Serpins
A family of serine proteinase inhibitors which are similar in amino acid sequence and mechanism of inhibition, but differ in their specificity toward proteolytic enzymes. This family includes alpha 1-antitrypsin, angiotensinogen, ovalbumin, antiplasmin, alpha 1-antichymotrypsin, thyroxine-binding protein, complement 1 inactivators, antithrombin III, heparin cofactor II, plasminogen inactivators, gene Y protein, placental plasminogen activator inhibitor, and barley Z protein. Some members of the serpin family may be substrates rather than inhibitors of SERINE ENDOPEPTIDASES, and some serpins occur in plants where their function is not known.
alpha 1-Antitrypsin
alpha 1-Antichymotrypsin
Glycoprotein found in alpha(1)-globulin region in human serum. It inhibits chymotrypsin-like proteinases in vivo and has cytotoxic killer-cell activity in vitro. The protein also has a role as an acute-phase protein and is active in the control of immunologic and inflammatory processes, and as a tumor marker. It is a member of the serpin superfamily.
Leukocyte Elastase
Protein C Inhibitor
Complement C1 Inactivator Proteins
Protease Nexins
Molecular Sequence Data
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Amino Acid Sequence
Serine Endopeptidases
Pancreatic Elastase
Antithrombins
Serpin E2
Cathepsin G
alpha-2-Antiplasmin
A member of the serpin superfamily found in plasma that inhibits the lysis of fibrin clots which are induced by plasminogen activator. It is a glycoprotein, molecular weight approximately 70,000 that migrates in the alpha 2 region in immunoelectrophoresis. It is the principal plasmin inactivator in blood, rapidly forming a very stable complex with plasmin.
Cowpox virus
Antithrombin III
Prolamins
Cystatin A
Protein Conformation
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Heparin Cofactor II
Plasminogen Activator Inhibitor 1
Chymotrypsin
Trypsin Inhibitors
Granzymes
Models, Molecular
Sequence Alignment
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
Catechol Oxidase
Protease Inhibitors
Cathepsins
Sequence Homology, Amino Acid
Cucurbita
Protein Structure, Secondary
Chymases
Plasminogen Activator Inhibitor 2
Electrophoresis, Polyacrylamide Gel
Protein Binding
Binding Sites
Heparin
A highly acidic mucopolysaccharide formed of equal parts of sulfated D-glucosamine and D-glucuronic acid with sulfaminic bridges. The molecular weight ranges from six to twenty thousand. Heparin occurs in and is obtained from liver, lung, mast cells, etc., of vertebrates. Its function is unknown, but it is used to prevent blood clotting in vivo and vitro, in the form of many different salts.
Trypsin
MENT, a heterochromatin protein that mediates higher order chromatin folding, is a new serpin family member. (1/1699)
Terminal cell differentiation is correlated with the extensive sequestering of previously active genes into compact transcriptionally inert heterochromatin. In vertebrate blood cells, these changes can be traced to the accumulation of a developmentally regulated heterochromatin protein, MENT. Cryoelectron microscopy of chicken granulocyte chromatin, which is highly enriched with MENT, reveals exceptionally compact polynucleosomes, which maintain a level of higher order folding above that imposed by linker histones. The amino acid sequence of MENT reveals a close structural relationship with serpins, a large family of proteins known for their ability to undergo dramatic conformational transitions. Conservation of the "hinge region" consensus in MENT indicates that this ability is retained by the protein. MENT is distinguished from the other serpins by being a basic protein, containing several positively charged surface clusters, which are likely to be involved in ionic interactions with DNA. One of the positively charged domains bears a significant similarity to the chromatin binding region of nuclear lamina proteins and with the A.T-rich DNA-binding motif, which may account for the targeting of MENT to peripheral heterochromatin. MENT ectopically expressed in a mammalian cell line is transported into nuclei and is associated with intranuclear foci of condensed chromatin. (+info)The intracellular serpin proteinase inhibitor 6 is expressed in monocytes and granulocytes and is a potent inhibitor of the azurophilic granule protease, cathepsin G. (2/1699)
