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Tumor Biology |
3ß1 Integrin-mediated Adhesion and Neurite-like Outgrowth and Inhibits Proliferation of Small Cell Lung Carcinoma Cells
Laboratory of Pathology, National Cancer Institute, NIH, Bethesda, Maryland 20892 [N-h. G., H. A-B., J. C., J. M. S., H. C. K., D. D. R.], and Center for Cell and Gene Therapy, Baylor College of Medicine, Houston, Texas 77030 [N. S. T.]
Although human small cell lung carcinoma (SCLC) cell lines are typically
anchorage-independent and do not attach on most extracellular matrix
proteins, OH-1, and several other SCLC cell lines attached on
substrates coated with thrombospondin-1 (TSP1). SCLC cells grew
long-term as adherent cells on a TSP1-coated substrate. Adhesion of
SCLC cells on TSP1 was inhibited by heparin, function-blocking
antibodies recognizing 
3 or ß1 integrin subunits, and by soluble
3ß1 integrin ligands. SCLC cells extended neurite-like processes
on a TSP1 substrate, which was also mediated by 3ß1 integrin.
Process formation on a TSP1 substrate was specifically stimulated by
epidermal growth factor and somatostatin. Adhesion on TSP1 weakly
inhibited SCLC cell proliferation, but this inhibition was strongly
enhanced in the presence of epidermal growth factor. TSP1 and an
3ß1 integrin-binding peptide from TSP1 also inhibited
proliferation when added in solution. High-affinity binding of
125I-labeled TSP1 to OH-1 cells was heparin-dependent and
may be mediated by sulfated glycolipids, which are the major sulfated
glycoconjugates synthesized by these cells. Synthesis or secretion of
TSP1 by SCLC cells could not be detected. On the basis of these
results, the 3ß1 integrin and sulfated glycolipids cooperate to
mediate adhesion of SCLC cells on TSP1. Interaction with TSP1 through
this integrin inhibits growth and induces neurotypic differentiation,
which suggests that this response to TSP1 may be exploited to inhibit
the progression of SCLC.
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