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Gene Review

SERPINB10  -  serpin peptidase inhibitor, clade B...

Homo sapiens

Synonyms: Bomapin, PI-10, PI10, Peptidase inhibitor 10, Serpin B10, ...
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Disease relevance of SERPINB10


High impact information on SERPINB10

  • Bomapin PCR products were readily detected in normal bone marrow, which was designated as a medium mRNA level [3].
  • Therefore, we analyzed the expression of bomapin within cell lines that exhibited characteristics of the monocytic lineage [3].
  • Because PMA and TNF-alpha induce monocytic differentiation in THP-1 and AML-193 cells, these data increase the possibility that bomapin may play a role in the regulation of protease activities specifically in early stages of cellular differentiation [3].
  • Our group recently cloned the cDNA-encoding bomapin, a member of the serine protease inhibitor (serpin) superfamily, from a human bone marrow cDNA library (J Biol Chem 270:2675, 1995) [3].
  • These data suggest that bomapin expression may be elevated in hematopoietic cells of monocytic lineage [3].

Biological context of SERPINB10


Anatomical context of SERPINB10

  • A single 2.3-kilobase bomapin transcript is highly expressed in human bone marrow cells but was undetectable in all other analyzed human tissues [4].

Associations of SERPINB10 with chemical compounds

  • PI10-containing complexes are dissociated with conditions known to separate classical protease-serpin complexes (i.e., 1.5 m ammonium hydroxide in the presence of SDS) [2].
  • 1,2-Didecanoylglycerol (diC10) is taken up by human platelets and sequentially converted to 1,2-didecanoylphosphatidic acid (PA10) and 1,2-didecanoylphosphatidylinositol (PI10) [6].
  • Agents that increase cyclic AMP in platelets, such as prostacyclin and forskolin, sequentially convert diC10 to PA10 and PI10 [6].

Other interactions of SERPINB10

  • Three of the serpins, PI8, PI10, and PAI2 mapped to the same YACs, yA27D8 and yA24E4 [7].
  • Preflo corn starches (CH-10, CH-20, CH-30) and Preflo potato starches (P-250, PI-10, PJ-20) were evaluated and compared with respect to their pharmaceutical properties such as particle size, density, flowability, friability, and compression properties [8].

Analytical, diagnostic and therapeutic context of SERPINB10


  1. Nucleotide variations in genes encoding plasminogen activator inhibitor-2 and serine proteinase inhibitor B10 associated with prostate cancer. 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. J. Hum. Genet. (2005) [Pubmed]
  2. 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. Schleef, R.R., Chuang, T.L. J. Biol. Chem. (2000) [Pubmed]
  3. Expression of bomapin, a novel human serpin, in normal/malignant hematopoiesis and in the monocytic cell lines THP-1 and AML-193. Riewald, M., Chuang, T., Neubauer, A., Riess, H., Schleef, R.R. Blood (1998) [Pubmed]
  4. Molecular cloning of bomapin (protease inhibitor 10), a novel human serpin that is expressed specifically in the bone marrow. Riewald, M., Schleef, R.R. J. Biol. Chem. (1995) [Pubmed]
  5. Identification of a nuclear targeting domain in the insertion between helices C and D in protease inhibitor-10. Chuang, T.L., Schleef, R.R. J. Biol. Chem. (1999) [Pubmed]
  6. Incorporation of synthetic 1,2-diacylglycerol into platelet phosphatidylinositol is increased by cyclic AMP. Lapetina, E.G. FEBS Lett. (1986) [Pubmed]
  7. Cytoplasmic antiproteinase 2 (PI8) and bomapin (PI10) map to the serpin cluster at 18q21.3. Bartuski, A.J., Kamachi, Y., Schick, C., Overhauser, J., Silverman, G.A. Genomics (1997) [Pubmed]
  8. Evaluation of Preflo modified starches as new direct compression excipients. I. Tabletting characteristics. Sanghvi, P.P., Collins, C.C., Shukla, A.J. Pharm. Res. (1993) [Pubmed]
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