The monocyte and granulocyte azurophilic granule proteinases elastase, proteinase 3, and cathepsin G are implicated in acute and chronic diseases thought to result from an imbalance between the secreted proteinase(s) and circulating serpins such as alpha1-proteinase inhibitor and alpha1-antichymotrypsin. We show here that the intracellular serpin, proteinase inhibitor 6 (PI-6), is present in monocytes, granulocytes, and myelomonocytic cell lines. In extracts from these cells, PI-6 bound an endogenous membrane-associated serine proteinase to form an sodium dodecyl sulfate (SDS)-stable complex. Using antibodies to urokinase, elastase, proteinase 3, or cathepsin G, we demonstrated that the complex contains cathepsin G. Native cathepsin G and recombinant PI-6 formed an SDS-stable complex in vitro similar in size to that observed in the extracts. Further kinetic analysis demonstrated that cathepsin G and PI-6 rapidly form a tight 1:1 complex (ka = 6.8 +/- 0.2 x 10(6) mol/L-1s-1 at 17 degrees C; Ki = 9.2 +/- 0.04 x 10(-10) mol/L). We propose that PI-6 complements alpha1-proteinase inhibitor and alpha1-antichymotrypsin (which control extracellular proteolysis) by neutralizing cathepsin G that leaks into the cytoplasm of monocytes or granulocytes during biosynthesis or phagocytosis. Control of intracellular cathepsin G may be particularly important, because it has recently been shown to activate the proapoptotic proteinase, caspase-7. (+info)Role for caspase-mediated cleavage of Rad51 in induction of apoptosis by DNA damage. (3/1699)
We report here that the Rad51 recombinase is cleaved in mammalian cells during the induction of apoptosis by ionizing radiation (IR) exposure. The results demonstrate that IR induces Rad51 cleavage by a caspase-dependent mechanism. Further support for involvement of caspases is provided by the finding that IR-induced proteolysis of Rad51 is inhibited by Ac-DEVD-CHO. In vitro studies show that Rad51 is cleaved by caspase 3 at a DVLD/N site. Stable expression of a Rad51 mutant in which the aspartic acid residues were mutated to alanines (AVLA/N) confirmed that the DVLD/N site is responsible for the cleavage of Rad51 in IR-induced apoptosis. The functional significance of Rad51 proteolysis is supported by the finding that, unlike intact Rad51, the N- and C-terminal cleavage products fail to exhibit recombinase activity. In cells, overexpression of the Rad51(D-A) mutant had no effect on activation of caspase 3 but did abrogate in part the apoptotic response to IR exposure. We conclude that proteolytic inactivation of Rad51 by a caspase-mediated mechanism contributes to the cell death response induced by DNA damage. (+info)Bcl-xL blocks activation of related adhesion focal tyrosine kinase/proline-rich tyrosine kinase 2 and stress-activated protein kinase/c-Jun N-terminal protein kinase in the cellular response to methylmethane sulfonate. (4/1699)
The stress-activated protein kinase/c-Jun N-terminal protein kinase (JNK) is induced in response to ionizing radiation and other DNA-damaging agents. Recent studies indicate that activation of JNK is necessary for induction of apoptosis in response to diverse agents. Here we demonstrate that methylmethane sulfonate (MMS)-induced activation of JNK is inhibited by overexpression of the anti-apoptotic protein Bcl-xL, but not by caspase inhibitors CrmA and p35. By contrast, UV-induced JNK activity is insensitive to Bcl-xL. The results demonstrate that treatment with MMS is associated with an increase in tyrosine phosphorylation of related adhesion focal tyrosine kinase (RAFTK)/proline-rich tyrosine kinase 2 (PYK2), an upstream effector of JNK and that this phosphorylation is inhibited by overexpression of Bcl-xL. Furthermore, overexpression of a dominant-negative mutant of RAFTK (RAFTK K-M) inhibits MMS-induced JNK activation. The results indicate that inhibition of RAFTK phosphorylation by MMS in Bcl-xL cells is attributed to an increase in tyrosine phosphatase activity in these cells. Hence, treatment of Bcl-xL cells with sodium vanadate, a tyrosine phosphatase inhibitor, restores MMS-induced activation of RAFTK and JNK. These findings indicate that RAFTK-dependent induction of JNK in response to MMS is sensitive to Bcl-xL, but not to CrmA and p35, by a mechanism that inhibits tyrosine phosphorylation and thereby activation of RAFTK. Taken together, these findings support a novel role for Bcl-xL that is independent of the caspase cascade. (+info)Ligand binding properties of the very low density lipoprotein receptor. Absence of the third complement-type repeat encoded by exon 4 is associated with reduced binding of Mr 40,000 receptor-associated protein. (5/1699)
