Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.
A chromogenic substrate that permits direct measurement of peptide hydrolase activity, e.g., papain and trypsin, by colorimetry. The substrate liberates p-nitroaniline as a chromogenic product.
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Enzyme that is a major constituent of kidney brush-border membranes and is also present to a lesser degree in the brain and other tissues. It preferentially catalyzes cleavage at the amino group of hydrophobic residues of the B-chain of insulin as well as opioid peptides and other biologically active peptides. The enzyme is inhibited primarily by EDTA, phosphoramidon, and thiorphan and is reactivated by zinc. Neprilysin is identical to common acute lymphoblastic leukemia antigen (CALLA Antigen), an important marker in the diagnosis of human acute lymphocytic leukemia. There is no relationship with CALLA PLANT.
A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from GLYCINE or THREONINE. It is involved in the biosynthesis of PURINES; PYRIMIDINES; and other amino acids.
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.
A potent inhibitor of membrane metalloendopeptidase (ENKEPHALINASE). Thiorphan potentiates morphine-induced ANALGESIA and attenuates naloxone-precipitated withdrawal symptoms.
A membrane-bound metalloendopeptidase that may play a role in the degradation or activation of a variety of PEPTIDE HORMONES and INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS. Genetic mutations that result in loss of function of this protein are a cause of HYPOPHOSPHATEMIC RICKETS, X-LINKED DOMINANT.
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.
ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.
ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.
Peptide hydrolases that contain at the active site a SERINE residue involved in catalysis.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Proteins which contain carbohydrate groups attached covalently to the polypeptide chain. The protein moiety is the predominant group with the carbohydrate making up only a small percentage of the total weight.
A biologically active tridecapeptide isolated from the hypothalamus. It has been shown to induce hypotension in the rat, to stimulate contraction of guinea pig ileum and rat uterus, and to cause relaxation of rat duodenum. There is also evidence that it acts as both a peripheral and a central nervous system neurotransmitter.
A 25-kDa peptidase produced by Staphylococcus simulans which cleaves a glycine-glcyine bond unique to an inter-peptide cross-bridge of the STAPHYLOCOCCUS AUREUS cell wall. EC 3.4.24.75.
The process of cleaving a chemical compound by the addition of a molecule of water.
A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.
The rate dynamics in chemical or physical systems.
Peptides composed of two amino acid units.
A potent natriuretic and vasodilatory peptide or mixture of different-sized low molecular weight PEPTIDES derived from a common precursor and secreted mainly by the HEART ATRIUM. All these peptides share a sequence of about 20 AMINO ACIDS.
Peptides composed of between two and twelve amino acids.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Proteins prepared by recombinant DNA technology.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.
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.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
A key enzyme in SPHINGOLIPIDS biosynthesis, this enzyme catalyzes the pyridoxal-5'-phosphate-dependent condensation of L-SERINE and PALMITOYL COENZYME A to 3-dehydro-D-sphinganine. The enzyme consists of two different subunits.
A di-isopropyl-fluorophosphate which is an irreversible cholinesterase inhibitor used to investigate the NERVOUS SYSTEM.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
A subclass of EXOPEPTIDASES that act on the free N terminus end of a polypeptide liberating a single amino acid residue. EC 3.4.11.
An eleven-amino acid neurotransmitter that appears in both the central and peripheral nervous systems. It is involved in transmission of PAIN, causes rapid contractions of the gastrointestinal smooth muscle, and modulates inflammatory and immune responses.
A nonapeptide messenger that is enzymatically produced from KALLIDIN in the blood where it is a potent but short-lived agent of arteriolar dilation and increased capillary permeability. Bradykinin is also released from MAST CELLS during asthma attacks, from gut walls as a gastrointestinal vasodilator, from damaged tissues as a pain signal, and may be a neurotransmitter.
A sub-class of PEPTIDE HYDROLASES that act only near the ends of polypeptide chains.
One of the endogenous pentapeptides with morphine-like activity. It differs from MET-ENKEPHALIN in the LEUCINE at position 5. Its first four amino acid sequence is identical to the tetrapeptide sequence at the N-terminal of BETA-ENDORPHIN.
A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in SOIL and WATER. Its organisms are also found in raw meats, MILK and other FOOD, hospital environments, and human clinical specimens. Some species are pathogenic in humans.
A family of SERINE ENDOPEPTIDASES isolated from Bacillus subtilis. EC 3.4.21.-
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
A thermostable extracellular metalloendopeptidase containing four calcium ions. (Enzyme Nomenclature, 1992) 3.4.24.27.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
A condition of an abnormally low level of PHOSPHATES in the blood.
A serotype of botulinum toxins that has specificity for cleavage of SYNAPTOSOMAL-ASSOCIATED PROTEIN 25.
Aryl CYCLOPENTANES that are a reduced (protonated) form of INDENES.
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)
The sum of the weight of all the atoms in a molecule.
Endoproteases that contain proteolytic core domains and ATPase-containing regulatory domains.
Carboxypeptidases that are primarily found the DIGESTIVE SYSTEM that catalyze the release of C-terminal amino acids. Carboxypeptidases A have little or no activity for hydrolysis of C-terminal ASPARTIC ACID; GLUTAMIC ACID; ARGININE; LYSINE; or PROLINE. This enzyme requires ZINC as a cofactor and was formerly listed as EC 3.4.2.1 and EC 3.4.12.2.

Identification of APC2, a homologue of the adenomatous polyposis coli tumour suppressor. (1/8246)

The adenomatous polyposis coli (APC) tumour-suppressor protein controls the Wnt signalling pathway by forming a complex with glycogen synthase kinase 3beta (GSK-3beta), axin/conductin and betacatenin. Complex formation induces the rapid degradation of betacatenin. In colon carcinoma cells, loss of APC leads to the accumulation of betacatenin in the nucleus, where it binds to and activates the Tcf-4 transcription factor (reviewed in [1] [2]). Here, we report the identification and genomic structure of APC homologues. Mammalian APC2, which closely resembles APC in overall domain structure, was functionally analyzed and shown to contain two SAMP domains, both of which are required for binding to conductin. Like APC, APC2 regulates the formation of active betacatenin-Tcf complexes, as demonstrated using transient transcriptional activation assays in APC -/- colon carcinoma cells. Human APC2 maps to chromosome 19p13.3. APC and APC2 may therefore have comparable functions in development and cancer.  (+info)

Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D. (2/8246)

The crystal structure of profactor D, determined at 2.1 A resolution with an Rfree and an R-factor of 25.1 and 20.4%, respectively, displays highly flexible or disordered conformation for five regions: N-22, 71-76, 143-152, 187-193 and 215-223. A comparison with the structure of its mature serine protease, complement factor D, revealed major conformational changes in the similar regions. Comparisons with the zymogen-active enzyme pairs of chymotrypsinogen, trypsinogen and prethrombin-2 showed a similar distribution of the flexible regions. However, profactor D is the most flexible of the four, and its mature enzyme displays inactive, self-inhibited active site conformation. Examination of the surface properties of the N-terminus-binding pocket indicates that Ile16 may play the initial positioning role for the N-terminus, and Leu17 probably also helps in inducing the required conformational changes. This process, perhaps shared by most chymotrypsinogen-like zymogens, is followed by a factor D-unique step, the re-orientation of an external Arg218 to an internal position for salt-bridging with Asp189, leading to the generation of the self-inhibited factor D.  (+info)

The virulence plasmid-encoded impCAB operon enhances survival and induced mutagenesis in Shigella flexneri after exposure to UV radiation. (3/8246)

Upon exposure to UV radiation, Shigella flexneri SA100 displayed survival and mutation frequencies comparable to those of Escherichia coli AB1157, which contains a functional UmuDC error-prone DNA repair system. Survival of SA100 after UV irradiation was associated with the presence of the 220-kb virulence plasmid, pVP. This plasmid encodes homologues of ImpA and ImpB, which comprise an error-prone DNA repair system encoded on plasmid TP110 that was initially identified in Salmonella typhimurium, and ImpC, encoded upstream of ImpA and ImpB. Although the impB gene was present in representatives of all four species of Shigella, not all isolates tested contained the gene. Shigella isolates that lacked impB were more sensitive to UV radiation than isolates that contained impB. The nucleotide sequence of a 2.4-kb DNA fragment containing the imp operon from S. flexneri SA100 pVP was 96% identical to the imp operon from the plasmid TP110. An SA100 derivative with a mutation in the impB gene had reduced survival following UV irradiation and less UV-induced mutagenesis relative to the parental strain. We also found that S. flexneri contained a chromosomally encoded umuDC operon; however, the umuDC promoter was not induced by exposure to UV radiation. This suggests that the imp operon but not the umuDC operon contributes to survival and induced mutagenesis in S. flexneri following exposure to UV radiation.  (+info)

Alternating antineutrophil cytoplasmic antibody specificity: drug-induced vasculitis in a patient with Wegener's granulomatosis. (4/8246)

We describe a patient who presented with Wegener's granulomatosis associated with antineutrophil cytoplasmic antibodies (ANCA) directed against proteinase 3 (PR3) with a cytoplasmic immunofluorescence pattern (cANCA), whose ANCA type changed to antimyeloperoxidase antibodies with a perinuclear immunofluorescence pattern (pANCA) when treated with propylthiouracil, and changed back to anti-PR3 antibodies with cANCA after the medication was discontinued. The patient developed flares of vasculitis symptoms associated with rises in either type of ANCA. Tests for antimyeloperoxidase ANCA were repeatedly negative before the drug was started, strongly implicating the drug as the cause of the episode. This case demonstrates that patients with idiopathic ANCA-positive vasculitis may quickly develop a superimposed drug-associated ANCA-positive vasculitis. Iatrogenic vasculitis should be suspected when a patient with idiopathic vasculitis with one type of ANCA develops the other type of ANCA.  (+info)

An Arabidopsis 14-3-3 protein can act as a transcriptional activator in yeast. (5/8246)

The 14-3-3 proteins are a group of highly conserved and widely distributed eukaryotic proteins with diverse functions. One 14-3-3 protein, AFT1 from Arabidopsis thaliana, was found to be able to activate transcription in yeast. When fused to the DNA-binding domain of a bacterial protein LexA, AFT1 can activate transcription of reporter genes that contain LexA operator sequences in their promoters. Although the in vivo function of AFT1 is not completely known, its similarity to previously identified proteins found in transcription complexes of Arabidopsis and maize suggests that AFT1 and some other 14-3-3 proteins may activate gene expression in other systems as well.  (+info)

Dengue virus NS3 serine protease. Crystal structure and insights into interaction of the active site with substrates by molecular modeling and structural analysis of mutational effects. (6/8246)

The mosquito-borne dengue viruses are widespread human pathogens causing dengue fever, dengue hemorrhagic fever, and dengue shock syndrome, placing 40% of the world's population at risk with no effective treatment. The viral genome is a positive strand RNA that encodes a single polyprotein precursor. Processing of the polyprotein precursor into mature proteins is carried out by the host signal peptidase and by NS3 serine protease, which requires NS2B as a cofactor. We report here the crystal structure of the NS3 serine protease domain at 2.1 A resolution. This structure of the protease combined with modeling of peptide substrates into the active site suggests identities of residues involved in substrate recognition as well as providing a structural basis for several mutational effects on enzyme activity. This structure will be useful for development of specific inhibitors as therapeutics against dengue and other flaviviral proteases.  (+info)

Bile duct epithelial cells exposed to alpha-naphthylisothiocyanate produce a factor that causes neutrophil-dependent hepatocellular injury in vitro. (7/8246)

