Identification of an Amino Acid Sequence from the Laminin A Chain That Stimulates Metastasis and Collagenase IV Production

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1990 Mar 1

PMID 2156266

Citations 27

Authors

T KANEMOTO

R Reich

L Royce

D Greatorex

S H Adler

N Shiraishi

G R Martin

Y Yamada

H K Kleinman

Affiliations

Soon will be listed here.

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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