Definition of a sequence, RYVVLPR, within laminin peptide F-9 that mediates metastatic fibrosarcoma cell adhesion and spreading.

Abstract

A synthetic peptide from the inner globule of the B1 chain of laminin, termed peptide F-9 (RYVVLPRPVCFEKGMNYTVR; residues 641-660), has been shown to have heparin-binding and cell adhesion-promoting activities for diverse cell types (Charonis et al., J. Cell. Biol., 107: 1253-1260, 1988). In this study, the metastatic murine fibrosarcoma cell line, UV-2237-MM, adhered and spread on surfaces coated with laminin and peptide F-9 in a concentration- and time-dependent fashion. Cells migrated toward laminin in Boyden microchemotaxis chambers but not toward peptide F-9. However, exogenous soluble peptide F-9 inhibited both the adhesion and migration of cells toward laminin. Polyclonal antibodies raised against peptide F-9 were capable of inhibiting laminin-mediated cell adhesion and migration. Peptide F-9 is located 265 residues from CDPGYIGSR, another sequence on the B1 chain of laminin which has been reported by others to promote cell adhesion (Graft et al., Cell, 48: 989-996, 1987). In contrast to peptide F-9, various control peptides including CDPGYIGSR did not promote the adhesion, spreading, or migration of the UV-2237-MM fibrosarcoma cells. In addition, neither exogenous peptide CDPGYIGSR nor antibodies raised against peptide CDPGYIGSR were capable of inhibiting laminin-mediated cell adhesion or migration. These results indicate that peptide F-9, but not peptide CDPGYIGSR, represents a major fibrosarcoma cell adhesion-promoting domain on intact laminin. A series of overlapping peptides were synthesized which contained various portions of the parent peptide F-9. The use of these peptides in cell adhesion assays demonstrated that the sequence RYVVLPR from the amino terminus of peptide F-9 was essential for cell adhesion-promoting activity.

• Authors: A P Skubitz, J B McCarthy, Q Zhao, X Y Yi, L T Furcht
• Journal: Cancer research (Cancer Res) Vol. 50 Issue 23 Pg. 7612-22 (Dec 01 1990) ISSN: 0008-5472 [Print] United States
• PMID: 2253210 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Laminin
• Peptide Fragments
• laminin F9

Topics

• Amino Acid Sequence
• Animals
• Cell Adhesion (drug effects)
• Cell Movement (drug effects)
• Dose-Response Relationship, Drug
• Fibrosarcoma (physiopathology)
• Humans
• In Vitro Techniques
• Kidney Neoplasms (physiopathology)
• Laminin (chemistry, pharmacology)
• Mice
• Molecular Sequence Data
• Neoplasm Metastasis
• Peptide Fragments (chemistry, pharmacology)
• Time Factors