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Expression and secretion of gro/MGSA by stimulated human endothelial cells.

1989; Springer Nature; Volume: 8; Issue: 6 Linguagem: Inglês

10.1002/j.1460-2075.1989.tb03569.x

1460-2075

D. Z. Wen, Aaron Rowland, Rik Derynck,

S100 Proteins and Annexins

Research Article1 June 1989free access Expression and secretion of gro/MGSA by stimulated human endothelial cells. D. Z. Wen D. Z. Wen Department of Developmental Biology, Genentech, Inc., South San Francisco, CA 94080. Search for more papers by this author A. Rowland A. Rowland Department of Developmental Biology, Genentech, Inc., South San Francisco, CA 94080. Search for more papers by this author R. Derynck R. Derynck Department of Developmental Biology, Genentech, Inc., South San Francisco, CA 94080. Search for more papers by this author D. Z. Wen D. Z. Wen Department of Developmental Biology, Genentech, Inc., South San Francisco, CA 94080. Search for more papers by this author A. Rowland A. Rowland Department of Developmental Biology, Genentech, Inc., South San Francisco, CA 94080. Search for more papers by this author R. Derynck R. Derynck Department of Developmental Biology, Genentech, Inc., South San Francisco, CA 94080. Search for more papers by this author Author Information D. Z. Wen1, A. Rowland1 and R. Derynck1 1Department of Developmental Biology, Genentech, Inc., South San Francisco, CA 94080. The EMBO Journal (1989)8:1761-1766https://doi.org/10.1002/j.1460-2075.1989.tb03569.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Melanoma growth stimulatory activity factor (MGSA) is a polypeptide which was initially isolated from Hs294 human melanoma cells. Its sequence is identical to the deduced amino acid sequence of the human gro cDNA, isolated from a human tumor cell line. MGSA stimulates the proliferation of malignant melanoma cells, but its function for normal cells has not been defined. Here we report that human umbilical vein endothelial cells are capable of synthesizing and secreting MGSA. The expression and secretion of MGSA are strongly induced by factors often involved in inflammation such as IL-1, TNF, LPS and thrombin. The induction of MGSA mRNA is dose and time dependent and is independent of new protein synthesis. This stimulation could be mimicked by TPA, suggesting that the action could be mediated through activation of protein kinase C. Furthermore, addition of MGSA to the endothelial cell cultures induces gro/MGSA gene expression, implying that an autocrine mechanism exists. Our data suggest that the protein encoded by gro/MGSA mRNA may play a role in inflammation and exert its effects on endothelial cells in an autocrine fashion. Previous ArticleNext Article Volume 8Issue 61 June 1989In this issue RelatedDetailsLoading ...