The acute hepatotoxicity induced by alpha-naphthylisothiocyanate (ANIT) in rats is manifested as neutrophil-dependent necrosis of bile duct epithelial cells (BDECs) and hepatic parenchymal cells. This hepatotoxicity mirrors that of drug-induced cholangiolitic hepatitis in humans. Since BDECs are primary targets of ANIT-induced toxicity, we hypothesized that after exposure to ANIT, BDECs produce a factor(s) that causes neutrophil chemotaxis and neutrophil-dependent hepatocellular injury. To test this hypothesis BDECs were isolated from male Sprague Dawley rats and incubated with ANIT (6.25, 12.5, 25, or 50 microM) or vehicle for 24 h. The conditioned medium (CM) was collected and placed in the bottom chamber of a two-chambered chemotaxis system, while isolated neutrophils were placed in the top chamber. Chemotaxis was indicated by neutrophil migration through a membrane to the bottom chamber. CM from BDECs exposed to each concentration of ANIT was chemotactic, whereas CM from vehicle-treated BDECs was not. ANIT alone caused a modest degree of chemotaxis at 50 microM. The conditioned media were added to isolated hepatocytes or to hepatocyte-neutrophil cocultures and incubated for 24 h. Hepatocyte toxicity was indicated by alanine aminotransferase release into the culture medium. CM from vehicle-treated BDECs did not cause hepatocyte killing in either hepatocyte-neutrophil cocultures or hepatocyte cultures. In contrast, the addition of CM from ANIT-treated BDECs (CM-BDEC-A) to hepatocyte-neutrophil cocultures resulted in hepatocyte killing. The same CM was not cytotoxic to hepatocyte cultures devoid of neutrophils. The hepatocyte killing could not be explained by residual ANIT in the CM, which was below the limit of detection (< or = 0.5 microM). The addition of antiproteases afforded protection against neutrophil-dependent hepatocellular injury induced by CM-BDEC-A. These results indicate that ANIT causes BDECs to release a factor(s) that attracts neutrophils and stimulates them to injure hepatocytes in vitro.  (+info)

Subtilisin-like proprotein convertases, PACE4 and PC8, as well as furin, are endogenous proalbumin convertases in HepG2 cells. (8/8246)

Serum albumin is synthesized as a larger precursor form, proalbumin, which undergoes proteolytic processing at a dibasic site by a hepatic proprotein convertase within the secretory pathway to generate the mature form. Although furin, a member of the subtilisin-like proprotein convertase (SPC) family, was thought to be the only candidate hepatic convertase for proalbumin, SPC family members other than furin were recently suggested to also be involved in proalbumin processing. This study was designed to identify the endogenous proprotein convertases involved in proalbumin processing. Since human hepatoma HepG2 cells are highly differentiated and produce major plasma proteins, this cell line was used as a model for hepatocytes. Northern blot analysis revealed that PACE4, furin and PC8 of the SPC family were expressed in HepG2 cells as well as in the liver. Ribonuclease protection assay showed that PACE4A-II mRNA is the major transcript in HepG2 cells among the PACE4 isoforms. The coexpression studies showed that furin, PACE4A-II and PC8 were all able to convert proalbumin to albumin correctly. To elucidate the roles of these endogenous SPC family members in proalbumin processing, the antisense RNA for PACE4, furin and PC8 was stably expressed in HepG2 cells, respectively. The expression of each antisense RNA resulted in approximately 30% inhibition of endogenous proalbumin processing. We therefore concluded that PACE4 and PC8, as well as furin, are involved in the processing of proalbumin in HepG2 cells, and that these SPC family members are functionally redundant in this processing.  (+info)

