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Connective Tissue Growth Factor (IGFBP-rP2) Expression and Regulation in Cultured Bovine Endothelial Cells¹

Department of Internal Medicine, Diabetes and Endocrinology Research Center, Veterans Administration Medical Center, The University of Iowa, Iowa City, Iowa 52246; and the Department of Pediatrics, Oregon Health Sciences University, Portland, Oregon 97201

Address all correspondence and requests for reprints to: Robert S. Bar, The University of Iowa, Department of Internal Medicine, ENDO-3E19 VA Medical Center, Iowa City, Iowa 52246. E-mail: rbar{at}icva.gov

Media from large vessel endothelial cells (pulmonary artery, aorta) contained intact connective tissue growth factor (CTGF) and a dominant 19-kDa band. N-terminal analysis of the 19-kDa band showed sequence corresponding to CTGF amino acid 181–190, suggesting that the 19-kDa band represented a proteolytic fragment of CTGF. Intact CTGF was increased by cAMP but not by transforming growth factor-ß (TGFß). CTGF messenger RNA (mRNA) was not changed by cAMP nor TGFß. In two microvessel endothelial cells, mRNA was found at low levels by PCR and Northern analysis, but no CTGF protein was seen on Western analysis. In the microvessel cells, TGFß increased and cAMP did not change CTGF mRNA levels, with neither TGFß nor cAMP increasing CTGF protein. The discordance between protein and mRNA levels in large vessel and microvessel endothelial cells was mostly explained by the effects of cAMP and TGFß on media proteolytic activity; in large vessel cells, cAMP inhibited degradation of CTGF, whereas in microvessel cells, TGFß and cAMP stimulated proteolytic activity against CTGF.

We conclude that in large vessel endothelial cells, cAMP increased intact CTGF protein by inhibiting degradation of CTGF, whereas TGFß stimulated neither CTGF mRNA nor protein; in microvessel cells, TGFß increased CTGF mRNA, while both TGFß and cAMP stimulated CTGF degradation.

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