Disease relevance of SERPINB10

• A case-control study involving 292 prostate-cancer patients and 384 controls revealed significant differences in regard to distribution of four missense variations in genes encoding plasminogen activator inhibitor 2 (PAI2) and SERPINB10 [1].
• Protease inhibitor 10 (PI10) is a member of the ovalbumin family of serine protease inhibitors (ov-serpin) that is expressed at elevated levels in patients with acute myeloid leukemia and chronic myelomonocytic leukemia [2].
• Blood from patients with chronic myeloid leukemia (n = 6), chronic myelomonocytic leukemia (n = 6), acute myeloid leukemia (n = 5), and acute lymphocytic leukemia (n = 5) exhibited low to medium levels of bomapin expression [3].
• Furthermore, a high level of bomapin expression was detected in one individual with acute monocytic leukemia [3].
• In peripheral blood, bomapin expression was low or undetectable in normal donors (n = 6) and patients with chronic lymphocytic leukemia (n = 6) [3].

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

• Strong linkage disequilibrium in the region encompassing PAI2 and SERPINB10 extended to about 50 kbp [1].
• The level of PI10 expression in the stable transfectants was found to correlate with their resistance to TNFalpha-induced cell death [2].
• The restricted expression of bomapin to the bone marrow raises the possibility that this serpin may play a role in the regulation of protease activities during hematopoiesis [4].
• Transfection of HeLa cells with plasmids encoding enhanced green fluorescent protein (EGFP) coupled to PI-10 revealed an intense fluorescence of the nucleus [5].

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

• Molecular cloning of bomapin (protease inhibitor 10), a novel human serpin that is expressed specifically in the bone marrow [4].
• Immunoprecipitation/immunoblotting experiments demonstrated that PI10 is able to form SDS-stable complexes (i.e. M(r) >100,000) with a cytosolic protein(s) [2].
• Bomapin antigen levels were correspondingly reduced after treatment with PMA [3].
• Northern blotting confirmed these results and showed that the expression of bomapin in THP-1 cells was downregulated over a 4-day period by PMA and, to a lesser extent, TNF-alpha [3].

References