FSAP (Factor VII-activating protease) is a novel plasma-derived serine protease that regulates haemostasis as well as vascular cell proliferation. FSAP undergoes autoactivation in the presence of polyanionic macromolecules such as heparin and RNA. Competition experiments suggest that RNA and heparin bind to the same or overlapping interaction sites. A proteolysis approach, where FSAP was hydrolysed into smaller fragments, was used to identify the polyanion-binding site. The EGF (epidermal growth factor)-like domains EGF2 and EGF3 of FSAP are the major interaction domains for RNA. The amino acids Arg170, Arg171, Ser172 and Lys173 within the EGF3 domain were essential for this binding. This is also the region with the highest positive net charge in the protein and is most probably located in an exposed loop. It is also highly conserved across five species. Disruption of disulphide bridges led to the loss of RNA and heparin binding, indicating that the three-dimensional structure of the EGF3 domain ...
Membrane-bound serine proteases play essential assignments in different natural procedures. the Tyr deletion is in charge of the HAI-2 lack of function. Our useful assay allowed us to recognize membrane-bound serine proteases as mobile focus on for inhibition by HAI-2 outrageous type and mutants, also to better define the function from the Tyr in the next Kunitz domains in the inhibitory activity of HAI-2. Launch Membrane-bound or membrane-anchored serine proteases possess lately emerged being a subfamily of 20 serine proteases that talk about a conserved catalytic domains and a transmembrane domains [1]. They screen different pathophysiological and physiological assignments such as for example assignments in epidermis and intestinal hurdle integrity [2]C[5], handling of atrial natriuretic peptide [6], iron homeostasis [7]C[9], trophoblastic advancement [10], hearing [11], ion and [12] homeostasis [13], [14]. Even more elusive, however, will be the identity as well as the assignments of their ...
Our data also support a role for the E(zip) genes in RhoA signaling. By genetic analyses three of the E(zip) mutants encode known components of the RhoA signaling pathway (RhoGEF211-3, RhoA12-6, and zip33-1). All E(zip) mutations are strongly interactive with RhoA and, with the exception of 31-6, which is a semilethal mutation, exhibit moderate-to-strong interactions with zipEbr (Table 10). However, our interaction data suggest that the unidentified 12-5, 18-5, and 31-6 genes may not act in the same pathway as Sb-sbd during leg morphogenesis. First, weak interactions are observed between the 12-5, 18-5, and 31-6 mutants and RhoA pathway members such as DRhoGEF2, drok, and Df(2R)Jp1. In contrast Sb-sbd mutants exhibit robust interactions with drok and Df(2R)Jp1. Second, while interactions between E(zip) and Sb-sbd mutants are robust (all moderate), they are not as strong as those observed between Sb-sbd and the RhoA signaling pathway. Additional mutants and characterization of the gene products ...
The prolyl oligopeptidase family, which is a group of serine peptidases, can hydrolyze peptides smaller than 30 residues. The prolyl oligopeptidase family in plants includes four members, which are prolyl oligopeptidase (POP, EC3.4.21.26), dipeptidyl peptidase IV (DPPIV, EC3.4.14.5), oligopeptidase B (OPB, EC3.4.21.83), and acylaminoacyl peptidase (ACPH, EC3.4.19.1). POP is found in human and rat, and plays important roles in multiple biological processes, such as protein secretion, maturation and degradation of peptide hormones, and neuropathies, signal transduction and memory and learning. However, the function of POP is unclear in plants. In order to study POP function in plants, we cloned the cDNA of the OsPOP5 gene from rice by nested-PCR. Sequence analysis showed that the cDNA encodes a protein of 596 amino acid residues with Mw ≈ 67.29 kD. In order to analyze the protein function under different abiotic stresses, OsPOP5 was expressed in Escherichia coli. OsPOP5 protein enhanced the
TY - JOUR. T1 - Mitochondrial serine protease HtrA2/Omi as a potential therapeutic target. AU - Bhuiyan, Md Shenuarin. AU - Fukunaga, Koji. PY - 2009/5/18. Y1 - 2009/5/18. N2 - Deregulation of apoptosis has been shown to contribute to the development of many diseases, including ischemia/reperfusion injury of organs, different types of cancer formation, as well as neurodegenerative and autoimmune disorders. Recently, the mitochondrial serine protease High temperature requirement A2 (HtrA2)/Omi has drawn attention as it played pivotal role in different pathological conditions. We critically discussed the rationale for therapeutically targeting HtrA2 signaling in pathological conditions and explore the molecular mechanisms of HtrA2 inhibition as a novel therapeutic strategy. The precise mode of action and importance of HtrA2 in mitochondrial quality control as well as in apoptosis in mammalian cells has been recently studied through biochemical, structural and genetic studies. This review ...
Hepcidin is a liver-derived hormone with a key role in iron homeostasis. In addition to iron, it is regulated by inflammation and hypoxia, although mechanisms of hypoxic regulation remain unclear. In hepatocytes, hepcidin is induced by bone morphogenetic proteins (BMPs) through a receptor complex requiring hemojuvelin (HJV) as a co-receptor. Type II transmembrane serine proteinase (TMPRSS6) antagonizes hepcidin induction by BMPs by cleaving HJV from the cell membrane. Inactivating mutations in TMPRSS6 lead to elevated hepcidin levels and consequent iron deficiency anemia. Here we demonstrate that TMPRSS6 is up-regulated in hepatic cell lines by hypoxia and by other activators of hypoxia-inducible factor (HIF). We show that TMPRSS6 expression is regulated by both HIF-1α and HIF-2α. This HIF-dependent up-regulation of TMPRSS6 increases membrane HJV shedding and decreases hepcidin promoter responsiveness to BMP signaling in hepatocytes. Our results reveal a potential role for TMPRSS6 in hepcidin
Hepcidin is a liver-derived hormone with a key role in iron homeostasis. In addition to iron, it is regulated by inflammation and hypoxia, although mechanisms of hypoxic regulation remain unclear. In hepatocytes, hepcidin is induced by bone morphogenetic proteins (BMPs) through a receptor complex requiring hemojuvelin (HJV) as a co-receptor. Type II transmembrane serine proteinase (TMPRSS6) antagonizes hepcidin induction by BMPs by cleaving HJV from the cell membrane. Inactivating mutations in TMPRSS6 lead to elevated hepcidin levels and consequent iron deficiency anemia. Here we demonstrate that TMPRSS6 is up-regulated in hepatic cell lines by hypoxia and by other activators of hypoxia-inducible factor (HIF). We show that TMPRSS6 expression is regulated by both HIF-1α and HIF-2α. This HIF-dependent up-regulation of TMPRSS6 increases membrane HJV shedding and decreases hepcidin promoter responsiveness to BMP signaling in hepatocytes. Our results reveal a potential role for TMPRSS6 in hepcidin
Airway Trypsin-like Protease/HAT/TMPRSS11D Lysates available through Novus Biologicals. Browse our Airway Trypsin-like Protease/HAT/TMPRSS11D Lysate catalog backed by our Guarantee+.
Nucleosomes may be released during cell death but may also derive from NETs that are released from neutrophils.17 It was previously demonstrated that NETs are cytotoxic when added to human alveolar epithelial cells and that histones, and not DNA, mediate the observed cytotoxic effects.18 Strikingly, anti-histone antibodies only partly neutralized the cytotoxicity of NETs, presumably because other proteins in NETs also conferred cytotoxicity. Instead, in a study by Kumar et al,48 the cytotoxicity of NETs was completely inhibited by an anti-histone antibody. The size of the chromatin fragments, presence of antimicrobial proteins, and different histone modifications that modulate chromatin condensation, and thus histone exposure, may have influenced NET cytotoxicity. Because injection of anti-histone antibodies had beneficial effects in mouse and baboon sepsis,11,49 and our results suggest that histones circulate as nucleosomes that are not cytotoxic in vitro, other mechanisms must be involved in ...
TY - JOUR. T1 - High temperature requirement A3 (HtrA3) promotes etoposide- and cisplatin-induced cytotoxicity in lung cancer cell lines. AU - Beleford, Daniah. AU - Rattan, Ramandeep. AU - Chien, Jeremy. AU - Shridhar, Viji. PY - 2010/4/16. Y1 - 2010/4/16. N2 - Lung cancer is the leading cause of cancer-related deaths worldwide. Here we show for the first time that HtrA3 is a mitochondrial stress-response factor that promotes cytotoxicity to etoposide and cisplatin in lung cancer cell lines. Exogenous expression of wild type HtrA3 domain variants significantly attenuated cell survival with etoposide and cisplatin treatment in lung cancer cell lines H157 and A549 compared with expression of protease inactive mutants (S305A) or vector control. Conversely, HtrA3 suppression promoted cell survival with etoposide and cisplatin treatment in lung cancer cell lines Hop62 and HCC827. Survival was attenuated by re-expression of wild type HtrA3 variants during treatment but not by protease inactive ...
Identification of the molecular nature of the barrier is still under investigation, with the consensus that a protein lipid layer, which is located in the top layers of the epidermis and TJs, plays an essential role in development of the skin barrier function (Tsuruta et al., 2002). Evidence that cornified envelope assembly is necessary for barrier development in skin is obtained from the study of transglutaminase 1-deficient mice that lack confirmed envelopes. These mice suffer from water loss, resulting in neonatal lethality (Matsuki et al., 1998). Alterations of corneocyte morphology have also been described in various mouse models with epidermal permeability barrier defects ranging from near absence in transglutaminase 1-deficient mice (Matsuki et al., 1998) to irregular shaped corneocytes (e.g., Klf4−/− mice; Segre et al., 1999). Our corneocyte phenotype mostly resembled that of matriptase/MT-SP1-deficient mice, a member of the type II transmembrane serine protease family (List et al., ...
A series of substrate analogue inhibitors of the serine protease HAT, containing a 4-amidinobenzylamide moiety as the P1 residue, was prepared. The most potent compounds possess a basic amino acid in the d-configuration as P3 residue. Whereas inhibitor 4 (K(i) 13 nM) containing proline as the P2 residue completely lacks selectivity, incorporation of norvaline leads to a potent inhibitor (15, K(i) 15 nM) with improved selectivity for HAT in comparison to the coagulation proteases thrombin and factor Xa or the fibrinolytic plasmin. Selected inhibitors were able to suppress influenza virus replication in a HAT-expressing MDCK cell model.
1GBF: ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID
Campylobacter jejuni has emerged as a leading cause of bacterial enterocolitis. The serine protease HtrA has been shown to be a pivotal, novel C. jejuni virulence factor involved in cell invasion and transmigration across polarised epithelial cells in vitro. However, the functional relevance of the htrA gene for the interaction of C. jejuni with the host immune system in the infant mouse infection model has not been investigated so far. Here we studied the role of C. jejuni htrA during infection of 3-weeks-old infant mice. Immediately after weaning, conventional wild-type mice were perorally infected with the NCTC11168∆htrA mutant (∆htrA) or the parental wild-type strain. Approximately one third of infected infant mice suffered from bloody diarrhea until day 7 post infection (p.i.), whereas colonic histopathological changes were rather moderate but comparable between the two strains. Interestingly, parental, but not ∆htrA mutant infected mice, displayed a multifold increase of apoptotic cells in
Purpose : Recent studies have shown a strong association between the serine protease HtrA1 and age-related macular degeneration (AMD). Increased HtrA1 expression in retinal pigment epithelium (RPE) has been shown to cause extracellular matrix degradation and destabilization of the Bruchs membrane. However, little is known about functional effects of HtrA1 overexpression on RPE. To investigate these effects we established an in vitro model of polarized RPE overexpressing HtrA1 where phagocytic activity, a key function of RPE, could be assessed. Methods : Human fetal RPE cells cultured on laminin-coated transwell membranes were infected either with the wild type HtrA1- or the HtrA1 Serine-Alanine mutation (S328A)-GFP IRES construct two weeks after seeding. After five weeks of growth in vitro phagocytosis assay was performed. Thereby, cells were incubated with CY5-labelled photoreceptor outer segments (POS) isolated from porcine retinas for six hours. POS internalization was observed by live cell ...
FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene encodes a member of the type II transmembrane serine protease class of the trypsin superfamily. Members of this family are composed of multiple structurally distinct domains. The encoded protein converts pro-atrial natriuretic peptide to biologically active atrial natriuretic peptide, a cardiac hormone that regulates blood volume and pressure. This protein may also function as a pro-brain-type natriuretic peptide convertase. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jun 2013 ...
TMPRSS4 is a novel type II transmembrane serine protease that is highly expressed on the cell surface in pancreatic, thyroid and other cancer tissues, although its oncogenic significance and molecular mechanisms are unknown. Previously, we have shown that TMPRSS4 promotes invasion, migration and metastasis of human tumor cells by facilitating an epithelial-mesenchymal transition (EMT). In this study, we explored the molecular basis underlying TMPRSS4-mediated effects. We show that multiple downstream signaling pathways, including focal adhesion kinase (FAK), extracellular signal-regulated kinase (ERK), Akt, Src and Rac1, are activated by TMPRSS4 expression and that FAK signaling and ERK activation are required for TMPRSS4-induced invasiveness and EMT, including cadherin switch. Inhibition of PI3K or Src reduced invasiveness and actin rearrangement mediated by TMPRSS4 without restoring E-cadherin expression. Downregulation of E-cadherin was required for TMPRSS4-mediated effects but was not ...
