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Identification of an amino acid sequence from the laminin A chain that stimulates metastasis and collagenase IV production.

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  • 1. Laboratory of Developmental Biology and Anomalies, National Institute of Dental Research, National Institutes of Health, Bethesda, MD 20892.
      Authors
    • Kanemoto T 1
    (1 author)

Proceedings of the National Academy of Sciences of the United States of America, 01 Mar 1990, 87(6):2279-2283
https://doi.org/10.1073/pnas.87.6.2279 PMID: 2156266 PMCID: PMC53670

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Abstract 

Tumor cells attach, degrade, and migrate through basement membranes as they metastasize. Laminin, a major glycoprotein of basement membranes, promotes the metastatic activity of tumor cells by stimulating the attachment and migration of the cells and their secretion of collagenase IV. We have identified a synthetic peptide of 19 amino acids (Cys-Ser-Arg-Ala-Arg-Lys-Gln-Ala-Ala-Ser-Ile-Lys-Val-Ala-Val-Ser-Ala-Asp -Arg) from the sequence of the A chain of laminin that increases experimental metastases of the lungs by murine melanoma cells. The peptide is active when injected either intravenously or intraperitoneally. The peptide increased collagenase IV activity, a key enzyme in the breakdown of basement membranes, to the same extent as laminin. This peptide represents an active site on laminin for promotion of the metastatic phenotype and generates a probe for studying the regulation of malignant activities.

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Proc Natl Acad Sci U S A. 1990 Mar; 87(6): 2279–2283.
PMCID: PMC53670
PMID: 2156266

Identification of an amino acid sequence from the laminin A chain that stimulates metastasis and collagenase IV production.

T Kanemoto, R Reich, L Royce, D Greatorex, S H Adler, N Shiraishi, G R Martin, Y Yamada, and H K Kleinman
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Abstract

Tumor cells attach, degrade, and migrate through basement membranes as they metastasize. Laminin, a major glycoprotein of basement membranes, promotes the metastatic activity of tumor cells by stimulating the attachment and migration of the cells and their secretion of collagenase IV. We have identified a synthetic peptide of 19 amino acids (Cys-Ser-Arg-Ala-Arg-Lys-Gln-Ala-Ala-Ser-Ile-Lys-Val-Ala-Val-Ser-Ala-Asp -Arg) from the sequence of the A chain of laminin that increases experimental metastases of the lungs by murine melanoma cells. The peptide is active when injected either intravenously or intraperitoneally. The peptide increased collagenase IV activity, a key enzyme in the breakdown of basement membranes, to the same extent as laminin. This peptide represents an active site on laminin for promotion of the metastatic phenotype and generates a probe for studying the regulation of malignant activities.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.
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