Identification of the substrates for plasma hyaluronan binding protein.

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Choi-Miura NH, Yoda M, Saito K, Takahashi K, Tomita M

Identification of the substrates for plasma hyaluronan binding protein.

Biol Pharm Bull. 2001 Feb;24(2):140-3.

PubMed ID

11217080 [ View in PubMed

]

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 alpha-chain at multiple sites and the beta-chain between lysine53 and lysine54 but not the gamma-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.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Hyaluronic acid	Hyaluronan-binding protein 2	Protein	Humans	Unknown	Binder	Details

Polypeptides

Name	UniProt ID
Hyaluronan-binding protein 2	Q14520	Details