SERPINB10
Serpin peptidase inhibitor, clade B (ovalbumin), member 10 is a protein that in humans is encoded by the SERPINB10 gene.
[3]
Function
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 (Huber and Carrell, 1989 [PubMed 2690952]). 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 (MIM 107400), 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 (summary by Bartuski et al., 1997 [PubMed 9268635]).
References
Further reading
- Chuang, T. L.; Schleef, R. R. (1999). "Identification of a nuclear targeting domain in the insertion between helices C and D in protease inhibitor-10". The Journal of Biological Chemistry. 274 (16): 11194–8. doi:10.1074/jbc.274.16.11194. PMID 10196205.
- Lindskog, C; Korsgren, O; Pontén, F; Eriksson, J. W.; Johansson, L; Danielsson, A (2012). "Novel pancreatic beta cell-specific proteins: Antibody-based proteomics for identification of new biomarker candidates". Journal of Proteomics. 75 (9): 2611–20. doi:10.1016/j.jprot.2012.03.008. PMID 22465717.
- Huber, R; Carrell, R. W. (1989). "Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins". Biochemistry. 28 (23): 8951–66. doi:10.1021/bi00449a001. PMID 2690952.
- Bartuski, A. J.; Kamachi, Y; Schick, C; Overhauser, J; Silverman, G. A. (1997). "Cytoplasmic antiproteinase 2 (PI8) and bomapin (PI10) map to the serpin cluster at 18q21.3". Genomics. 43 (3): 321–8. doi:10.1006/geno.1997.4827. PMID 9268635.
- Schleef, R. R.; Chuang, T. L. (2000). "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 of Biological Chemistry. 275 (34): 26385–9. doi:10.1074/jbc.C000389200. PMID 10871600.
- Przygodzka, P; Ramstedt, B; Tengel, T; Larsson, G; Wilczynska, M (2010). "Bomapin is a redox-sensitive nuclear serpin that affects responsiveness of myeloid progenitor cells to growth environment". BMC Cell Biology. 11: 30. doi:10.1186/1471-2121-11-30. PMC 2874763
. PMID 20433722.
- 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 (2005). "Nucleotide variations in genes encoding plasminogen activator inhibitor-2 and serine proteinase inhibitor B10 associated with prostate cancer". Journal of Human Genetics. 50 (10): 507–15. doi:10.1007/s10038-005-0285-1. PMID 16172807.
- Riewald, M; Schleef, R. R. (1995). "Molecular cloning of bomapin (protease inhibitor 10), a novel human serpin that is expressed specifically in the bone marrow". The Journal of Biological Chemistry. 270 (45): 26754–7. doi:10.1074/jbc.270.45.26754. PMID 7592909.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.