In our study, using mice with LKB1-deficient mammary glands, we found evidence that basement membrane may be degraded by type II transmembrane serine proteases (TTSPs) during mammary tumorigenesis [32]. We reported that loss of LKB1 does not induce palpable tumours during the lifetime of the mice but leads to mild abnormalities in the mammary gland, such as hyperbranching, partial disorganization of apical polarity and incomplete basement membrane. However, combining LKB1 deficiency with oncogenic MYC dramatically accelerates the appearance of mammary tumours in comparison with glands exposed to oncogenic MYC alone [32]. The study shows that both MYC+ and MYC+;LKB1− tumours are histopathologically mostly adenocarcinomas and not informative as such regarding the possible mechanisms underlying accelerated tumorigenesis. However, the histology of hyperplastic regions in between tumour areas was particularly interesting, providing a path for follow-up studies. Expression of oncogenic MYC alone, a ...
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Protein HtrA2, also known as Omi, is a mitochondrially-located serine protease. The human protein Serine protease HTRA2, mitochondrial is 49kDa in size and composed of 458 amino acids. The peptide fragment of 1-31 amino acid is the mitochondrial transition sequence, fragment 32-133 amino acid is propertied, and 134-458 is the mature protein Serine protease HTRA2, mitochondrial, and its theoretical pI of this protein is 6.12.[10] HtrA2 shows similarities with DegS, a bacterial protease present in the periplasm of gram-negative bacteria. Structurally, HtrA2 is a trimeric molecule with central protease domains and a carboxy-terminal PDZ domain, which is characteristic of the HtrA family. The PDZ domain preferentially binds C-terminus of the protein substrate and modulate the proteolytic activity of the trypsin-like protease domain.[11] ...
The polytopic membrane protein Rhomboid-1 promotes the cleavage of the membrane-anchored TGFalpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Until now, the mechanism of this key signaling regulator has been obscure, but our analysis suggests that Rhomboid-1 is a novel intramembrane serine protease that directly cleaves Spitz. In accordance with the putative Rhomboid active site being in the membrane bilayer, Spitz is cleaved within its transmembrane domain, and thus is, to our knowledge, the first example of a growth factor activated by regulated intramembrane proteolysis. Rhomboid-1 is conserved throughout evolution from archaea to humans, and our results show that a human Rhomboid promotes Spitz cleavage by a similar mechanism. This growth factor activation mechanism may therefore be widespread.
Testisin is a recently identified human serine protease expressed by premeiotic testicular germ cells and is a candidate tumor suppressor for testicular cancer. Here, we report the characterization of the gene encoding testisin, designated PRSS21, and its localization on the short arm of human chromosome 16 (16p13.3) between the microsatellite marker D16S246 and the radiation hybrid breakpoint CY23HA. We have further refined the localization to cosmid 406D6 in this interval and have established that the gene is approximately 4. 5 kb in length, and contains six exons and five intervening introns. The structure of PRSS21 is very similar to the human prostasin gene (PRSS8) which maps nearby on 16p11.2, suggesting that these genes may have evolved through gene duplication. Sequence analysis showed that the two known isoforms of testisin are generated by alternative pre-mRNA splicing. A major transcription initiation site was identified 97 nucleotides upstream of the testisin translation start and conforms
This gene encodes a protein that belongs to the serine protease family. The encoded protein contains a serine protease domain, a transmembrane domain, an LDL receptor-like domain, and a scavenger receptor cysteine-rich domain. Serine proteases are known to be involved in a variety of biological processes, whose malfunction often leads to human diseases and disorders. This gene was identified by its association with both congenital and childhood onset autosomal recessive deafness. This gene is expressed in fetal cochlea and many other tissues, and is thought to be involved in the development and maintenance of the inner ear or the contents of the perilymph and endolymph. This gene was also identified as a tumor-associated gene that is overexpressed in ovarian tumors. Alternatively spliced transcript variants have been described. [provided by RefSeq, Jan 2012 ...
BioAssay record AID 210651 submitted by ChEMBL: In vitro inhibitory concentration required to inhibit human serine protease enzyme thrombin (FIIa) by 50%.
1GBH: Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
The typeNII transmembrane serine protease matriptase plays an important role in the integrity of epithelial barriers. However, the molecular mechanisms underlying the role of matriptase are unknown. To study these mechanisms, two variants of MadinNDarby canine kidney (MDCK) cells were used, together with the calciumNswitch model of epithelial function with measurements of transepithelial electrical resistance (TEER). Inhibitors of matriptase proteolytic activity delayed the restoration of TEER after calciumNswitch in MDCKNI, which develop high TEER and lack the leaky tight junction protein claudinN2, but not MDCKNII. This effect was confirmed in MDCKNI, established to stably express matriptase targeted shRNA. The influence of matriptase inhibition on MDCKNI was shown not to involve altered expression or assembly of relevant components of paracelluar junctions or cytoskeleton. This excluded a role for claudinN2 in the function of matriptase, which had previously been shown in human CacoN2 ...
Human Transmembrane protease serine 6(TMPRSS6) ELISA kit https://www.sciencepro.com.br/produtos/csb-el023928hu https://www.sciencepro.com.br/@@site-logo/logo-novo.png ...
Serine protease with a variety of targets, including extracellular matrix proteins such as fibronectin. HTRA1-generated fibronectin fragments further induce synovial cells to up-regulate MMP1 and MMP3 production. May also degrade proteoglycans, such as aggrecan, decorin and fibromodulin. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. Inhibits signaling mediated by TGF-beta family members. This activity requires the integrity of the catalytic site, although it is unclear whether TGF-beta proteins are themselves degraded. By acting on TGF-beta signaling, may regulate many physiological processes, including retinal angiogenesis and neuronal survival and maturation during development. Intracellularly, degrades TSC2, leading to the activation of TSC2 downstream targets ...
Membrane-anchored serine proteases are involved in many aspects of biology from embryonic development to cancer metastasis. For many of these proteases, the cell biology, physiological function and role in disease remain to be defined. The symposium will include sessions to cover topics from cell biology, structure, regulation and roles in health and disease.. ...
The high temperature requirement A1 (HTRA1) is a potent protease involved in many diseases, including rheumatoid arthritis (RA). However, the regulatory mechanisms that control HTRA1 expression need to be determined. In this study, we demonstrated that IFN-γ significantly inhibited the basal and LPS-induced HTRA1 expression in fibroblasts and macrophages, which are two major cells for HTRA1 production in RA. Importantly, the inhibitory effect of IFN-γ on HTRA1 expression was evidenced in collagen-induced arthritis (CIA) mouse models and in human RA synovial cells. In parallel with the enhanced CIA incidence and pathological changes in IFN-γ-deficient mice, HTRA1 expression in the joint tissues was also increased as determined by real-time PCR and Western blots. IFN-γ deficiency increased the incidence of CIA and the pathological severity in mice. Neutralization of HTRA1 by Ab significantly reversed the enhanced CIA frequency and severity in IFN-γ-deficient mice. Mechanistically, IFN-γ ...
Ynm3 is the only budding yeast protein possessing a combination of a serine protease and PDZ domains, a defining feature of the widely conserved HtrA (high temperature requirement A) protein family. The bacterial HtrA/DegP is involved in protective stress response to aid survival at higher temperatures by cleaving irreversibly unfolded proteins in the periplasm. At ambient growth temperatures, it acts as a chaperone and aids maturation of outer membrane proteins that have escaped folding mediated by the primary periplasmic chaperone SurA. Studies involving overexpression of mammalian mitochondrial HtrA2/Omi in cell culture propose a proapoptotic role for the protein. Mice lacking HtrA2/Omi or its protease activity, however, show no evidence of reduced rate of cell death. Instead, these mice suffer loss of a population of neurons in the striatum leading to a Parkinsonian phenotype. Two mutations in the gene encoding human HtrA2/Omi, leading to partial loss of protease activity have been ...
Pneumonia is one of the commonest causes of death worldwide. High‑temperature requirement A2 (HtrA2) is a proapoptotic mitochondrial serine protease involved in caspase‑dependent or caspase‑independent cell apoptosis. UCF‑101 (5‑[5‑(2‑nitrophenyl) furfuryl iodine]‑1,3‑diphenyl‑2‑thiobarbituric acid), an inhibitor of HtrA2, has a protective effect on organs in various diseases by inhibiting cell apoptosis. The aim of the present study was to explore whether UCF‑101 has a protective effect on lungs in pneumonia. A lipopolysaccharide (LPS)‑induced pneumonia model was established in rats. UCF‑101 (2 µmol/kg) was used for treatment. Lung injury was detected by hematoxylin and eosin staining. Pro‑inflammatory cytokines and oxidative stress‑related factors were detected using corresponding test kits. TUNEL staining was used to measure the amount of cell apoptosis. Apoptosis‑associated proteins were detected by western blot assay. The present study indicated pulmonary ...
Purified Recombinant Human HTRA1 Protein, MYC/DDK-tagged, C13 and N15-labeled from Creative Biomart. Recombinant Human HTRA1 Protein, MYC/DDK-tagged, C13 and N15-labeled can be used for research.
The High temperature requirement A (HtrA) proteases are a family of serine proteases conserved from bacteria to mammals, and are known to have important functions in protecting cells from stress conditions. There are four mammalian HtrA paralogs (HtrA1-4). HtrA1 is involved in apoptosis and anoikis, and is proposed to function as a tumour suppressor. It has also been implicated in the development of other diseases such as arthritis, Alzheimers disease, age-related macular degeneration, and cerebral autosomal recessive arteriopathy with subcortical infarcts and leukoencephalopathy. We have previously shown that HtrA1 is highly enriched in the placenta compared to other tissues, and that in women HtrA1 is expressed in placental and endometrial cells at the placental-maternal interface during the first trimester of pregnancy. HtrA1 has recently been reported to be upregulated in preeclampsia (PE), a pregnancy-specific systemic disorder primarily involving hypertension and proteinuria, typically ...
High temperature requirement A (HtrA) is a widely expressed chaperone and serine protease in bacteria. HtrA proteases assemble and hydrolyze misfolded proteins to enhance bacterial survival under stress condit......
The OHSS cDNA clone of 1759 bp was found to encode a protein of 492 amino acids whose molecular mass was estimated to be 54.7 kDa (Fig. 3). A homology search indicated that the C-terminal part of the deduced amino acid sequence was composed of a trypsin-like serine protease domain (Fig. 4). Serine proteases are involved in many biological process including digestion, blood clotting, proenzyme activation and complement activation (e.g. Neurath, 1984; Lanz et al., 1993; Rawlings and Barrett, 1994; Klein et al., 1996; Levine et al., 2001). Numerous serine proteases are synthesized as inactive zymogens. Zymogens prevent premature physiological functioning of the active portion of the protease, thus protecting host cells from enzymatic damage (Neurath and Walsh, 1976; Rawlings and Barrett, 1994).. The protein encoded in the OHSS cDNA would be a zymogen of OHSS, which is likely to be proteolytically activated. The Arg-Ile-Ile-Gly-Gly motif (Fig. 3) clearly corresponds to the typical Arg-Ile-(Ile or ...
セリンプロテアーゼ阻害剤(FOY-305)による中性セリンプロテアーゼ活性の抑制を介したラット肝化学発癌の抑制効 ...
BCX 1470 is a serine protease inhibitor with the IC50 of 96 nM for factor D and 1.6 nM for C1s. Serine proteases are enzymes that cleave peptide bonds in proteins which are found ubiquitously in both eukaryotes and prokaryotes and serine serves as the nucleophilic amino acid at the active site. According to structure, serine proteases are divided into trypsin-like (chymotrypsin-like) family and subtilisin-like family. It is reported that serine proteases play an important role in various physiological functions, including digestion, immune response, blood coagulation and reproduction. BCX 1470 is a potent serine protease inhibitor and functions on the complement enzymes CIs and factor D sites. By determining the ability of enzyme to hydrolyze appropriate synthetic substrates, the result showed that BCX 1470 inhibited the factor D and C1s esterolytic activity which were important in the function of serine protease. In induced dermal RPA reaction rat model, administration of BCX 1470 markedly ...
TYTU : Changes in expression of serine proteases HtrA1 and HtrA2 during estrogen-induced oxidative stress and nephrocarcinogenesis in male Syrian hamster ...
IVERIC bio, Inc. is a biopharmaceutical company. The Company is focused on the discovering and developing of treatment options for retinal diseases. The Company is developing both therapeutic product candidates for age-related retinal diseases and gene therapy product candidates for orphan inherited retinal diseases (IRDs). The Companys therapeutics portfolio consists of its clinical stage product candidate Zimura (avacincaptad pegol), a complement C5 inhibitor, and IC-500, its preclinical product candidate from its High temperature requirement A serine peptidase one protein (HtrA1), inhibitors program. Its lead gene therapy products also includes IC-100 and IC-200. ...
Mouse (Mus musculus) のHtra1 (HtrA serine peptidase 1)遺伝子を含むベクター、レンチウイルス、アデノウイルス、 (AAV) アデノ随伴、アデノ随伴ウイルス、MMLV レトロウイルス,、piggyBac, shRNA、gRNA、 ガイドRNA、 CRISPR-Cas9 、クリスパー、プラスミド
TY - JOUR. T1 - Expression and functional significance of HtrA1 loss in endometrial cancer. AU - Mullany, Sally A.. AU - Moslemi-Kebria, Mehdi. AU - Rattan, Ramandeep. AU - Khurana, Ashwani. AU - Clayton, Amy. AU - Ota, Takayo. AU - Mariani, Andrea. AU - Podratz, Karl C.. AU - Chien, Jeremy. AU - Shridhar, Viji. PY - 2011/2/1. Y1 - 2011/2/1. N2 - Purpose: The purpose of this study was to determine if loss of serine protease HtrA1 in endometrial cancer will promote the invasive potential of EC cell lines. Experimental design: Western blot analysis and immunohistochemistry methods were used to determine HtrA1 expression in EC cell lines and primary tumors, respectively. Migration, invasion assays and in vivo xenograft experiment were performed to compare the extent of metastasis between HtrA1 expressing and HtrA1 knocked down clones. Results: Western blot analysis of HtrA1 in 13 EC cell lines revealed complete loss of HtrA1 expression in all seven papillary serous EC cell lines. Downregulation of ...
