TY - JOUR
T1 - Definition of a Sequence, RYWLPR, within Laminin Peptide F-9 that Mediates Metastatic Fibrosarcoma Cell Adhesion and Spreading
AU - Skubitz, Amy P.N.
AU - McCarthy, James B.
AU - Zhao, Qi
AU - Yi, Xiang Yan
AU - Furcht, Leo T.
PY - 1990/12/1
Y1 - 1990/12/1
N2 - A synthetic peptide from the inner globule of the Bl chain of laminin, termed peptide F-9 (RYWLPRPVCFEKGMNYTVR; 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 Bl 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.
AB - A synthetic peptide from the inner globule of the Bl chain of laminin, termed peptide F-9 (RYWLPRPVCFEKGMNYTVR; 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 Bl 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.
UR - http://www.scopus.com/inward/record.url?scp=0025609382&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025609382&partnerID=8YFLogxK
M3 - Article
C2 - 2253210
AN - SCOPUS:0025609382
SN - 0008-5472
VL - 50
SP - 7612
EP - 7622
JO - Cancer Research
JF - Cancer Research
IS - 23
ER -