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Papers In Press, published online ahead of print October 16, 2001
Pediatrics, Harvard Medical School, Children's Hospital, Boston, MA 02115
Corresponding Author: gary.silverman{at}tch.harvard.edu
Members of the human serpin family regulate a diverse array of serine and cysteine proteinases associated with essential biological processes such as fibrinolysis, coagulation, inflammation, cell mobility, cellular differentiation and apoptosis. Most serpins are secreted and attain physiologic concentrations in the blood and extracellular fluids. However, a subset of the serpin superfamily, the ov-serpins, also resides intracellularly. Using high-throughput genomic sequence, we identified a novel member of the human ov-serpin gene family, SERPINB12. The gene mapped to the ov-serpin cluster at 18q21 and resided between SERPINB5 (maspin) and SERPINB13 (headpin). The presence of SERPINB12 in silico was confirmed by cDNA cloning. Expression studies showed that SERPINB12 was expressed in many tissues including brain, bone marrow, lymph node, heart, lung, liver, pancreas, testis, ovary and intestines. Based on the presence of Arg and Ser at the reactive center of the RSL, SERPINB12 appeared to be an inhibitor of trypsin-like serine proteinases. This hypothesis was confirmed as recombinant SERPINB12 inhibited human trypsin and plasmin, but not thrombin, coagulation factor Xa or uPA. The second-order rate constants for the inhibitory reactions were 2.5 ± 1.6 x 105 M-1 s-1 and 1.6 ± 0.2 x 104 M-1 s-1, respectively. These data show that SERPINB12 encodes for a new functional member of the human ov-serpin family.
J. Biol. Chem, 10.1074/jbc.M108879200
Submitted on September 14, 2001
Revised on October 12, 2001
Accepted on October 16, 2001
SerpinB12 is a novel member of the human OV-serpin family that is widely expressed and inhibits trypsin-like serine proteinases
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