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The mechanism of a single gene giving rise to greater than one mRNA transcript is referred to as differential splicing. This system is often tightly regulated in a cell-type or developmental stage-specific manner and increases genome complexity by generating different proteins from the same mRNA. The presence of more than one mRNA form for the same gene is common among kallikreins. These variant mRNAs may result from alternative splicing, a retained intronic segment, or use of an alternative.... ...
I think the work by Agard on alpha-lytic protease suggests something , ,like this. , , Isnt that the protein whose folding is catalysed by a part of itself, , the Pro-region? If this is true, then that does not argue against my , statement. I think that the fold, that the protein adopts, is the , global minimum of the molecule _with_ its Pro-region. After the , Pro-region is cleaved, the global minimum is elswhere in the fold , space, but it is kinetically inaccessible. Thus, the native protein , does not adopt its global minimum, but it *folds*to* the global , minimum. From the point of view of someone who wants to do something , with this protein, you may say that this makes no difference. But from , the point of view of someone reasoning about the principles of protein , folding, it does. I completely agree with all of the above. What then about plasminogen activator inhibitor, PAI-1. This protein, AFAIR, has an active (as an inhibitor) state, which is in higher energy than an inactive ...
Reaktivität: Meerschweinchen, Pferd, Human and more. 21 verschiedene TMPRSS11D Antikörper vergleichen. Alle direkt auf antikörper-online bestellbar!
Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity ...
Ki: 9.36 and 13.1 nM for chymotrypsin and chymase, respectively Chymostatin is a chymotryptase-like serine proteases inhibitor. Serine proteases are enzymes cleaving peptide bonds, in which serine plays as the nucleophilic amino acid. Serine proteases c
View mouse Tmprss6 Chr15:78439668-78468634 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
K08653 MBTPS1; membrane-bound transcription factor site-1 protease [EC:3.4.21.112] K01349 FURIN; furin [EC:3.4.21.75] K01359 PCSK1; proprotein convertase subtilisin/kexin type 1 [EC:3.4.21.93] K01360 PCSK2; proprotein convertase subtilisin/kexin type 2 [EC:3.4.21.94] K08671 PCSK4; proprotein convertase subtilisin/kexin type 4 [EC:3.4.21.-] K08654 PCSK5; proprotein convertase subtilisin/kexin type 5 [EC:3.4.21.-] K08654 PCSK5; proprotein convertase subtilisin/kexin type 5 [EC:3.4.21.-] K08672 PCSK6; proprotein convertase subtilisin/kexin type 6 [EC:3.4.21.-] K08673 PCSK7; proprotein convertase subtilisin/kexin type 7 [EC:3.4.21.-] K08673 PCSK7; proprotein convertase subtilisin/kexin type 7 [EC:3.4.21.-] K13050 PCSK9; proprotein convertase subtilisin/kexin type 9 [EC:3.4.21.-] K01280 TPP2; tripeptidyl-peptidase II [EC:3.4.14.10 ...
K08653 MBTPS1; membrane-bound transcription factor site-1 protease [EC:3.4.21.112] K01349 FURIN; furin [EC:3.4.21.75] K01359 PCSK1; proprotein convertase subtilisin/kexin type 1 [EC:3.4.21.93] K01360 PCSK2; proprotein convertase subtilisin/kexin type 2 [EC:3.4.21.94] K08654 PCSK5; proprotein convertase subtilisin/kexin type 5 [EC:3.4.21.-] K08672 PCSK6; proprotein convertase subtilisin/kexin type 6 [EC:3.4.21.-] K08673 PCSK7; proprotein convertase subtilisin/kexin type 7 [EC:3.4.21.-] K13050 PCSK9; proprotein convertase subtilisin/kexin type 9 [EC:3.4.21.-] K01280 TPP2; tripeptidyl-peptidase II [EC:3.4.14.10 ...
Proprotein Convertase Subtilisin/Kexin Type 9 (Proprotein Convertase 9 or Neural Apoptosis-Regulated Convertase 1 or PCSK9 or EC 3.4.21.) - Pipeline Review, H1 2016 Proprotein Convertase - Market research report and industry analysis - 10197474
Proprotein convertase subtilisin/kexin type 9 (PCSK9) regulates LDL cholesterol metabolism by targeting LDL receptors for degradation. Statins increase serum PCSK9 concentration limiting the potential of statins to reduce LDL cholesterol, whereas ezetimibe, inhibitor of cholesterol absorption, has ambiguous effects on circulating PCSK9 levels. Plant stanols also reduce cholesterol absorption, but their effect on serum PCSK9 concentration is not known. Therefore, we performed a controlled, randomized, double-blind study, in which 92 normo- to moderately hypercholesterolemic subjects (35 males and 57 females) consumed vegetable-oil spread 20 g/d enriched (plant stanol group, n=46) or not (control group, n=46) with plant stanol 3g/d as ester for 6 months. Fasting blood samples were drawn at baseline and at the end of the study. Serum PCSK9 concentration was analyzed with Quantikine Elisa Immunoassay, serum and lipoprotein lipids enzymatically, and serum non-cholesterol sterols with gas-liquid ...
We read with interest the article by Rashid and colleagues1 in Circulation in which they studied the physiological role of proprotein convertase subtilisin/kexin type 9 (PCSK9) in intestinal triglyceride-rich lipoprotein production. In that article, Rashid et al stated that few investigators have characterized the functional importance of PCSK9 in the small intestine and its regulatory role on triglyceride-rich lipoprotein metabolism.1 However, they omitted 2 seminal articles that previously addressed the question.. We demonstrated and published in 2009 in Arteriosclerosis, Thrombosis, and Vascular Biology that PCSK9-deficient mice display reduced postprandial hypertriglyceridemia after an olive oil gavage.2 Using the lymph duct cannulation method, we also showed that PCSK9-deficient mice have reduced intestinal apolipoprotein B production compared with wild-type mice.2 Finally, we confirmed this relationship between intestinal PCSK9 and apolipoprotein B secretion in vitro in differentiated ...
PCSK1N (proprotein convertase subtilisin/kexin type 1 inhibitor), Authors: Dessen P. Published in: Atlas Genet Cytogenet Oncol Haematol.
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Proprotein convertase subtilisin/kexin 9 inhibitors in reducing cardiovascular outcomes: a systematic review and meta-analysis ...
The mature PCSK9 binds with LDLR protein to form a complex to direct LDLR protein toward lysosome for degradation. Thus, PCSK9 inhibits LDLR expression at a post-transcriptional level and plays a critical role in cholesterol homeostasis.23 In addition to SREBP2, we have reported that PPARγ is another transcription factor activating PCSK9 transcription because a PPRE exists in the PCSK9 promoter.24 In the current study, at cellular levels, we determined that PCSK9 expression can be induced by AdipoR agonists, and the induction was completed by activating PPARγ pathway. The induction of PCSK9 expression/secretion was also observed in wild-type mice. Meanwhile, AdipoR agonists activated SRE in the promoter of LDLR, but not of PCSK9, which resulted in a direct induction of LDLR expression by AdipoR agonists and surpassed the facilitation of LDLR degradation by increased PCSK9. Therefore, the long-term ADP355 treatment decreased serum total and LDL-C levels, but increased apoE levels in wild-type ...
Proprotein convertase involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues (By similarity). In males, important for ADAM2 processing as well as other acrosomal proteins with roles in fertilization and critical for normal fertilization events such as sperm capacitation, acrosome reaction and binding of sperm to zona pellucida (By similarity). Plays also a role in female fertility, involved in the regulation of trophoblast migration and placental development, may be through the proteolytical processing and activation of proteins such as IGF2 (PubMed:16040806). May also participate in folliculogenesis in the ovaries (By similarity).
Introduction: CAT-2003 is an orally active small molecule that inhibits SREBP maturation (nSREBP-1 and nSREBP-2) and activation of SREBP-target genes, including PCSK9. CAT-2003 mechanism of action was studied in HepG2 cells and in the transgenic ApoE*3 Leiden mouse model of hyperlipoproteinemia.. Methods and Results: In vitro, CAT-2003 was studied in HepG2 cells and dose dependently reduced mature SREBP-2 protein levels (50% at 25 μM, n=3), PCSK9 mRNA (IC50 16.2 +/- 1.1 μM, n=3), and PCSK9 protein secretion (IC50 = 17.8 +/- 1.1 μM, n=3). CAT-2003 treatment also reduced expression of other SREBP target genes as well as SREBP processing genes including those encoding for HMG-CoA reductase, SCD-1, ACC2, S1P and S2P proteins. The reduction in PCSK9 protein correlated dose dependently with an increase in both low and high molecular weight LDLR protein. Statins increase nSREBP-2 and increase the production of PCSK9. CAT-2003 reversed atorvastatin-induced increases in nSREBP-2 and PCSK9 production ...
We examine the secondary preventive effect of acute phase use of PCSK9 inhibitors after coronary intervention in patients with acute myocardial infarction.
Reaktivität: Fledermaus, Huhn, Rind (Kuh) and more. 63 verschiedene PCSK2 Antikörper vergleichen. Alle direkt auf antikörper-online bestellbar!
Japans largest platform for academic e-journals: J-STAGE is a full text database for reviewed academic papers published by Japanese societies
sp:NEC1_MOUSE tr:Q32MU0_MOUSE] Pcsk1, Nec-1, Nec1, PC1, PC3, Phpp-1, SPC3; proprotein convertase subtilisin/kexin type 1; K01359 proprotein convertase subtilisin/kexin type 1 [EC:3.4.21.93] ...
sp:NEC1_MOUSE] Pcsk1, Nec-1, Nec1, PC1, PC3, Phpp-1, SPC3; proprotein convertase subtilisin/kexin type 1; K01359 proprotein convertase subtilisin/kexin type 1 [EC:3.4.21.93] ...
A total of 406 participants were randomized to the AMG 145 treatment arms, placebo arms, and the ezetimibe arm, with approximately 45 participants per arm. The mean age of the patients was 51 years, 34% were men, and 79% were white. Mean LDL-C concentration at baseline was 3.7 mmol/L. Of the patients enrolled, 21% of patients had two or more cardiovascular risk factors, 32% had metabolic syndrome, and no one had a history of coronary artery disease. AMG 145 significantly reduced LDL-C concentrations in all dose groups. The changes from baseline were -41.0% (95% confidence interval -46.2 to -35.8) for the AMG 70 mg/2-week dose; -43.9% (-49.0 to -38.7) for the 105 mg/2-week dose; and -50.9% (-56.2 to -45.7) for the 140 mg/2-week dose. Doses given every 4 weeks also resulted in reduced LDL-C. The changes from baseline were -39.0% (-44.1 to -34.0) for the 280 mg/4-week dose; -43.2% (-48.3 to -38.1) for the 350 mg/4-week dose; and -48.0% (-53.1 to -42.9) for the 420 mg/4-week dose. The placebo groups ...
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Oryzin (EC 3.4.21.63, Aspergillus alkaline proteinase, aspergillopeptidase B, API 21, aspergillopepsin B, aspergillopepsin F, Aspergillus candidus alkaline proteinase, Aspergillus flavus alkaline proteinase, Aspergillus melleus semi-alkaline proteinase, Aspergillus oryzae alkaline proteinase, Aspergillus parasiticus alkaline proteinase, Aspergillus serine proteinase, Aspergillus sydowi alkaline proteinase, Aspergillus soya alkaline proteinase, Aspergillus melleus alkaline proteinase, Aspergillus sulphureus alkaline proteinase, prozyme, P 5380, kyorinase, seaprose S, semi-alkaline protease, sumizyme MP, prozyme 10, onoprose, onoprose SA, protease P, promelase) is an enzyme. This enzyme catalyses the following chemical reaction Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyse peptide amides This enzyme is a predominant extracellular alkaline endopeptidase of the mold Aspergillus oryzae. Nakagawa, Y. (1970). Alkaline proteinases from Aspergillus. ...
TY - JOUR. T1 - Multifaceted analyses of epidermal serine protease activity in patients with atopic dermatitis. AU - Nomura, Hayato. AU - Suganuma, Mutsumi. AU - Takeichi, Takuya. AU - Kono, Michihiro. AU - Isokane, Yuki. AU - Sunagawa, Ko. AU - Kobashi, Mina. AU - Sugihara, Satoru. AU - Kajita, Ai. AU - Miyake, Tomoko. AU - Hirai, Yoji. AU - Yamasaki, Osamu. AU - Akiyama, Masashi. AU - Morizane, Shin. PY - 2020/2. Y1 - 2020/2. N2 - The serine proteases kallikrein-related peptidase (KLK) 5 and KLK7 cleave cell adhesion molecules in the epidermis. Aberrant epidermal serine protease activity is thought to play an important role in the pathogenesis of atopic dermatitis (AD). We collected the stratum corneum (SC) from healthy individuals (n = 46) and AD patients (n = 63) by tape stripping and then measuring the trypsin-and chymotrypsin-like serine protease activity. We also analyzed the p.D386N and p.E420K of SPINK5 variants and loss-of-function mutations of FLG in the AD patients. The serine ...
Cell-cell fusion and cell invasion are essential for placental development. Human cytotrophoblasts in the chorionic villi may undergo cell-cell fusion to form syncytiotrophoblasts to facilitate nutrient-gas exchange or differentiate into extravillous trophoblasts (EVTs) to facilitate maternal-fetal circulation. The placental transcription factor glial cells missing 1 (GCM1) regulates syncytin-1 and -2 expression to mediate trophoblast fusion. Interestingly, GCM1 and syncytin-1 are also expressed in EVTs with unknown physiological functions. In this study, we performed chromatin immunoprecipitation-on-chip (ChIP-chip) analysis and identified the gene for high-temperature requirement protein A4 (HtrA4) as a GCM1 target gene, which encodes a serine protease facilitating cleavage of fibronectin and invasion of placental cells. Importantly, HtrA4 is immunolocalized in EVTs at the maternal-fetal interface, and its expression is decreased by hypoxia and in preeclampsia, a pregnancy complication associated with
Serine Protease Autotransporters of Enterobacteriaceae (SPATEs) constitute a large family of proteases secreted by Escherichia coli and Shigella. SPATEs exhibit two distinct proteolytic activities. First, a C-terminal catalytic site triggers an intra-molecular cleavage that releases the N-terminal portion of these proteins in the extracellular medium. Second, the secreted N-terminal domains of SPATEs are themselves proteases; each contains a canonical serine-protease catalytic site. Some of these secreted proteases are toxins, eliciting various effects on mammalian cells. Here, we discuss the biogenesis of SPATEs and their function as toxins.
