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PMID: 8280080 Published · ppublish English Journal Article

Regulation of matrix metalloproteinase expression in human vein and microvascular endothelial cells. Effects of tumour necrosis factor alpha, interleukin 1 and phorbol ester.

The Biochemical journal ·Vol. 296 ( Pt 3) ·1993-12-15 ·Pages 803-9

Hanemaaijer R, Koolwijk P, le Clercq L, de Vree WJ, van Hinsbergh VW

Abstract

Matrix metalloproteinases (MMPs) play a role in tissue remodelling and angiogenesis. We have investigated the expression and regulation of MMP-1 (interstitial collagenase), MMP-2 (gelatinase A), MMP-3 (stromelysin 1), MMP-7 (matrilysin), MMP-9 (gelatinase B) and their inhibitors TIMP-1 and TIMP-2 in human umbilical vein, femoral vein and microvascular endothelial cells, and compared these data with those obtained with human synovial fibroblasts. Non-stimulated vein endothelial cells expressed the mRNAs for MMP-1, MMP-2, TIMP-1 and TIMP-2. MMP-3 mRNA and protein were undetectable or only weakly expressed, but could be stimulated by the inflammatory mediator tumour necrosis factor alpha (TNF alpha). The expression of MMP-3 and MMP-1 was further enhanced by phorbol 12-myristate 13-acetate (PMA). Phorbol ester also induced TIMP-1 and MMP-9, the expression of the latter being further enhanced by TNF alpha or interleukin 1 alpha (IL-1 alpha). Similar stimulatory effects were observed in microvascular endothelial cells. Hence the inflammatory mediator TNF alpha induces/enhances the production of several matrix metalloproteinases in human endothelial cells. On the other hand, MMP-2 and TIMP-2 were not affected or were affected in a variable way by TNF alpha and/or phorbol ester, suggesting a dissimilar regulation of these proteins. The cyclic AMP-enhancing agent forskolin affected the production of MMPs in a cell-type-specific way. In human vein endothelial cells it enhanced the PMA-mediated induction of MMP-9, whereas it suppressed this induction in human microvascular endothelial cells and in synovial fibroblasts. On the other hand, forskolin suppressed the PMA-mediated induction of MMP-1 and MMP-3 in synovial fibroblasts, while it enhanced or did not affect this induction in various types of human endothelial cells. These observations may have implications for future pharmacological intervention in angiogenesis.

Related Genes
MMP TIMP-1 TIMP-2
MeSH Terms
Capillaries/enzymology Cells, Cultured Colforsin/pharmacology Endothelium, Vascular/enzymology Enzyme Induction Extracellular Matrix/enzymology Fibroblasts/enzymology Humans Interleukin-1/pharmacology Metalloendopeptidases/biosynthesis,genetics RNA, Messenger/metabolism Synovial Membrane/cytology,enzymology Tetradecanoylphorbol Acetate/pharmacology Tumor Necrosis Factor-alpha/pharmacology Veins/enzymology
Chemicals
Interleukin-1 RNA, Messenger Tumor Necrosis Factor-alpha Colforsin Metalloendopeptidases Tetradecanoylphorbol Acetate
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Hanemaaijer R
Gaubius Laboratory IVVO-TNO, Leiden, The Netherlands.
Koolwijk P
le Clercq L
de Vree W J
van Hinsbergh V W
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2960803
Published
1993-12-15
Pages
803-9
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1137766
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2960803 PMC Full Text View journal details
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