Identification of an amino acid sequence in laminin mediating cell attachment, chemotaxis, and receptor binding.
We have probed for active sites in the B1 chain of laminin using synthetic peptides comprising certain regions of its amino acid sequence as deduced from cDNA clones. An antibody to a 19-mer from domain III inhibited attachment of HT-1080 and CHO cells to laminin, while the peptide itself was inactive. A nearby peptide (CDPGYIGSR) from domain III with homology to epidermal growth factor was synthesized and found to be one of the principle sites in laminin mediating cell attachment, migration, and receptor binding.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002448:Cell Adhesion; D002460:Cell Line; D002633:Chemotaxis; D005354:Fibrosarcoma; D005910:Glioma; D006801:Humans; D006822:Hybrid Cells / Q000166:cytology; D007797:Laminin / Q000378:metabolism / Q000502:physiology*; D009447:Neuroblastoma; D011971:Receptors, Immunologic / Q000378:metabolism*; D017474:Receptors, Laminin
D007797:Laminin; D011971:Receptors, Immunologic; D017474:Receptors, Laminin