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vß3 and 5ß1 integrins
Craniofacial Developmental Biology and Regeneration Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, Maryland 20892, USA; and
* Graduate School of Environmental Earth Science, Hokkaido University, Sapporo, Japan
1Correspondence: CDBRB, NIDCR, NIH, Bldg. 30, Room 433, 30 Convent Dr., Bethesda, MD 20892, USA. E-mail address: hkleinman{at}dir.nidcr.nih.gov
Angiogenesis is important for wound healing, tumor growth, and
metastasis. Endothelial cells differentiate into capillary-like
structures on a laminin-1-rich matrix (Matrigel). We previously
identified 20 angiogenic sites on laminin-1 (
1ß1
1) by screening
559 overlapping synthetic peptides. C16, the most potent 1 chain
peptide, blocked laminin-1-mediated adhesion and was the only 1
chain peptide to block attachment to both collagen I and fibronectin.
This suggested that C16 was acting via a receptor common to these
substrates. We demonstrated that C16 is angiogenic in vivo. Affinity
chromatography identified the integrins 5ß1 and vß3 as
surface receptors. Blocking antibodies confirmed the role of these
receptors in C16 adhesion. C16 does not contain an RGD sequence and, as
expected, an RGD-containing peptide did not block C16 adhesion nor did
C16 act via MAP kinase phosphorylation. Furthermore, we identified a
C16 scrambled sequence, C16S, which antagonizes the angiogenic activity
of bFGF and of C16 by binding to the same receptors. Because the
laminin 1 chain is ubiquitous in most tissues, C16 is likely an
important functional site. Since the biological activity of C16 is
blocked by a scrambled peptide, C16S may serve as an anti-angiogenic
therapeutic agent.—Ponce, M. L., Nomizu, M., Kleinman, H. K.
An angiogenic laminin site and its antagonist bind through the vß3
and 5ß1 integrins.
Key Words: angiogenesis • laminin-1 • bFGF • endothelium • peptides
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