The very low density lipoprotein receptor (VLDLR) binds, among other ligands, the Mr 40,000 receptor-associated protein (RAP) and a variety of serine proteinase-serpin complexes, including complexes of the proteinase urokinase-type plasminogen activator (uPA) with the serpins plasminogen activator inhibitor-1 (PAI-1) and protease nexin-1 (PN-1). We have analyzed the binding of RAP, uPA.PAI-1, and uPA.PN-1 to two naturally occurring VLDLR variants, VLDLR-I, containing all eight complement-type repeats, and VLDLR-III, lacking the third complement-type repeat, encoded by exon 4. VLDLR-III displayed approximately 4-fold lower binding of RAP than VLDLR-I and approximately 10-fold lower binding of the most C-terminal one of the three domains of RAP. In contrast, the binding of uPA.PAI-1 and uPA.PN-1 to the two VLDLR variants was indistinguishable. Surprisingly, uPA.PN-1, but not uPA.PAI-1, competed RAP binding to both VLDLR variants. These observations show that the third complement-type repeat plays a crucial role in maintaining the contact sites needed for optimal recognition of RAP, but does not affect the proteinase-serpin complex contact sites, and that two ligands can show full cross-competition without sharing the same contacts with the receptor. These results elucidate the mechanisms of molecular recognition of ligands by receptors of the low density lipoprotein receptor family. (+info)Suppression of breast cancer growth and metastasis by a serpin myoepithelium-derived serine proteinase inhibitor expressed in the mammary myoepithelial cells. (6/1699)
A serpin was identified in normal mammary gland by differential cDNA sequencing. In situ hybridization has detected this serpin exclusively in the myoepithelial cells on the normal and noninvasive mammary epithelial side of the basement membrane and thus was named myoepithelium-derived serine proteinase inhibitor (MEPI). No MEPI expression was detected in the malignant breast carcinomas. MEPI encodes a 405-aa precursor, including an 18-residue secretion signal with a calculated molecular mass of 46 kDa. The predicted sequence of the new protein shares 33% sequence identity and 58% sequence similarity to plasminogen activator inhibitor (PAI)-1 and PAI-2. To determine whether MEPI can modulate the in vivo growth and progression of human breast cancers, we transfected a full-length MEPI cDNA into human breast cancer cells and studied the orthotopic growth of MEPI-transfected vs. control clones in the mammary fat pad of athymic nude mice. Overexpression of MEPI inhibited the invasion of the cells in the in vitro invasion assay. When injected orthotopically into nude mice, the primary tumor volumes, axillary lymph node metastasis, and lung metastasis were significantly inhibited in MEPI-transfected clones as compared with controls. The expression of MEPI in myoepithelial cells may prevent breast cancer malignant progression leading to metastasis. (+info)Regulation of pro-apoptotic leucocyte granule serine proteinases by intracellular serpins. (7/1699)
