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Originally published In Press as doi:10.1074/jbc.M102630200 on April 24, 2001

J. Biol. Chem., Vol. 276, Issue 27, 25318-25323, July 6, 2001
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Characterization of a Stellate Cell Activation-associated Protein (STAP) with Peroxidase Activity Found in Rat Hepatic Stellate Cells*

Norifumi KawadaDagger , Dan Bach Kristensen§, Kinji Asahina, Kazuki NakataniDagger , Yukiko MinamiyamaDagger , Shuichi SekiDagger , and Katsutoshi Yoshizato§||**

From the Dagger  Department of Hepatology, Graduate School of Medicine, Osaka City University Medical School, Osaka, 545-8585, § Hiroshima Proteome Laboratory, Regional Science Program of Hiroshima Industrial Technology Organization and Japan Science and Technology Corporation, Higashihiroshima, Hiroshima, 739-0046,  Hiroshima Tissue Regeneration Project, Hiroshima Prefecture Collaboration of Regional Entities for the Advancement of Technological Excellence, Japan Science and Technology Corporation, Higashihiroshima, Hiroshima, 739-0046, and the || Developmental Biology Laboratory, Department of Biological Science, Graduate School of Science, Hiroshima University, Hiroshima, 739-8526, Japan

A proteome approach for the molecular analysis of the activation of rat stellate cell, a liver-specific pericyte, led to the discovery of a novel protein named STAP (stellate cell activation-associated protein). We cloned STAP cDNA. STAP is a cytoplasmic protein with molecular weight of 21,496 and shows about 40% amino acid sequence homology with myoglobin. STAP was dramatically induced in in vivo activated stellate cells isolated from fibrotic liver and in stellate cells undergoing in vitro activation during primary culture. This induction was seen together with that of other activation-associated molecules, such as smooth muscle alpha -actin, PDGF receptor-beta , and neural cell adhesion molecule. The expression of STAP protein and mRNA was augmented time dependently in thioacetamide-induced fibrotic liver. Immunoelectron microscopy and proteome analysis detected STAP in stellate cells but not in other hepatic constituent cells. Biochemical characterization of recombinant rat STAP revealed that STAP is a heme protein exhibiting peroxidase activity toward hydrogen peroxide and linoleic acid hydroperoxide. These results indicate that STAP is a novel endogenous peroxidase catabolizing hydrogen peroxide and lipid hydroperoxides, both of which have been reported to trigger stellate cell activation and consequently promote progression of liver fibrosis. STAP could thus play a role as an antifibrotic scavenger of peroxides in the liver.

* This work was supported in part by Grant-in-aid from the Ministry of Education, Science and Culture of Japan 11670525.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AJ245663.

** To whom correspondence should be addressed: Developmental Biology Lab., Dept. of Biological Science, Graduate School of Science, Hiroshima University, 1-3-1, Kagamiyama, Higashihiroshima,  Hiroshima, 739-8526, Japan. Tel.: 81-824-24-7440; Fax: 81-824-24-1492; E-mail: kyoshiz@hiroshima-u.ac.jp.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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