid; benzene-1,2,4- ... ENCODES a protein that exhibits N-acylneuraminate-9-phosphatase activity; INVOLVED IN N-acetylneuraminate biosynthetic process ... Nanp (N-acetylneuraminic acid phosphatase). NCBI. Ortholog. Sus scrofa (pig):. NANP (N-acetylneuraminic acid phosphatase). HGNC ... N-acetylneuraminic acid phosphatase). NCBI. Ortholog. Canis lupus familiaris (dog):. NANP (N-acetylneuraminic acid phosphatase) ...
Browse our Prostatic Acid Phosphatase/ACPP product catalog backed by our Guarantee+. ... Prostatic Acid Phosphatase/ACPP products available through Novus Biologicals. ... PTMs for Prostatic Acid Phosphatase/ACPP. Learn more about PTMs related to Prostatic Acid Phosphatase/ACPP.. Cleavage. ... Diseases related to Prostatic Acid Phosphatase/ACPP. Discover more about diseases related to Prostatic Acid Phosphatase/ACPP.. ...
  • Lipin 2/3 deficiency caused phosphatidic acid accumulation and mammalian target of rapamycin complex 1 (mTORC1) activation, which were associated with enhanced protein levels of a key phospholipid biosynthetic enzyme (CTP:phosphocholine cytidylyltransferase α) and altered membrane phospholipid composition. (jci.org)
  • Mixed micelles of 32 P-labeled phosphatidylcholine or phosphatidic acid (PA) and the nonionic detergent octylphenol polyethylene oxide (NP-40 Nonidet) were used to assay the activities of phospholipase D and PA phosphatase in crude extracts of mung bean ( Vigna radiata ) cotyledons. (plantphysiol.org)
  • A phosphatase inhibition assay for detection of okadaic acid (OA) toxins in shellfish, OkaTest, was single laboratory validated according to international recognized guidelines (AOAC, EURACHEM). (mdpi.com)
  • Antagonistic Effects of Zinc and Aluminum on Lead Inhibition of delta-Aminolevulinic Acid Dehydratase. (ebscohost.com)
  • Examines the antagonistic effects of zinc (Zn) and aluminum (Al) on lead inhibition of delta-aminolevulinic acid dehydratase in human and animal nutrition. (ebscohost.com)
  • ABA binding to PYRABACTIN RESISTANCE1 (PYR1)/PYR1-LIKE (PYL)/REGULATORY COMPONENTS OF ABA RECEPTORS intracellular receptors leads to inhibition of key negative regulators of ABA signaling, i.e. clade A protein phosphatases type 2C (PP2Cs) such as ABA-INSENSITIVE1 and HYPERSENSITIVE TO ABA1 (HAB1), causing the activation of the ABA signaling pathway. (cpib.ac.uk)
  • Interestingly, AHG1 was resistant to inhibition by the PYR/PYL receptors tested, which suggests that this seed-specific phosphatase is still able to regulate ABA signaling in the presence of ABA and PYR/PYL receptors and therefore to control the highly active ABA signaling pathway that operates during seed development. (cpib.ac.uk)
  • Moreover, the differential sensitivity of the phosphatases At5g59220 and PP2CA to inhibition by ABA receptors reveals a functional specialization of PYR/PYL ABA receptors to preferentially inhibit certain PP2Cs. (cpib.ac.uk)
  • Scaffolds, guiding NPs, and substitution patterns of the two investigated NP-derived and -inspired compound collections, size of the collections, and SAR derived for the inhibition of different phosphatases. (pnas.org)
  • The plant hormone abscisic acid (ABA) is a key regulator of seed maturation and germination and mediates adaptive responses to environmental stress. (plantcell.org)
  • Statistical analyses of promoter regions of abscisic acid (ABA)-regulated genes reveal an overrepresented ABA responsive motif, which is the known ABA response element. (plantcell.org)
  • The plant hormone abscisic acid (ABA) plays a crucial role in the control of the stress response and the regulation of plant growth and development. (cpib.ac.uk)
  • Clade A protein phosphatases type 2C (PP2Cs) are negative regulators of abscisic acid (ABA) signaling that are inhibited in an ABA-dependent manner by PYRABACTIN RESISTANCE1 (PYR1)/PYR1-LIKE (PYL)/REGULATORY COMPONENTS OF ABA RECEPTORS (RCAR) intracellular receptors. (cpib.ac.uk)
  • Metabolic labeling experiments using promastigotes indicated that the intracellular enzyme was soluble prior to secretion and no evidence was found for the association of secretory acid phosphatase with cell membranes after protein synthesis. (lancs.ac.uk)
  • The results demonstrated that acid phosphatase was secreted into the flagellar reservoir by Leishmania promastigotes using a conventional constitutive secretory mechanism, and subsequently released from the reservoir into the extracellular medium. (lancs.ac.uk)
  • Except in the non-secretory reservoir regions, silk glands of all the species examined are rich in cytoplasmic ribonucleic acid. (biologists.org)
  • 11 nonamer peptides derived from the amino acid sequence of PAP were used as stimulator antigens in functional ELISPOT assays with peripheral blood mononuclear cells from 20 HLA-A2+ patients with prostate cancer or ten healthy blood donors. (springer.com)
  • Based on its properties and amino acid sequence analyses, SapS was classified as a new member of the bacterial class C family of non-specific acid phosphatases. (up.ac.za)
  • Histochemical examination of these cells demonstrates that innumerable granules containing acid phosphatase develop in the cytoplasm before mitosis. (sciencemag.org)
  • In view of the latter point, it is interesting to note that no sulphydryl groups can be detected in the phosphatase border zone (in the more insoluble constituents which remain informalin-fixed frozen sections), although the main bulk of th e cytoplasm is rich in sulphydryl groups. (biologists.org)
  • Although the latter is abundant in the main body of the cell, it is, however, absent from the phosphatase border zone, so that in the cytoplasm nucleic acid ends where phosphatase begins. (biologists.org)
  • To quantitatively assess the superoxide dismutase 1 ( SOD1 ), transforming growth factor, beta 1 ( TGF-β1 ), and dual-specificity phosphatase 1 ( DUSP1 ) messenger ribonucleic acid (mRNA) expression levels as the main intracellular reactive oxygen species neutralizers, wound healing mediators, and immunomodulators (respectively) in keratoconic (KCN) and non-KCN corneas. (molvis.org)