Journal of Histochemistry and Cytochemistry, Vol. 50, 1625-1632, December 2002, Copyright © 2002, The Histochemical Society, Inc.
Distinct Distribution of Laminin and Its Integrin Receptors in the Pancreas
Fang-Xu Jianga,
Gaetano Nasellia, and
Leonard C. Harrisona
a Autoimmunity and Transplantation Division, the Walter and Eliza Hall Institute of Medical Research, The Royal Melbourne Hospital, Parkville, Australia
Correspondence to:
Leonard C. Harrison, Walter & Eliza Hall Inst. of Medical Research, Royal Melbourne Hospital, Parkville 3050, Victoria, Australia. E-mail: harrison@wehi.edu.au
Tissue function is regulated by the extracellular microenvironment including cell basement membranes, in which laminins are a major component. Previously, we found that laminin-1 promotes differentiation and survival of pancreatic islet cells. Here we characterize the expression pattern of laminins and their integrin receptors in adult pancreas. Although they are expressed in the basement membrane of acinar cells and duct epithelium, no laminin chains examined were detected extracellularly in the pancreatic islets. In contrast to laminin ß1- and 1-chains, the 1-chain, unique to laminin-1, was not detected. Laminin-10 ( 5ß1 1) was expressed in acinar tissue, whereas laminins-2 ( 2ß1 1) and -10 were expressed in the blood vessels. The laminin connector molecule, nidogen-1, had a distribution similar to that of laminin ß1 and 1, whereas fibulin-1 and -2, which compete with nidogen-1, were mostly confined to blood vessels. Integrin subunits 6 and 3 were detected in acinar cells and duct epithelial cells, but 6 was absent in islet cells. Integrin 6ß4 was detected only in duct cells, 6ß1 in both acinar and ductal cells, and 3ß1 in acinar, duct, and islet cells. These findings are a basis for further investigation of the role of extracellular matrix molecules and their receptors in pancreas function.
(J Histochem Cytochem 50:16251632, 2002)
Key Words:
laminin, nidogen, fibulin, integrin, pancreas

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