Introduction: Anti-proprotein convertase subtilisin/kexin type 9 (PCSK9) antibodies have been very effective to lower low-density lipoprotein (LDL)-cholesterol. They attracted the attention on PCSK9 enzyme role in multiple pathways and underlined the complex correlations between lipid metabolism and various other liver or extrahepatic diseases, that are insufficiently known. Hepatocyte nuclear factor 1, sterol regulatory element-binding protein (SREBP) 1c and SREBP2 are the main modulators of liver PCSK9 gene and protein expression, processes that can also be influenced by some natural and synthetic compounds (as berberine, or bortezomib and rosuvastatin, respectively), endoplasmic reticulum stress, metabolic status and the diurnal pattern.. Aim: This minireview is an analysis of PCSK9 involvement in liver pathology.. Results and Conclusion: PCSK9 is a key enzyme which increases LDL-receptor degradation. Hepatitis C virus (HCV) enters into hepatocytes in combination with lipoproteins through ...
PCSK9 inhibitor and high cholesterol. Computer illustration of low-density lipoprotein (LDL, bad cholesterol) molecules (round) bound to LDL receptor (LDLR) proteins, with a molecule of the enzyme proprotein convertase subtilisin/kexin type 9 (PCSK9, blue) bound to a PCSK9 inhibitor antibody (pink). When there are high levels of LDL cholesterol in the blood it builds up on the sides of blood vessels hardening them, a condition named atherosclerosis. This narrows the blood vessels and may block them. LDL receptors recognise and bind to LDL molecules to remove them from the bloodstream. When PCSK9 binds to an LDLR, the receptor is destroyed along with the LDL particle. But if PCSK9 does not bind, the receptor can return to the surface of the cell and remove more cholesterol. Monoclonal antibodies that bind to and inhibit PCSK9 are being used to reduce the amount of cholesterol in the blood by improving the livers ability to recycle LDLRs. - Stock Image C026/3508
Lipoprotein and PCSK9 bound to receptor. Computer illustration of a low-density lipoprotein (LDL), or bad cholesterol, molecule (round) and a molecule of the enzyme proprotein convertase subtilisin/kexin type 9 (PCSK9, blue) bound to an LDL receptor (LDLR) protein (Y-shaped), with red blood cells (erythrocytes, discs) in a blood vessel (not to scale). When there are high levels of LDL cholesterol in the blood it builds up on the sides of blood vessels hardening them, a condition named atherosclerosis. This narrows the blood vessels and may block them. LDL receptors recognise and bind to LDL molecules to remove them from the bloodstream. When PCSK9 binds to an LDLR, the receptor is destroyed along with the LDL particle. But if PCSK9 does not bind, the receptor can return to the surface of the cell and remove more cholesterol. PCSK9 inhibitor drugs reduce the amount of cholesterol in the blood by improving the livers ability to recycle LDLRs. - Stock Image C026/3517
Hepatitis C virus (HCV) associates with lipoproteins to form lipoviral particles (LVPs) that can facilitate viral entry into hepatocytes. Initial attachment occurs via heparan sulphate proteoglycans and low-density lipoprotein receptor (LDLR); CD81 then mediates a post-attachment event. Proprotein convertase subtilisin kexin type 9 (PCSK9) enhances the degradation of the LDLR and modulates liver CD81 levels. We measured LVP and PCSK9 in patients chronically infected with HCV genotype (G)3. PCSK9 concentrations were also measured in HCV-G1 to indirectly examine the role of LDLR in LVP clearance.. ...
Intracellular serine protease-1 (ISP-1) from Bacillus subtilis had been previously purified to homogeneity. The purified protease (Mr = 31,000) had undergone processing to remove 17 to 20 amino-terminal amino acid residues. Then observations and a number of other studies led to the proposal that ISP-1 is synthesized in B. subtilis cells as an inactive precursor, which may undergo activation by amino-terminal processing. To examine these questions, monospecific polyclonal antibodies against ISP-1 were raised. A variety of procedures for extracting ISP-1 from cells under conditions that prevent proteolysis in vitro were evaluated by immunobloting and ISP-1 activity assays. ISP-1 was found to be always produced in a form (Mr = 34,000) that was larger than the purified form. This larger form was readily converted to the smaller form in vitro in crude extracts at pH 8.5 in the presence of Ca$\sp{2+}$ ions. It was also found that the appearance of ISP-1 activity and immunologically cross-reactive ...
At baseline, human chymase gene expression in heart was significantly higher but chymase activity is similar between WT and Tg mice. Treatment with LPS Tg mice showed cardiac hypertrophy, and heart chymase activity tended to show higher than in WT mice but these changes were not statistically significant. Previous studies showed that sepsis is associated with cardiovascular dysfunction [3]. We therefore speculate that LPS-induced cardiovascular dysfunction may be augmented, at least in part, by over-expression of the human chymase gene. This concept is consistent with a recent study by Koga et al. [9] that showed human chymase expression in mice induces mild hypertension with left ventricular hypertrophy, characterized by cardiomyocyte hyperplasia and increased fibrosis in the left ventricle. From this data it is difficult to explain about the role of human chymase in LPS-induced increase mortality is due to cardiovascular dysfunction. Because of the low prevalence of survival of LPS induced Tg ...
However, achieving LDL levels of 70 mg/dL or lower in patients with high initial values is often not possible with statins alone, even with maximum dosages.It needs often combination with other drugs (like ezetimibe). Consequently,the search for new cholesterol-lowering interventions is mandatory.. The number of LDL-R expressed on the surface of hepatocytes is the primary determinant of plasma LDL levels.It binds plasma LDL on the hepatocyte surface, mediating LDL uptake and delivery to the endosomal system, where the LDL particle is released, and the LDL-R is recycled back to the hepatocyte surface to bind LDL particles.. The PCSK9 (proprotein convertase subtilisin/kexin type 9.)protein appears to control the number of low-density lipoprotein receptors,which determines how quickly cholesterol (in the form of low-density lipoproteins) is removed from the bloodstream. Studies suggest that the PCSK9 protein helps control blood cholesterol levels by breaking down low-density lipoprotein receptors ...
Complete information for PCSK1N gene (Protein Coding), Proprotein Convertase Subtilisin/Kexin Type 1 Inhibitor, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Complete information for PCSK9 gene (Protein Coding), Proprotein Convertase Subtilisin/Kexin Type 9, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Our recent findings indicate that hepatocyte CD36 is involved in the regulation of the IR (insulin receptor) in the liver and this modulates insulin action on glucose and lipid metabolism, including de-novo lipogenesis (DNL) and hepatic glucose production (HGP). We also identify the influence of hepatic CD36 in transcriptional effects of insulin on Pcsk9 (Proprotein convertase subtilisin/kexin type 9) and Angptl3 (Angiopoietin-like 3), which are essential effectors of triglyceride (TG)/lipoprotein clearance. These findings suggest a link between CD36 signaling, FA flux and insulin action in regulation of liver metabolism and function in lipoprotein clearance. This is highly relevant to our understanding of hepatic insulin sensitivity and diabetic dyslipidemia and etiology of cardiovascular disease ...
(HealthDay)-Proprotein convertase subtilisin/kexin type 9 (PCSK9) monoclonal antibodies may represent a promising treatment option for acute coronary syndrome (ACS), according to a review published online March 22 in the ...
PARIS and TARRYTOWN, N.Y., July 24, 2015 /PRNewswire/ - Sanofi and Regeneron Pharmaceuticals, Inc. announced today that the U.S. Food and Drug Administration (FDA) approved Praluent® (alirocumab) Injection, the first FDA-approved treatment in a new class of drugs known as PCSK9 (proprotein convertase subtilisin/kexin type 9) inhibitors. Praluent is indicated as an adjunct to diet and maximally tolerated statin therapy for the treatment of adults with heterozygous familial hypercholesterolemia or clinical atherosclerotic cardiovascular disease (ASCVD), who require additional lowering of low-density lipoprotein (LDL) cholesterol. The effect of Praluent on cardiovascular morbidity and mortality has not been determined.. Praluent is the first and only PCSK9 inhibitor approved in the U.S. and is available in two different doses (75 mg and 150 mg). Both doses of Praluent are available in a single 1 milliliter (mL) injection delivered in a single-dose prefilled pen or syringe that patients ...
MONDAY, Oct. 30, 2017 (HealthDay News) -- A combination of clinical factors and payer type increase the likelihood of approval for proprotein convertase subtilisin/kexin type 9 inhibitor (PCSK9i) treatment, and rates of approval are low overall, according to a study published online Oct. 30 in Circulation.. Gregory P. Hess, M.D., from the University of Pennsylvania in Philadelphia, and colleagues conducted a retrospective cohort study using nationwide pharmacy claims linked to electronic medical records. The data set included more than 220 million patients from all 50 states and all payer types, with 5,140 distinct health plans. In the pharmacy data set, PCSK9i prescriptions were submitted for 51,466 patients. Approval or rejection of PCSK9i prescription claims was the main outcome.. The researchers found that 47 percent of patients who were prescribed a PCSK9i were approved for coverage by the payer. Age ,65 years, history of atherosclerotic cardiovascular disease, prescription by a ...
Values are mean ± SD, n (%), or median (Q1, Q3).. ApoB = apolipoprotein B; ASCVD = atherosclerotic cardiovascular disease; CD4 = cluster of differentiation 4; HDL-C = high-density lipoprotein cholesterol; HIV = human immunodeficiency virus; LDL-C = low-density lipoprotein cholesterol; Lp(a) = lipoprotein(a); NNRTI = non-nucleoside reverse transcriptase inhibitor; NRTI = nucleoside reverse transcriptase inhibitor; PCSK9 = proprotein convertase subtilisin/kexin type 9; Q = quartile; QM = monthly; VLDL-C = very low-density lipoprotein cholesterol.. ...
The introduction of singular therapies, such as proprotein convertase subtilisin/kexin type 9 inhibitors (PCSK9i), to lower high cholesterol levels requires better classification of patients eligible for intensive lipid lowering therapy. According to the European Medicines Administration, PCSK9i are recommended in primary prevention only in familial hypercholesterolemia (FH) patients. Therefore, an FH diagnosis is not simply an academic issue, because it has many clinical implications. The bases of a diagnosis of FH are not entirely clear. The availability of genetic testing, including large genome-wide association analyses and whole genome studies, has shown that some patients with a clinical diagnosis of definite FH have no mutations in the genes associated with the disease. This fact does not exclude the very high cardiovascular risk of these patients, and an early and intensive lipid lowering therapy is recommended in all FH patients. Because an FH diagnosis is a cornerstone for decisions ...
Alirocumab (SAR236553/REGN727) is a fully human monoclonal antibody that binds PCSK9 (proprotein convertase subtilisin/kexin type 9).. Primary Objective of the study:. To demonstrate the reduction of low-density lipoprotein cholesterol (LDL-C) by alirocumab as add-on therapy to stable maximally tolerated daily statin therapy in comparison with ezetimibe after 24 weeks of treatment in participants with hypercholesterolemia at high cardiovascular (CV) risk.. Secondary Objectives:. ...
Alirocumab (SAR236553/REGN727) is a fully human monoclonal antibody that binds PCSK9 (proprotein convertase subtilisin/kexin type 9).. Primary Objective of the study:. To demonstrate the reduction of low-density lipoprotein cholesterol (LDL-C) by alirocumab as add-on therapy to stable maximally tolerated daily statin therapy in comparison with ezetimibe after 24 weeks of treatment in participants with hypercholesterolemia at high cardiovascular (CV) risk.. Secondary Objectives:. ...
Elevated low-density lipoprotein (LDL) cholesterol is one of the leading causes of cardiovascular disease. Proprotein convertase subtilisin/kexin type 9
A rare glimpse into the prior authorization requirements implemented by public and private insurance providers across the country has found substantial administrative burden for a new class of medications for patients with high cholesterol that places them at high risk for heart attack or stroke. So-called proprotein convertase subtilisin/kexin type 9 (PCSK9) inhibitors are self-injected medications approved for individuals with a genetic condition called familial hypercholesterolemia (FH) and those with atherosclerotic cardiovascular disease (ASCVD) who have high cholesterol despite receiving traditional statin medications and other treatments. Results of the study are published in Circulation: Cardiovascular Quality and Outcomes.. ...
A rare glimpse into the prior authorization requirements implemented by public and private insurance providers across the country has found substantial administrative burden for a new class of medications for patients with high cholesterol that places them at high risk for heart attack or stroke. So-called proprotein convertase subtilisin/kexin type 9 (PCSK9) inhibitors are self-injected medications approved for individuals with a genetic condition called familial hypercholesterolemia (FH) and those with atherosclerotic cardiovascular disease (ASCVD) who have high cholesterol despite receiving traditional statin medications and other treatments. Results of the study are published in Circulation: Cardiovascular Quality and Outcomes.. ...
We thank Drs. Cao and Li for their comment (1) on our article (2). We also think that the tools available to check the risk of any rare adverse event, such as worsening type 2 diabetes or new-onset diabetes, lack precision. In our case, a large set of evidence and the potential clinical utility of therapy with proprotein convertase subtilisin/kexin type 9 inhibitors (PCSK9i) provide plausibility for the investigation and relevance for the report.. A major limitation that we had to deal with in our meta-analysis is the fact that PCSK9i studies were not designed for testing the hypothesis and hence no information was available on the concomitant use and titration of antidiabetes medicines up or down. This drawback may certainly overshadow the sizing of the effect as well as its statistical significance (2). To partially overcome this issue, we separated individuals with and without diabetes at study entry and found very similar results in both groups, reducing our concern about this potential ...