Caspase activation and apoptosis can be initiated by the introduction of serine proteinases into the cytoplasm of a cell. Cytotoxic lymphocytes have evolved at least one serine proteinase with specific pro-apoptotic activity (granzyme B), as well as the mechanisms to deliver it into a target cell, and recent evidence suggests that other leucocyte granule proteinases may also have the capacity to kill if released into the interior of cells. For example, the monocyte/granulocyte proteinase cathepsin G can activate caspases in vitro, and will induce apoptosis if its entry into cells is mediated by a bacterial pore-forming protein. The potent pro-apoptotic activity of granzyme B and cathepsin G suggests that cells producing these (or other) proteinases would be at risk from self-induced death if the systems involved in packaging, degranulation or targeting fail and allow proteinases to enter the host cell cytoplasm. The purpose of the present review is to describe recent work on a group of intracellular serine proteinase inhibitors (serpins) which may function in leucocytes to prevent autolysis induced by the granule serine proteinases. (+info)Anti-viral strategies of cytotoxic T lymphocytes are manifested through a variety of granule-bound pathways of apoptosis induction. (8/1699)
Cytotoxic T cells and natural killer cells together constitute a major defence against virus infection, through their ability to induce apoptotic death in infected cells. These cytolytic lymphocytes kill their targets through two principal mechanisms, and one of these, granule exocytosis, is essential for an effective in vivo immune response against many viruses. In recent years, the authors and other investigators have identified several distinct mechanisms that can induce death in a targeted cell. In the present article, it is postulated that the reason for this redundancy of lethal mechanisms is to deal with the array of anti-apoptotic molecules elaborated by viruses to extend the life of infected cells. The fate of such a cell therefore reflects the balance of pro-apoptotic (immune) and anti-apoptotic (viral) strategies that have developed over eons of evolutionary time. (+info)
Serpin
2 serpins), 42D (5 serpins), 43A (4 serpins), 77B (3 serpins) and 88E (2 serpins). Studies on Drosophila serpins reveal that ... The term uterine serpin refers to members of the serpin A clade that are encoded by the SERPINA14 gene. Uterine serpins are ... Amino acid sequence analysis has placed 14 of these serpins in serpin clade Q and three in serpin clade K with the remaining ... Examples of cross-class inhibitory serpins include serpin B4 a squamous cell carcinoma antigen 1 (SCCA-1) and the avian serpin ...
Uterine serpin
In other analyses, uterine serpins have been considered as a separate clade in the serpin superfamily. The uterine serpins are ... Ovine uterine serpin also binds to activin, IgM and IgA. Another possible role for uterine serpins is in the inhibition of ... Uterine serpins are members of the A clade of the serine protease inhibitor (serpin) superfamily of proteins and are encoded by ... There are two lines of evidence to indicate that uterine serpins do not function as protease inhibitors. Uterine serpins from ...
SERPIN A12
... serpin) family. In humans, Serpin A12 is encoded by the SERPINA12 gene. First discovered in 2005, Serpin A12 was highly ... Serpin A12 has a single protein domain consisting of 7 to 9 alpha helices and 3 beta strands (A,B,C). Serpins are a large group ... Serpin A12 (OL-64, Vaspin, Visceral adipose-specific serpin, Ser A12) is a glycoprotein that is a class A member of the serine ... Serpin A12 is coded by the 14q32.13 gene, on the 14th chromosome. Serpin A12 is made up of 414 amino acids. Its molecular ...
SERPINA2
Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 2 is a protein that in humans is encoded by ... Extracellular predictions of SERPINs and common domain clades show that ER localisation of SERPINA2 are most likely be more, ... The model was created using swissmodel in EXPASY, and has shown that SERPINA2 preserves a SERPIN reactive centre loop which is ... "Entrez Gene: Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 2". Retrieved 2017-09-21. Hofker ...
Heparin cofactor II
"Entrez Gene: SERPIND1 serpin peptidase inhibitor, clade D (heparin cofactor), member 1". Tollefsen, D M; Majerus, D W; Blank, M ... Pizzo SV (1989). "Serpin receptor 1: a hepatic receptor that mediates the clearance of antithrombin III-proteinase complexes". ... Griffith MJ, Carraway T, White GC, Dombrose FA (1983). "Serpin receptor 1: heparin cofactor activities in a family with ... Huntington, James A. (2005-01-01). "Heparin Activation of Serpins". Chemistry and Biology of Heparin and Heparan Sulfate: 367- ...
