Identification of an amino acid sequence in laminin mediating cell attachment, chemotaxis, and receptor binding |
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| Authors: | J Graf Y Iwamoto M Sasaki G R Martin H K Kleinman F A Robey Y Yamada |
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| Affiliation: | 1. Laboratory of Developmental Biology and Anomalies National Institute of Dental Research National Institutes of Health Bethesda, Maryland 20892 USA;2. Center for Drugs and Biologics Food and Drug Administration Bethesda, Maryland 20892 USA;1. Division of Pediatric and Congenital Cardiothoracic Surgery, Arkansas Children’s Hospital, University of Arkansas for Medical Sciences, Little Rock, Arkansas;2. Biostatistics Program, Department of Pediatrics, Arkansas Children’s Hospital, University of Arkansas for Medical Sciences, Little Rock, Arkansas;3. Center for Integrative Nanotechnology Sciences, University of Arkansas at Little Rock, Little Rock, Arkansas;4. Children’s Medical Center, Department of Pediatric Cardiovascular Surgery, Kyoto Prefectural University of Medicine, Kyoto, Japan;1. Department of Thoracic and Vascular Surgery, Arnaud de Villeneuve Hospital, Montpellier, France;2. INSERM U 1046, Montpellier, France;1. Department of Anesthesiology, Wake Forest School of Medicine, Winston-Salem, North Carolina;2. Section of Molecular Medicine, Department of Internal Medicine, Wake Forest School of Medicine, Winston-Salem, North Carolina;3. Department of Surgery, Wake Forest School of Medicine, Winston-Salem, North Carolina;4. Hypertension and Vascular Research Center, Wake Forest School of Medicine, Winston-Salem, North Carolina;5. Department of Physiology & Pharmacology, Wake Forest School of Medicine, Winston-Salem, North Carolina;6. Department of Cardiothoracic Surgery, Wake Forest School of Medicine, Winston-Salem, North Carolina |
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| Abstract: | 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. |
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