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Blockade of ß1 Integrin–Laminin-5 Interaction Affects Spreading and Insulin Secretion of Rat ß-Cells Attached on Extracellular Matrix

¹ Department of Genetic Medicine and Development, University Medical Center, Geneva, Switzerland
² Cell Isolation and Transplantation Center, Division of Surgical Research, Department of Surgery, University Hospital, Geneva, Switzerland

Address correspondence and reprint requests to Geraldine Parnaud, Department of Genetic Medicine and Development, University Medical Center, 1 rue Michel-Servet, 1211 Geneva-4, Switzerland. E-mail: geraldine.parnaud{at}medecine.unige.ch

Abbreviations: DMEM, Dulbecco’s modified Eagle’s medium; FAK, focal adhesion kinase; HRP, horseradish peroxidase; KRBH, Krebs-Ringer bicarbonate HEPES buffer

When attached on a matrix produced by a rat bladder carcinoma cell line (804G matrix), rat pancreatic ß-cells spread in response to glucose and secrete more insulin compared with cells attached on poly-L-lysine. The aim of this study was to determine whether laminin-5 and its corresponding cell receptor ß1 integrin are implicated in these phenomena. By using specific blocking antibodies, we demonstrated that laminin-5 is the component present in 804G matrix responsible for the effect of 804G matrix on ß-cell function and spreading. When expression of two well-known laminin-5 ligands, ß1 and ß4 integrin, was assessed by Western blot and RT-PCR, only the ß1 integrin was detected in ß-cells. Anti–ß1 integrin antibody reduced the spreading of ß-cells on 804G matrix. Blockade of the interaction between ß1 integrins and laminin-5 resulted in a reduction in glucose-stimulated insulin secretion. Blocking anti–ß1 integrin antibody also inhibited focal adhesion kinase phosphorylation induced by 804G matrix. In conclusion, anti–ß1 integrin and –laminin-5 antibodies interfere with spreading of ß-cells, resulting in decreased insulin secretion in response to glucose. Our findings indicate that outside-in signaling via engagement of ß1 integrins by laminin-5 is an important component of normal ß-cell function.

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