When plasmin breaks down fibrin, a number of soluble parts are produced. These are called fibrin degradation products (FDPs). FDPs compete with thrombin, and thus slow down clot formation by preventing the conversion of fibrinogen to fibrin. This effect can be seen in the thrombin clotting time (TCT) test, which is prolonged in a person that has active fibrinolysis.. FDPs, and a specific FDP, the D-dimer, can be measured using antibody-antigen technology. This is more specific than the TCT, and confirms that fibrinolysis has occurred. It is therefore used to indicate deep-vein thrombosis, pulmonary embolism, DIC and efficacy of treatment in acute myocardial infarction. Alternatively, a more rapid detection of fibrinolytic activity, especially hyperfibrinolysis, is possible with thromboelastometry (TEM) in whole blood, even in patients on heparin. In this assay, increased fibrinolysis is assessed by comparing the TEM profile in the absence or presence of the fibrinolysis inhibitor aprotinin. ...
Drotrecogin alpha (activated) belongs to the class of serine proteases. Drotrecogin alfa has not been found to improve outcomes ...
... acts as an acetylating agent where an acetyl group is covalently attached to a serine residue in the active site of the ...
These drugs deplete the active form of the vitamin by inhibiting the enzyme vitamin K epoxide reductase and thus the recycling of the inactive vitamin K epoxide back to the active reduced form of vitamin K. The drugs are structurally similar to vitamin K and act as competitive inhibitors of the enzyme. The term "vitamin K antagonist" is a misnomer, as the drugs do not directly antagonise the action of vitamin K in the pharmacological sense, but rather the recycling of vitamin K. Vitamin K is required for the proper production of certain proteins involved in the blood clotting process. For example, it is needed to carboxylate specific glutamic acid residues on prothrombin. Without these residues carboxylated, the protein will not form the appropriate conformation of thrombin, which is needed to produce the fibrin monomers that are polymerized to form clots.[1] The action of this class of anticoagulants may be reversed by administering vitamin K for the duration of the anticoagulant's residence in ...
The drug is clear with a pH of 10.[7] Its production is inhibited indirectly by NSAIDs, which inhibit the cyclooxygenase enzymes COX1 and COX2. These convert arachidonic acid to prostaglandin H2 (PGH2), the immediate precursor of prostacyclin. Since thromboxane (an eicosanoid stimulator of platelet aggregation) is also downstream of COX enzymes, one might think that the effect of NSAIDs would act to balance. However, prostacyclin concentrations recover much faster than thromboxane levels, so aspirin administration initially has little to no effect but eventually prevents platelet aggregation (the effect of prostaglandins predominates as they are regenerated). This is explained by understanding the cells that produce each molecule, TXA2 and PGI2. Since PGI2 is primarily produced in a nucleated endothelial cell, the COX inhibition by NSAID can be overcome with time by increased COX gene activation and subsequent production of more COX enzymes to catalyze the formation of PGI2. In contrast, TXA2 is ...
... (Ro 48-3657, proposed brand name Xubix) is the double prodrug of Ro-44-3888, which is a platelet aggregation inhibitor. It was being developed for secondary prevention of arterial thrombosis following unstable angina pectoris and acute myocardial infarction (MI). On August 6, 1999, Hoffmann-La Roche announced that the preliminary results from Phase III clinical trials had not shown that sibrafiban was better than aspirin in preventing recurrent ischemic events in patients suffering from acute coronary syndrome. The development of sibrafiban was terminated. ...
In industry, EDTA is mainly used to sequester metal ions in aqueous solution. In the textile industry, it prevents metal ion impurities from modifying colors of dyed products. In the pulp and paper industry, EDTA inhibits the ability of metal ions, especially Mn2+, from catalyzing the disproportionation of hydrogen peroxide, which is used in chlorine-free bleaching. In a similar manner, EDTA is added to some food as a preservative or stabilizer to prevent catalytic oxidative decoloration, which is catalyzed by metal ions.[4] In soft drinks containing ascorbic acid and sodium benzoate, EDTA mitigates formation of benzene (a carcinogen).[5] The reduction of water hardness in laundry applications and the dissolution of scale in boilers both rely on EDTA and related complexants to bind Ca2+, Mg2+, as well as other metal ions. Once bound to EDTA, these metal centers tend not to form precipitates or to interfere with the action of the soaps and detergents. For similar reasons, cleaning solutions often ...
As of March 2017, brands included Aclop, Actaclo, Agregex, Agrelan, Agrelax, Agreless, Agrelex, Agreplat, Anclog, Angiclod, Anplat, Antiagrex, Antiban, Antigrel, Antiplaq, Antiplar, Aplate, Apolets, Areplex, Artepid, Asogrel, Atelit, Atelit, Ateplax, Atervix, Atheros, Athorel, Atrombin, Attera, Bidogrel, Bigrel, Borgavix, Carder, Cardogrel, Carpigrel, Ceraenade, Ceruvin, Cidorix, Clatex, Clavix, Clentel, Clentel, Clidorel, Clodel, Clodelib, Clodian, Clodil, Cloflow, Clofre, Clogan, Clogin, Clognil, Clogrel, Clogrelhexal, Clolyse, Clont, Clood, Clopacin, Clopcare, Clopeno, Clopex Agrel, Clopez, Clopi, Clopid, Clopida, Clopidep, Clopidexcel, Clopidix, Clopidogrel, Clopidogrelum, Clopidomed, Clopidorex, Clopidosyn, Clopidoteg, Clopidowel, Clopidra, Clopidrax, Clopidrol, Clopigal, Clopigamma, Clopigrel, Clopilet, Clopimed, Clopimef, Clopimet, Clopinovo, Clopione, Clopiright, Clopirite, Clopirod, Clopisan, Clopistad, Clopistad, Clopitab, Clopithan, Clopitro, ClopiVale, Clopivas, Clopivaz, Clopivid, ...
... Antithrombotic agents is a therapeutic subgroup of the Anatomical Therapeutic Chemical Classification System, a system of alphanumeric codes developed by the World Health Organization (WHO) for the classification of drugs and other medical products.[1][2] Subgroup B01 is part of the anatomical group B Blood and blood forming organs.[3] Codes for veterinary use (ATCvet codes) can be created by placing the letter Q in front of the human ATC code: for example, QB01.[4] National issues of the ATC classification may include additional codes not present in this list, which follows the WHO version.. ...
Wikimedia Commons has media related to Serine endopeptidases.. EC 3.4.21 Serine endopeptidases ...
The extracellular matrix is degraded by serine endopeptidases and metalloproteinases. Examples of such metalloproteinases are ... The embryo releases serine proteases which causes the epithelial cell membrane to depolarize and activates the epithelial Na+ ...
It is a serine endopeptidase (protease group S1, PA clan). Factor X is synthesized in the liver and requires vitamin K for its ... Factor X is an enzyme, a serine endopeptidase, which plays a key role at several stages of the coagulation system. Factor X is ... Factor Xa is inactivated by protein Z-dependent protease inhibitor (ZPI), a serine protease inhibitor (serpin). The affinity of ... "Complementary DNA cloning and kinetic characterization of a novel intracellular serine proteinase inhibitor: mechanism of ...
CS1 maint: discouraged parameter (link) Serine Endopeptidases: Advances in Research and Application: 2011 Edition. ...
... "serine-type endopeptidase activity" (GO:0004252)". Amigo. Gene Ontology Consortium. Retrieved 2018-10-17. "GO:0008236 serine- ... Assembled in the genome of the clavibacter michiganensis specie, It is a putative serine protease gene that belongs to the ... This is possible due to the catalytic triad in their active site of their protein sequence: Aspartate, Serine and Histidine ( ... Universal protein resource accession number A5CU31 for "sbtB - Putative serine protease, peptidase family S8A - Clavibacter ...
"Yeast KEX2 genes encodes an endopeptidase homologous to subtilisin-like serine proteases". Biochemical and Biophysical Research ... paired-basic endopeptidase, yeast cysteine proteinase F, paired-basic endopeptidase, andrenorphin-Gly-generating enzyme, ... Kexin (EC 3.4.21.61) is a prohormone-processing protease, specifically a yeast serine peptidase, found in the budding yeast (S ... Mizuno K, Nakamura T, Ohshima T, Tanaka S, Matsuo H (February 1989). "Characterization of KEX2-encoded endopeptidase from yeast ...
Chymotrypsin is a serine endopeptidase that is present in pancreatic juice and helps the hydrolysis of proteins and peptide. It ... A covalent bond formed between the active site and DIFP, so the serine side chain is no longer available to the substrate. ... Many enzymes including serine protease, cysteine protease, protein kinase and phosphatase evolved to form transient covalent ... Diisopropyl fluorophosphate (DIFP) is an irreversible inhibitor that blocks the action of serine protease. When it binds to the ...
It is the zymogen form of factor XIIa, an enzyme (EC 3.4.21.38) of the serine protease (or serine endopeptidase) class. In ... Chung DW, Fujikawa K, McMullen BA, Davie EW (May 1986). "Human plasma prekallikrein, a zymogen to a serine protease that ...
... 1 is a serine endopeptidase, a specific type of protease that has the amino acid serine at its active site ... Studies of human pancreatic elastase 1 have shown that this serine protease maps to the chromosomal region 12q13 and it is ... Elastases form a subfamily of serine proteases, characterized by a distinctive structure consisting of two beta barrel domains ... or serine elastase. The first isozyme, pancreatic elastase 1, was initially thought to be expressed in the pancreas. However it ...
13 KD serine protease, or 24KD endopeptidase. Angiostatin is known to bind many proteins, especially to angiomotin and ...
... may refer to: IgA specific serine endopeptidase, an enzyme IgA-specific metalloendopeptidase, an enzyme This set ...
Sendai virus uses activating proteases that are serine endopeptidases represented by tryptase beta 2-(TPSB2),WikiGenes - ... For example, transmembrane serine protease 2 (TMPRSS2), which is an F-protein-processing enzyme, is often overexpressed in ... Not all cancer cells have cell entry receptors for the virus and not all cancer cells express virus processing serine proteases ... and transmembrane serine protease 2 (TMPRSS2). Most likely, blood clotting factor X (F10) is capable to cleave and activate SeV ...
... serine endopeptidases MeSH D08.811.277.656.300.760.030 - acrosin MeSH D08.811.277.656.300.760.176 - chymotrypsin MeSH D08.811. ... endopeptidase clp MeSH D08.811.277.656.149.500 - protease la MeSH D08.811.277.656.300 - endopeptidases MeSH D08.811.277.656. ... endopeptidase clp MeSH D08.811.277.656.300.760.247 - endopeptidase k MeSH D08.811.277.656.300.760.284 - enteropeptidase MeSH ... Serine-type D-Ala-D-Ala carboxypeptidase MeSH D08.811.277.656.350.245.280 - gamma-glutamyl hydrolase MeSH D08.811.277.656. ...
It is the type serine endopeptidase of MEROPS family S8. The structure of subtilisin has been determined by X-ray ... Subtilisins belong to subtilases, a group of serine proteases that - like all serine proteases - initiate the nucleophilic ... It is structurally unrelated to the chymotrypsin-clan of serine proteases, but uses the same type of catalytic triad in the ... Polgár L (1987). "Structure and function of serine proteases". In Brocklehurst K, Neuberger A (eds.). Hydrolytic enzymes. ...
... such as Val-Val This Escherichia coli serine endopeptidase is essential for the clearance of denatured proteins from the inner- ... Pallen MJ, Wren BW (October 1997). "The HtrA family of serine proteases". Molecular Microbiology. 26 (2): 209-21. doi:10.1046/j ... is an endopeptidase". Journal of Bacteriology. 172 (4): 1791-7. doi:10.1128/jb.172.4.1791-1797.1990. PMC 208670. PMID 2180903. ... a large serine protease containing multiple subunits". Archives of Biochemistry and Biophysics. 224 (2): 543-54. doi:10.1016/ ...
... s (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins, in which serine serves as the ... Serine Peptidase Serine Proteases site at Saint Louis University (SLU) Serine+proteases at the US National Library of Medicine ... The serine -OH attacks the carbonyl carbon, and the nitrogen of the histidine accepts the hydrogen from the -OH of the [serine ... Serine proteases are paired with serine protease inhibitors, which turn off their activity when they are no longer needed. ...
... (EC 3.4.21.67, E. coli cytoplasmic proteinase, proteinase So, Escherichia coli serine proteinase So) is an ... Endopeptidase+So at the US National Library of Medicine Medical Subject Headings (MeSH) Biology portal v t e. ... Chung CH, Goldberg AL (April 1983). "Purification and characterization of protease So, a cytoplasmic serine protease in ... or Bz-Arg-OEt This is an Escherichia coli cytoplasmic endopeptidase. Goldberg AL, Swamy KH, Chung CH, Larimore FS (1981). " ...
... (EC 3.4.21.57, plant Leu-proteinase, leucine-specific serine proteinase, leucine endopeptidase, spinach ... Leucyl+endopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Biology portal. ... Aducci P, Ascenzi P, Ballio A (October 1986). "Esterolytic Properties of Leucine-Proteinase, the Leucine-Specific Serine ... serine proteinase (leucine specific), spinach leucine-specific serine proteinase, Leu-proteinase) is an enzyme. This enzyme ...
... is a large cytosolic enzyme that belongs to a distinct class of serine peptidases. It was first described ... Prolyl endopeptidase is a cytosolic prolyl endopeptidase that cleaves peptide bonds on the C-terminal side of prolyl residues ... prolyl+endopeptidase,+human at the US National Library of Medicine Medical Subject Headings (MeSH) Prolyl Endopeptidase entry ... "Entrez Gene: PREP prolyl endopeptidase". Oliveira EB, Martins AR, Camargo AC (May 1976). "Isolation of brain endopeptidases: ...
... staphylococcal serine proteinase) is an extracellular bacterial serine protease of the glutamyl endopeptidase I family that was ... Glutamyl endopeptidase is in S. aureus expressed from the gene sspA within the operon ssp. Downstream of sspA, the operon also ... Glutamyl endopeptidase is expressed as a zymogen that, in order to become fully active, has been modified both through ... Glutamyl endopeptidase can inhibit the activation of targets within the complement system. It is indicated to cause inhibition ...
S. epidermidis glutamyl endopeptidase GluSE Also called S. epidermidis serine protease (Esp). S. warneri glutamyl endopeptidase ... subtilis glutamyl endopeptidase GluBS Enterococcus E. faecalis glutamyl endopeptidase SprE Glutamyl endopeptidase is in at ... Glutamyl endopeptidase I is a family of extracellular bacterial serine proteases. The proteases within this family have been ... Birktoft, Jens J.; Breddam, Klaus (1994). "[8] Glutamyl endopeptidases". Proteolytic Enzymes: Serine and Cysteine Peptidases. ...

