Home LiteratureArticle Details
PMID: 12114504 Published · ppublish English Journal Article

Matrix metalloproteinases cleave connective tissue growth factor and reactivate angiogenic activity of vascular endothelial growth factor 165.

The Journal of biological chemistry ·Vol. 277 ·No. 39 ·2002-09-27 ·Pages 36288-95

Hashimoto G, Inoki I, Fujii Y, Aoki T, Ikeda E, Okada Y

Abstract

Vascular endothelial growth factor (VEGF), a potent angiogenic mitogen, plays a crucial role in angiogenesis under various pathophysiological conditions. We have recently demonstrated that VEGF(165), one of the VEGF isoforms, binds connective tissue growth factor (CTGF) and that its angiogenic activity is inhibited in the VEGF(165).CTGF complex form (Inoki, I., Shiomi, T., Hashimoto, G., Enomoto, H., Nakamura, H., Makino, K., Ikeda, E., Takata, S., Kobayashi, K. and Okada, Y. (2002) FASEB J. 16, 219-221). In the present study, we further examined the susceptibility of the VEGF(165).CTGF complex to matrix metalloproteinases (MMP-1, -2, -3, -7, -9, and -13), ADAMTS4 (aggrecanase-1), and serine proteinases, and evaluated the recovery of the angiogenic activity of VEGF(165) after the treatment. Among the MMPs, MMP-1, -3, -7, and -13 processed CTGF of the complex into the major NH(2)- and COOH-terminal fragments, whereas VEGF(165) was completely resistant to the MMPs. On the other hand, elastase and plasmin cleaved both CTGF and VEGF(165) of the complex, but they were completely resistant to ADAMTS4. By digestion of the immobilized VEGF(165).CTGF complex with MMP-3 or MMP-7, both NH(2)- and COOH-terminal fragments of CTGF were dissociated and released from the complex into the liquid phase. The in vitro angiogenic activity of VEGF(165) blocked in the VEGF(165).CTGF complex was reactivated to original levels after CTGF digestion of the complex with MMP-1, -3, and -13. Recovery of angiogenic activity was further confirmed by in vivo angiogenesis assay using a Matrigel injection model in mice. These results demonstrate for the first time that CTGF is a substrate of MMPs and that the angiogenic activity of VEGF(165) suppressed by the complex formation with CTGF is recovered through the selective degradation of CTGF by MMPs. MMPs may play a novel role through CTGF degradation in VEGF-induced angiogenesis during embryonic development, tissue maintenance, and/or pathological processes of various diseases.

MeSH Terms
Animals Aorta/cytology Binding Sites Cattle Collagenases/metabolism Connective Tissue Growth Factor DNA, Complementary/metabolism Endothelial Growth Factors/metabolism Endothelium, Vascular/cytology Fibrinolysin/metabolism Humans Immediate-Early Proteins/metabolism Immunoblotting Intercellular Signaling Peptides and Proteins/metabolism Lymphokines/metabolism Matrix Metalloproteinase 1/metabolism Matrix Metalloproteinase 13 Matrix Metalloproteinase 3/metabolism Matrix Metalloproteinase 7/metabolism Matrix Metalloproteinases/metabolism Neovascularization, Pathologic Neovascularization, Physiologic Pancreatic Elastase/metabolism Protein Binding Recombinant Proteins/metabolism Serine Endopeptidases/metabolism Time Factors Vascular Endothelial Growth Factor A Vascular Endothelial Growth Factors
Chemicals
CCN2 protein, human CCN2 protein, mouse DNA, Complementary Endothelial Growth Factors Immediate-Early Proteins Intercellular Signaling Peptides and Proteins Lymphokines Recombinant Proteins VEGFA protein, human Vascular Endothelial Growth Factor A Vascular Endothelial Growth Factors Connective Tissue Growth Factor Serine Endopeptidases Pancreatic Elastase Fibrinolysin Collagenases MMP13 protein, human Matrix Metalloproteinase 13 Matrix Metalloproteinases Matrix Metalloproteinase 3 Matrix Metalloproteinase 7 Matrix Metalloproteinase 1
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Hashimoto Gakuji
Department of Pathology, School of Medicine, Keio University, 35 Shinanomachi, Shinjuku-ku, Tokyo, Japan.
Inoki Isao
Fujii Yutaka
Aoki Takanori
Ikeda Eiji
Okada Yasunori
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
2002-09-27
Epub
2002-00-11
Pages
36288-95
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com