Michael Kanost
Meekins, David A.; Kanost, Michael R.; Michel, Kristin (2017). "Serpins in arthropod biology". Seminars in Cell & Developmental ... studying lipophorin and serpins in insect hemolymph. In 1991, Kanost became Assistant Professor of Biochemistry at Kansas State ...
Enzyme inhibitor
ISBN 978-3-527-65970-8. Sanrattana W, Maas C, de Maat S (2019). "SERPINs-From Trap to Treatment". Frontiers in Medicine. 6: 25 ... The most prominent example are serpins (serine protease inhibitors) which are produced by animals to protect against ...
Protein C inhibitor
... (PCI) is serine protease inhibitor of serpin type that is found in most tissues and fluids, including blood ... Serpins Activated protein C-protein C inhibitor GRCh38: Ensembl release 89: ENSG00000188488 - Ensembl, May 2017 GRCm38: Ensembl ... It is a 52kD glycoprotein and belongs to serine protease inhibitor ( Serpin) super family of protein. In the beginning protein ... Protein C inhibitor (PCI, SERPINA5) is a serine protease inhibitor (serpin) that limits the activity of protein C (an ...
Granzyme B
Kaiserman D, Bird PI (April 2010). "Control of granzymes by serpins". Cell Death and Differentiation. 17 (4): 586-95. doi: ...
Silicimonas
cite journal}}: Cite journal requires ,journal= (help) Crenn, K; Serpin, D; Lepleux, C; Overmann, J; Jeanthon, C (November 2016 ...
Antithrombin
Bjork, I; Olson, JE (1997). Antithrombin, A bloody important serpin (in Chemistry and Biology of Serpins). Plenum Press. pp. 17 ... Antithrombin is a serpin (serine protease inhibitor) and is thus similar in structure to most other plasma protease inhibitors ... The P' region of antithrombin is unusually long relative to the P' region of other serpins and in un-activated or heparin ... O'Reilly MS, Pirie-Shepherd S, Lane WS, Folkman J (1999). "Antiangiogenic activity of the cleaved conformation of the serpin ...
Caspase 8
Ye S, Goldsmith EJ (2002). "Serpins and other covalent protease inhibitors". Curr. Opin. Struct. Biol. 11 (6): 740-5. doi: ...
Rhomboid protease
In Toxoplasma specifically, some serpins inhibit rhomboids.: 519 A rhomboid in the Gram-negative bacterium Providencia stuartii ...
Albumin
They are not in the same family as vertebrate albumins: Ovalbumin is a storage protein in egg white (albumen). It is a serpin. ...
Maspin
Hence the serpin functions as a suicide inhibitor of the protease. This transition does not occur in serpins that lack ... Serpins have a complex structure, a key component of which is the reactive site loop, RSL. Inhibitory serpins transition ... Zou Z, Anisowicz A, Hendrix MJ, Thor A, Neveu M, Sheng S, Rafidi K, Seftor E, Sager R (1994). "Maspin, a serpin with tumor- ... A tumor suppressing serpin". Adv. Exp. Med. Biol. 425: 77-88. doi:10.1007/978-1-4615-5391-5_8. PMID 9433491. Sheng S (2006). " ...
Alpha-1 antitrypsin
A1AT is a 52-kDa serpin and, in medicine, it is considered the most prominent serpin; the terms α1-antitrypsin and protease ... Most serpins inactivate enzymes by binding to them covalently. These enzymes are released locally in relatively low ... Alpha-1 antitrypsin or α1-antitrypsin (A1AT, α1AT, A1A, or AAT) is a protein belonging to the serpin superfamily. It is encoded ... An extremely rare form of Pi, termed PiPittsburgh, functions as an antithrombin (a related serpin), due to a mutation ( ...
Ovalbumin
... displays sequence and three-dimensional homology to the serpin superfamily, but unlike most serpins it is not a ... When heated, ovalbumin undergoes a conformational change from its soluble, serpin structure into an insoluble all-β-sheet ... Gettins PG (December 2002). "Serpin structure, mechanism, and function". Chemical Reviews. 102 (12): 4751-804. doi:10.1021/ ... studies of serpin structure and function (the fact that ovalbumin does not inhibit proteases means that by comparing its ...