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IgA-specific+serine+endopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Biology portal. ... IgA protease (EC 3.4.21.72, IgA-specific serine endopeptidase, IgA proteinase, IgA-specific proteinase, immunoglobulin A ... where the X in the squence preferably is a Proline or Serine; the Y = Threonine, Serine or Alanine; and Z preferably is ...
The Gene Ontology (GO) project is a collaborative effort to address the need for consistent descriptions of gene products across databases. You can use this browser to view terms, definitions, and term relationships in a hierarchical display. Links to summary annotated gene data at MGI are provided in Term Detail reports.
"Serine Endopeptidases" by people in this website by year, and whether "Serine Endopeptidases" was a major or minor topic of ... "Serine Endopeptidases" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis. ... Below are the most recent publications written about "Serine Endopeptidases" by people in Profiles. ...
Prolyl endopeptidase-like (PREPL) protein is structurally related to the serine peptidases belonging to the POP family. Based ... Furthermore, despite this lack of hydrolytic cleavage, the serine peptidase active site inhibitor phenylmethylsulfonyl fluoride ... α-Syn oligomerization/aggregation is accelerated by the serine peptidase, prolyl oligopeptidase (POP). Factors that affect POP ... PREPL (prolyl endopeptidase-like) protein is structurally related to the proteins from clan SC of the serine peptidases, family ...
Prolyl endopeptidase. Prolyl oligopeptidase (POP), also called prolyl endopeptidase, is a cytosolic enzyme that has been ... Orally active, brain penetrant, potent and specific prolyl endopeptidase (PPCE) inhibitor €125.00 ...
Purification and biochemical characterization of a vacuolar serine endopeptidase induced by glucose starvation in maize roots. ... RSIP is the first vacuolar serine endopeptidase to be identified. Glucose starvation induced RSIP: after 4 days of starvation, ... Purification and biochemical characterization of a vacuolar serine endopeptidase induced by glucose starvation in maize roots ... Purification and biochemical characterization of a vacuolar serine endopeptidase induced by glucose starvation in maize roots ...
Lysyl endopeptidase [3.4.21.50]. (0,0). (0,0,0). - 1: Mannan-binding lectin-associated serine protease-2 [3.4.21.104]. (0,0). ( ... IgA-specific serine endopeptidase [3.4.21.72]. (2,1). (2,0,0). - 1: Infectious pancreatic necrosis birnavirus Vp4 pept [3.4. ... Serine endopeptidases. (show info) Enzyme Commission (EC). Each enzyme is allocated a four-digit EC number, the first three ... 50494 - Trypsin-like serine proteases. 0. DIRECT. 50494,52540,52540. *50494 - Trypsin-like serine proteases. *52540 - P-loop ...
IgA-specific serine endopeptidase can also refer to... IgA‐specific serine endopeptidase ... IgA‐specific serine endopeptidase. in Oxford Dictionary of Biochemistry and Molecular Biology ... From: IgA‐specific serine endopeptidase in Oxford Dictionary of Biochemistry and Molecular Biology » ... Search for the text `IgA-specific serine endopeptidase anywhere in Oxford Index » ...
serine-type endopeptidase inhibitor activity. id: GO:0004867. name: serine-type endopeptidase inhibitor activity. namespace: ... Description: Stops, prevents or reduces the activity of serine-type endopeptidases, enzymes that catalyze the hydrolysis of ... nonterminal peptide bonds in a polypeptide chain; a serine residue (and a histidine residue) are at the active center of the ...
... an asparagine-specific endopeptidase, has been purified from germinating vetch (Vicia sativa L.) seeds. The final preparation ... Serine Endopeptidases / chemistry * Serine Endopeptidases / genetics * Serine Endopeptidases / isolation & purification* ... Proteinase B, an asparagine-specific endopeptidase, has been purified from germinating vetch (Vicia sativa L.) seeds. The final ... Purification, cDNA cloning and characterization of proteinase B, an asparagine-specific endopeptidase from germinating vetch ( ...
Find out information about Serine endopeptidase. A family of endopeptidases whose proteolytic activity involves the hydroxy ... group of the serine residue; they play an important role in digestion, blood... Explanation of Serine endopeptidase ... serine protease. (redirected from Serine endopeptidase) serine protease. [¦se‚rēn ′prōd·ə‚ās] (cell and molecular biology) A ... Serine endopeptidase , Article about Serine endopeptidase by The Free Dictionary https://encyclopedia2.thefreedictionary.com/ ...
GO:0004252 serine-type endopeptidase activity GO:0008236 serine-type peptidase activity GO:0070008 serine-type exopeptidase ...
When plasmin breaks down fibrin, a number of soluble parts are produced. These are called fibrin degradation products (FDPs). FDPs compete with thrombin, and thus slow down clot formation by preventing the conversion of fibrinogen to fibrin. This effect can be seen in the thrombin clotting time (TCT) test, which is prolonged in a person that has active fibrinolysis.. FDPs, and a specific FDP, the D-dimer, can be measured using antibody-antigen technology. This is more specific than the TCT, and confirms that fibrinolysis has occurred. It is therefore used to indicate deep-vein thrombosis, pulmonary embolism, DIC and efficacy of treatment in acute myocardial infarction. Alternatively, a more rapid detection of fibrinolytic activity, especially hyperfibrinolysis, is possible with thromboelastometry (TEM) in whole blood, even in patients on heparin. In this assay, increased fibrinolysis is assessed by comparing the TEM profile in the absence or presence of the fibrinolysis inhibitor aprotinin. ...
Drotrecogin alpha (activated) belongs to the class of serine proteases. Drotrecogin alfa has not been found to improve outcomes ...
Serine Endopeptidases/genetics. *Serine Endopeptidases/immunology*. *T-Lymphocytes, Cytotoxic/enzymology. *T-Lymphocytes, ... They kill target cells by multiple mechanisms, but utilize a pore-forming protein, perforin, and a family of serine proteinases ... Recent studies have demonstrated that perforin and serine proteinases synergistically trigger an endogenous pathway of ...
Serine endopeptidases. Non-topical/index: *Uses of Wikidata Infobox. Navigation menu. Personal tools. *English ...
... are any member of the group of Endopeptidases as serine proteases, containing at the active site a Serine residue involved in ... Serine Endopeptidases. "Serine Endopeptidases" In enzyme science, Serine Endopeptidases, as serine proteases, are any member of ... Mannan-Binding Lectin Serine Proteases) are serum serine proteases (serine endopeptidases), which participate in complement ... Serine Endopeptidases ⌊Life (Life Sciences). ⌊Catalysts. ⌊Biocatalysts. ⌊Enzymes. ⌊Hydrolases [EC 3] (Hydrolase Enzymes). ⌊ ...
Serine Endopeptidases. *Serine Endopeptidases: metabolism. *Serine Endopeptidases: physiology. *Skin. *Skin: blood supply ...
Serine Endopeptidases / genetics * Serine Endopeptidases / metabolism* * Serine Endopeptidases / pharmacology * Substrate ...
serine-type endopeptidase activity Source: InterPro. *serine-type exopeptidase activity Source: InterPro ... Prolyl endopeptidaseAdd BLAST. 710. Amino acid modifications. Feature key. Position(s). DescriptionActions. Graphical view. ... endopeptidase activity Source: RGD ,p>Inferred from Direct Assay,/p> ,p>Used to indicate a direct assay for the function, ... "Distribution of prolyl endopeptidase activities in rat and human brain.". Irazusta J., Larrinaga G., Gonzalez-Maeso J., Gil J. ...
serine-type endopeptidase activity Source: InterPro. *serine-type exopeptidase activity Source: InterPro ... Prolyl endopeptidaseAdd BLAST. 710. Amino acid modifications. Feature key. Position(s). DescriptionActions. Graphical view. ... "cDNA cloning of porcine brain prolyl endopeptidase and identification of the active-site seryl residue.". Rennex D., Hemmings B ... "Inactivation of prolyl endopeptidase by a peptidylchloromethane. Kinetics of inactivation and identification of sites of ...
... five serine-type proteases, two Zn2+ endopeptidases, two Zn2+-leucine aminopeptidases, and one Zn2+ carboxypeptidase (4,5). ... Purification of four serine endopeptidases. J. Biol. Chem. 247, 4144-4154.PubMedGoogle Scholar ... Amino acid sequence around the reactive serine residue of DFP-sensitive components with esterase activity. Biochim. Biophys. ... Activity of a serine enzyme in 6M guanidinium chloride. J. Biol. Chem. 247, 4155-4159.PubMedGoogle Scholar ...
transmembrane protease serine 5. Names. transmembrane protease, serine 5. NP_001275678.1. *EC 3.4.21.- ... Tryp_SPc; Trypsin-like serine protease. cd00190. Location:150 → 338. Tryp_SPc; Trypsin-like serine protease; Many of these are ... Tryp_SPc; Trypsin-like serine protease. cd00190. Location:174 → 407. Tryp_SPc; Trypsin-like serine protease; Many of these are ... Tryp_SPc; Trypsin-like serine protease. cd00190. Location:209 → 442. Tryp_SPc; Trypsin-like serine protease; Many of these are ...
Aeromonas sobria serine protease (ASP): a subtilisin family endopeptidase with multiple virulence activities. Imamura, Takahisa ...
Serine endopeptidases. Reaction(IUBMB). Selective cleavage of Arg!Gly bonds in fibrinogen to form fibrin and release ... Active-site mapping of bovine and human blood coagulation serine proteases using synthetic peptide 4-nitroanilide and thio ...
Serine endopeptidases. Reaction(IUBMB). Selective cleavage of -Arg18! and -Arg47! bonds in coagulogen to form coagulin and ... Further studies on lipopolysaccharide-sensitive serine protease zymogen (factor C): its isolation from Limulus polyphemus ...
... which depends critically on the proteolytic activity of the LPS-responsive serine protease zymogen factor C. In response to ... 0/Arthropod Proteins; 0/Enzyme Precursors; 0/Lipopolysaccharides; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.84/Limulus ... which depends critically on the proteolytic activity of the LPS-responsive serine protease zymogen factor C. In response to ...
AMPK is a serine/threonine protein kinase that acts as an ultra-sensitive cellular energy sensor maintaining the energy balance ... protein serine/threonine kinase activator activity - receptor activator activity - regulation of gene expression by genetic ... Serine Endopeptidases. *Tea. *Bladder Cancer. *Potassium Channels, Voltage-Gated. *Cancer Gene Expression Regulation ... positive regulation of protein serine/threonine kinase activity - positive regulation of receptor activity - positive ...
0 (Insect Proteins); 0 (Melanins); 0 (Membrane Proteins); EC 3.4.21.- (Serine Endopeptidases); EC 3.4.21.89 (type I signal ... Serina Endopeptidases/metabolismo. Tribolium/enzimologia. [Mh] Termos MeSH secund rio:. Animais. Feminino. Trato ...
  • Proteinase K, originally isolated from the mold Tritirachium album, is a serine protease with broad substrate specificity and relatively high proteolytic activity. (cusabio.com)
  • As opposed to control cells, the Gedatolisib NF-B that gathered in the nucleus of cells with high SAH amounts had not been phosphorylated at serine 536, an adjustment connected with activation from the transactivation potential of the transcription aspect. (morainetownshipdems.org)