Biological and Pharmaceutical Bulletin
Online ISSN : 1347-5215
Print ISSN : 0918-6158
ISSN-L : 0918-6158
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Identification of the Substrates for Plasma Hyaluronan Binding Protein
Nam-Ho CHOI-MIURAMadoka YODAKiyomi SAITOKatsuhiko TAKAHASHIMotowo TOMITA
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2001 Volume 24 Issue 2 Pages 140-143

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Abstract
Plasma hyaluronan biding protein (PHBP) is a novel serine protease, which has an amino acid sequence homology to that of hepatocyte growth factor activator (HGFA), and has a similar domain structure to that of urinary plasminogen activator (u-PA), found in human plasma. We searched the PHBP substrate in human plasma by measuring the digested protein bands on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The results showed that fibrinogen and fibronectin were the major substrates of PHBP. PHBP cleaved the α-chain at multiple sites and the β-chain between lysine53 and lysine54 but not the γ-chain of fibrinogen. Therefore, PHBP did not initiate the formation of the fibrin clot and did not cause the fibrinolysis directly. PHBP did not cleave (activate) prothrombin and plasminogen, but it converted the inactive single chain urinary plasminogen activator to the active two chain form.
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© 2001 The Pharmaceutical Society of Japan
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