Plasminogen activator inhibitor-2
Like other serpins, PAI-2 has three beta sheets (A, B, C) and nine alpha helices (hA-hI). The structure of PAI-2 mutants have ... Due to its position on chromosome 18 close to the bcl-2 protooncogene and several other serpins, PAI-2's role in apoptosis has ... Plasminogen activator inhibitor-2 (placental PAI, SerpinB2, PAI-2), a serine protease inhibitor of the serpin superfamily, is a ... Mikus P, Ny T (April 1996). "Intracellular polymerization of the serpin plasminogen activator inhibitor type 2". The Journal of ...
Heat shock protein 47
... , also known as SERPINH1 is a serpin which serves as a human chaperone protein for collagen. This protein ... "Entrez Gene: SERPINH1 serpin peptidase inhibitor, clade H (heat shock protein 47), member 1, (collagen binding protein 1)". ... Gettins PG (December 2002). "Serpin structure, mechanism, and function". Chemical Reviews. 102 (12): 4751-804. doi:10.1021/ ... is a member of the serpin superfamily of serine proteinase inhibitors. Its expression is induced by heat shock. HSP47 is ...
B13R (virus protein)
SPI-2 belongs in superfamily of the inhibitors of serine proteases (serpins). Serpins are the most broadly distributed family ... In mammals serpins are secreted in plasma where they serve as inhibitors of proteases involved in blood coagulation, ... Kettle S, Blake NW, Law KM, Smith GL (January 1995). "Vaccinia virus serpins B13R (SPI-2) and B22R (SPI-1) encode M(r) 38.5 and ... Vaccinia virus encodes two more serpin - SPI-1 and SPI-3. SPI-1 influences the host range and SPI-3 stops infected cells from ...
Hi-C (genomic analysis technique)
"Scaling Concepts in Serpin Polymer Physics". Materials. 14 (10): 2577. Bibcode:2021Mate...14.2577R. doi:10.3390/ma14102577. ...
SERPINB4
Serpin B4 is a protein that in humans is encoded by the SERPINB4 gene. Serpin GRCh38: Ensembl release 89: ENSG00000206073 - ... 2000). "Circulating serpin tumor markers SCCA1 and SCCA2 are not actively secreted but reside in the cytosol of squamous ... 2003). "SCCA2-like serpins mediate genetic predisposition to skin tumors". Cancer Res. 63 (8): 1871-5. PMID 12702576. Pontisso ... "Entrez Gene: SERPINB4 serpin peptidase inhibitor, clade B (ovalbumin), member 4". Barnes RC, Worrall DM (1995). "Identification ...
Neutrophil elastase
One group of inhibitors are the Serpins (Serine Protease Inhibitors). Neutrophil elastase has been shown to interact with Alpha ... 2-antiplasmin, which belongs to the Serpin family of proteins. Elastase ENSG00000197561 GRCh38: Ensembl release 89: ...
C1-inhibitor
The C-terminal serpin domain is similar to other serpins, which is the part of C1-inhibitor that provides the inhibitory ... C1-inhibitor is the largest member among the serpin superfamily of proteins. It can be noted that, unlike most family members, ... C1-inhibitor (C1-inh, C1 esterase inhibitor) is a protease inhibitor belonging to the serpin superfamily. Its main function is ... 2006). "An overview of the serpin superfamily". Genome Biology. 7 (5): 216. doi:10.1186/gb-2006-7-5-216. PMC 1779521. PMID ...
Acute-phase protein
Others give negative feedback on the inflammatory response, e.g. serpins. Alpha 2-macroglobulin and coagulation factors affect ...
DEFA1
Panyutich AV, Hiemstra PS, van Wetering S, Ganz T (1995). "Human neutrophil defensin and serpins form complexes and inactivate ...
Actinic keratosis
The role of serin peptidase inhibitors (Serpins) is also being investigated. SerpinA1 was found to be elevated in the ...
