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J Biol Chem, Vol. 275, Issue 17, 12475-12480, April 28, 2000

Des-Arg10-kallidin Engagement of the B1 Receptor Stimulates Type I Collagen Synthesis via Stabilization of Connective Tissue Growth Factor mRNA*

Dennis A. RicuperoDagger §, Jose R. Romero||, David C. RishikofDagger **, and Ronald H. GoldsteinDagger

From the Dagger  Pulmonary Center, Departments of Medicine and Biochemistry, Boston University School of Medicine and the Boston Veterans Affairs Medical Center and the  Endocrine-Hypertension Division, Department of Medicine, Harvard Medical School, Boston, Massachusetts 02118-2394

Expression of the kinin B1 receptor is up-regulated in chronic inflammatory and fibrotic disorders; however, little is known about its role in fibrogenesis. We examined human embryonic lung fibroblasts that constitutively express the B1 receptor and report that engagement of the B1 receptor by des-Arg10-kallidin stabilized connective tissue growth factor (CTGF) mRNA, stimulated an increase in alpha 1(I) collagen mRNA, and stimulated type I collagen production. These events were not observed in B2 receptor-activated fibroblasts. In addition, B1 receptor activation by des-Arg10-kallidin induced a rise in cytosolic Ca2+ that is consistent with B1 receptor pharmacology. Our results show that the des-Arg10-kallidin-stimulated increase in alpha 1(I) collagen mRNA was time- and dose-dependent, with a peak response observed at 20 h with 100 nM des-Arg10-kallidin. The increase in CTGF mRNA was also time- and dose-dependent, with a peak response observed at 4 h with 100 nM des-Arg10-kallidin. The increase in CTGF mRNA was blocked by the B1 receptor antagonist des-Arg10,Leu9-kallidin. Inhibition of protein synthesis by cycloheximide did not block the des-Arg10-kallidin-induced increase in CTGF mRNA. These results suggest that engagement of the kinin B1 receptor contributes to fibrogenesis through increased expression of CTGF.

* This work was supported in part by NHLBI Grant P50HL56386 from the National Institutes of Health and by the Veterans Affairs Medical Center Merit Review Research Program.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.

|| Supported by NIDDK Grant R03DK53538 from the National Institutes of Health.

** Boston Veterans Affairs Medical Center Research Enhancement Awards Program Fellow.

§ To whom correspondence should be addressed: Pulmonary Center, Boston University School of Medicine, 715 Albany St., R3, Boston, MA 02118-2394. Tel.: 617-638-4860; Fax: 617-536-8093l; E-mail: ricupero@ bu.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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