SERPINB10

The superfamily of high molecular weight serine proteinase inhibitors (serpins) regulate a diverse set of intracellular and extracellular processes such as complement activation, fibrinolysis, coagulation, cellular differentiation, tumor suppression, apoptosis, and cell migration. Serpins are characterized by a well-conserved tertiary structure that consists of 3 beta sheets and 8 or 9 alpha helices.{{cite journal | vauthors = Huber R, Carrell RW | title = Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins | journal = Biochemistry | volume = 28 | issue = 23 | pages = 8951–66 | date = November 1989 | pmid = 2690952 | doi = 10.1021/bi00449a001 }} A critical portion of the molecule, the reactive center loop connects beta sheets A and C. Protease inhibitor-10 (PI10; SERPINB10) is a member of the ov-serpin subfamily, which, relative to the archetypal serpin PI1, is characterized by a high degree of homology to chicken ovalbumin, lack of N- and C-terminal extensions, absence of a signal peptide, and a serine rather than an asparagine residue at the penultimate position.* {{cite journal | vauthors = Bartuski AJ, Kamachi Y, Schick C, Overhauser J, Silverman GA | title = Cytoplasmic antiproteinase 2 (PI8) and bomapin (PI10) map to the serpin cluster at 18q21.3 | journal = Genomics | volume = 43 | issue = 3 | pages = 321–8 | date = August 1997 | pmid = 9268635 | doi = 10.1006/geno.1997.4827 }}

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• {{cite journal | vauthors = Chuang TL, Schleef RR | title = Identification of a nuclear targeting domain in the insertion between helices C and D in protease inhibitor-10 | journal = The Journal of Biological Chemistry | volume = 274 | issue = 16 | pages = 11194–8 | date = April 1999 | pmid = 10196205 | doi = 10.1074/jbc.274.16.11194 | doi-access = free }}
• {{cite journal | vauthors = Lindskog C, Korsgren O, Pontén F, Eriksson JW, Johansson L, Danielsson A | title = Novel pancreatic beta cell-specific proteins: antibody-based proteomics for identification of new biomarker candidates | journal = Journal of Proteomics | volume = 75 | issue = 9 | pages = 2611–20 | date = May 2012 | pmid = 22465717 | doi = 10.1016/j.jprot.2012.03.008 }}
• {{cite journal | vauthors = Schleef RR, Chuang TL | title = Protease inhibitor 10 inhibits tumor necrosis factor alpha -induced cell death. Evidence for the formation of intracellular high M(r) protease inhibitor 10-containing complexes | journal = The Journal of Biological Chemistry | volume = 275 | issue = 34 | pages = 26385–9 | date = August 2000 | pmid = 10871600 | doi = 10.1074/jbc.C000389200 | doi-access = free }}
• {{cite journal | vauthors = Przygodzka P, Ramstedt B, Tengel T, Larsson G, Wilczynska M | title = Bomapin is a redox-sensitive nuclear serpin that affects responsiveness of myeloid progenitor cells to growth environment | journal = BMC Cell Biology | volume = 11 | pages = 30 | date = April 2010 | pmid = 20433722 | pmc = 2874763 | doi = 10.1186/1471-2121-11-30 | doi-access = free }}
• {{cite journal | vauthors = Shioji G, Ezura Y, Nakajima T, Ohgaki K, Fujiwara H, Kubota Y, Ichikawa T, Inoue K, Shuin T, Habuchi T, Ogawa O, Nishimura T, Emi M | title = Nucleotide variations in genes encoding plasminogen activator inhibitor-2 and serine proteinase inhibitor B10 associated with prostate cancer | journal = Journal of Human Genetics | volume = 50 | issue = 10 | pages = 507–15 | year = 2005 | pmid = 16172807 | doi = 10.1007/s10038-005-0285-1 | doi-access = free }}
• {{cite journal | vauthors = Riewald M, Schleef RR | title = Molecular cloning of bomapin (protease inhibitor 10), a novel human serpin that is expressed specifically in the bone marrow | journal = The Journal of Biological Chemistry | volume = 270 | issue = 45 | pages = 26754–7 | date = November 1995 | pmid = 7592909 | doi = 10.1074/jbc.270.45.26754 | doi-access = free }}

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{{Serpins}}

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