Trypsin inhibitor
A trypsin inhibitor (TI) is a protein and a type of serine protease inhibitor (serpin) that reduces the biological activity of ... Serpins - including trypsin inhibitors - are irreversible and suicide substrate-like inhibitors. It destructively alters ... Cohen, Maja; Davydov, Olga; Fluhr, Robert (2019-02-05). "Plant serpin protease inhibitors: specificity and duality of function ... "The Serpins Are an Expanding Superfamily of Structurally Similar but Functionally Diverse Proteins". Journal of Biological ...
Thyroxine-binding globulin
In terms of genomics, TBG is a serpin; however, it has no inhibitory function like many other members of this class of proteins ...
L1 (protein)
February 2014). "Serpins promote cancer cell survival and vascular co-option in brain metastasis". Cell. 156 (5): 1002-16. doi: ... However, recent studies have noted these cancer cells overproduce anti-PA serpins, which are the usual inhibitors of plasmin, ...
dna simple - Serpins
Conformational changes in serpins: I. The native and cleaved conformations of α<sub>1</sub>...
The serpin structures illustrate detailed control of conformation within a single protein. Serpins are also an unusual family ... The serpin structures illustrate detailed control of conformation within a single protein. Serpins are also an unusual family ... The serpin structures illustrate detailed control of conformation within a single protein. Serpins are also an unusual family ... The serpin structures illustrate detailed control of conformation within a single protein. Serpins are also an unusual family ...
Onuma Y et al. (2006),
A Serpin family gene, protease nexin-1 has an a... -
Paper
A Serpin family gene, protease nexin-1 has an activity distinct from protease inhibition in early Xenopus embryos. Onuma Y , ... Protease nexin-1 (PN-1)/glia-derived nexin (GDN) is a member of the Serpin (serine proteinase inhibitor) family, and can ... which is essential for the protease inhibitory activity of all serpins, had effects on Xenopus development indistinguishable ...
Vaccinia virus serpins B13R and B22R do not inhibit antigen presentation to class I-restricted cytotoxic T lymphocytes. -...
Cytotoxicity assays showed that deletion of the VV serpin genes B13R and B22R and other genes between B13R and B24R did not ... Recombinant VVs were constructed which express influenza virus proteins HA, NP or NS1 and which lack serpin gene B13R or both ... CD8+ CTL was compared to the lysis of cells infected with viruses expressing both the influenza proteins and the serpin genes. ... Vaccinia virus serpins B13R and B22R do not inhibit antigen presentation to class I-restricted cytotoxic T lymphocytes. ...
Structural basis for redox regulation of Yap1 transcription factor localization | Nature
Orphanet: Search a disease
AGT gene: MedlinePlus Genetics
SCOPe 2.08: Domain d1r1li : 1r1l I
SERPINA6 gene: MedlinePlus Genetics
6-aminohexanoic acid - Ontology Report - Rat Genome Database
Salivary proteome of aphthous stomatitis reveals the participation of vitamin metabolism, nutrients, and bacteria | medRxiv
Biomarker Correlates of Survival in Pediatric Patients with Ebola Virus Disease - Volume 20, Number 10-October 2014 - Emerging...
Pathophysiological Changes in the Hemostatic System and Anti... : Transplantation
Factor X
Hereditary Angioedema: Practice Essentials, Background, Pathophysiology
Alpha 1 Antitrypsin Antibody [AAT/1379] - Cat. No. 33-599 | ProSci
New project investigates potentially lethal angiooedema - Newsfood - Nutrimento e Nutrimente - News dal mondo Food
MeSH Browser
It is a member of the serpin superfamily.. Terms. Antithrombin III Preferred Term Term UI T003049. Date01/01/1999. LexicalTag ... Serpin C1 Thrombate III Pharm Action. Antithrombins. Registry Number. 9000-94-6. NLM Classification #. QV 193. Public MeSH Note ... Serpin C1 Term UI T734786. Date02/09/2009. LexicalTag NON. ThesaurusID NLM (2010). ... It is a member of the serpin superfamily.. Entry Term(s). Antithrombin III-Alpha Atenativ Heparin Co-Factor I Heparin Cofactor ...
