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Identification of a second active site in laminin for promotion of cell adhesion and migration and inhibition of in vivo melanoma lung colonization.
Kleinman, H K; Graf, J; Iwamoto, Y; Sasaki, M; Schasteen, C S; Yamada, Y; Martin, G R; Robey, F A.
Affiliation
  • Kleinman HK; Laboratory of Developmental Biology and Anomalies, National Institutes of Health, Bethesda, Maryland 20892.
Arch Biochem Biophys ; 272(1): 39-45, 1989 Jul.
Article in En | MEDLINE | ID: mdl-2735766
Previously we reported that a pentapeptide (Tyr-Ile-Gly-Ser-Arg or YIGSR) from domain III of the B1 chain of laminin is a cell attachment site with the ability to stimulate cell adhesion and migration and to block experimental metastases. Here we report studies on the activities of synthetic peptides that cover domain III and report a second biologically active peptide PDSGR from this domain with activities similar to YIGSR. We also show that cyclic YIGSR is more potent in these assays than the linear peptide as expected since this sequence on laminin is bracketed by cysteines. Due to their proximity and similar spectrum of activities, it is possible that these sequences act in concert in the native laminin molecule.
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Collection: 01-internacional Database: MEDLINE Main subject: Oligopeptides / Melanoma, Experimental / Laminin Type of study: Diagnostic_studies Limits: Animals / Female / Humans Language: En Journal: Arch Biochem Biophys Year: 1989 Document type: Article Country of publication: United States
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Collection: 01-internacional Database: MEDLINE Main subject: Oligopeptides / Melanoma, Experimental / Laminin Type of study: Diagnostic_studies Limits: Animals / Female / Humans Language: En Journal: Arch Biochem Biophys Year: 1989 Document type: Article Country of publication: United States