Publications - Salk Institute for Biological Studies
SerpinB13 antibodies promote β cell development and resistance to type 1 diabetes - Fingerprint
- Experts@Minnesota
Reactome | 3x4Hyp-COL13A1 [endoplasmic reticulum lumen]
Cross-talk between red blood cells and plasma influences blood flow and omics phenotypes in severe COVID-19 | eLife
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Peptidase1
- Serpin peptidase inhibitor (SERPINB5) haplotypes are associated with susceptibility to hepatocellular carcinoma. (cdc.gov)
Inhibitor5
- Here we report the biochemical and genetic characterization of a Drosophila serine protease inhibitor protein, Serpin-27A, which regulates the melanization cascade through the specific inhibition of the terminal protease prophenoloxidase-activating enzyme. (elsevier.com)
- Protease nexin-1 (PN-1)/glia-derived nexin (GDN) is a member of the Serpin (serine proteinase inhibitor) family, and can inhibit thrombin, plasmin , and plasminogen activators. (xenbase.org)
- Factor Xa is inactivated by protein Z-dependent protease inhibitor (ZPI), a serine protease inhibitor (serpin). (bionity.com)
- Alpha-1 Antitrypsin or alpha1-antitrypsin (A1AT) is a protease inhibitor belonging to the serpin superfamily. (prosci-inc.com)
- Acute episodes of HAE in Europe tend to be treated by giving the patient a serine protease inhibitor (serpin) protein (C1-INH). (newsfood.com)
Superfamily1
- It is a member of the serpin superfamily. (nih.gov)
SERine Proteinase1
- The serpins (SERine Proteinase INhibitors) are a family of proteins with important physiological roles, including but not limited to the inhibition of chymotrypsin-like serine proteinases. (elsevier.com)
Protein2
- The serpin structures illustrate detailed control of conformation within a single protein. (elsevier.com)
- Braun BC, Meyer HA, Reetz A, Fuhrmann U, Kohrle J. Effect of mutations of the human serpin protein corticosteroid-binding globulin on cortisol-binding, thermal and protease sensitivity. (medlineplus.gov)
Gene3
- 2006), A Serpin family gene, protease nexin-1 has an a. (xenbase.org)
- A Serpin family gene, protease nexin-1 has an activity distinct from protease inhibition in early Xenopus embryos. (xenbase.org)
- Recombinant VVs were constructed which express influenza virus proteins HA, NP or NS1 and which lack serpin gene B13R or both B13R and B22R. (ox.ac.uk)
Inhibitory3
- In inhibitory serpins, in the cleaved (R) state the reactive centre loop forms an additional strand within the β-sheet. (elsevier.com)
- Determination of the structures of inhibitory serpins in multiple conformational states permits a detailed analysis of the mechanism of the S → R transition, and of the way in which a single sequence can form two stabilised states of different topology. (elsevier.com)
- Interestingly, expression of point or deletion mutation of the Reactive Center Loop of xPN1,which is essential for the protease inhibitory activity of all serpins, had effects on Xenopus development indistinguishable from those of wild type xPN-1. (xenbase.org)
Genes3
- We have investigated whether VV genes B13R and B22R, which encode proteins with amino acid similarity to serine protease inhibitors (serpins), are involved in this process. (ox.ac.uk)
- The lysis of cells infected with these viruses by influenza virus-specific CD8+ CTL was compared to the lysis of cells infected with viruses expressing both the influenza proteins and the serpin genes. (ox.ac.uk)
- Cytotoxicity assays showed that deletion of the VV serpin genes B13R and B22R and other genes between B13R and B24R did not increase the level of lysis, indicating that these genes are not involved in inhibition of antigen presentation of the epitopes tested. (ox.ac.uk)
Proteins1
- Serpins are also an unusual family of proteins in which homologues have native states with different folding topologies. (elsevier.com)
Member1
- To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. (neuromics.com)
Activity1
- Our data demonstrate that Serpin-27A is required to restrict the phenoloxidase activity to the site of injury or infection, preventing the insect from excessive melanization. (elsevier.com)
Control1
- Control of the coagulation system by serpins. (bvsalud.org)