First Author | Riopel MM | Year | 2013 |
Journal | Lab Invest | Volume | 93 |
Issue | 1 | Pages | 31-40 |
PubMed ID | 23069938 | Mgi Jnum | J:190701 |
Mgi Id | MGI:5449485 | Doi | 10.1038/labinvest.2012.147 |
Citation | Riopel MM, et al. (2013) beta1 integrin-extracellular matrix interactions are essential for maintaining exocrine pancreas architecture and function. Lab Invest 93(1):31-40 |
abstractText | Integrin receptors are responsible for integrating extracellular matrix signals inside the cell. The most prominent integrin receptor, beta1 integrin, has a role in cell function, survival and differentiation. Recently, we demonstrated a profound in vivo role of beta1 integrin expression in the pancreas on glucose homeostasis and islet function. Here, we extend these results by examining the role of beta1 integrin in exocrine pancreatic structure and function. Adult C57Bl/6 mice hemizygous for a collagen type Ialpha2 (Col1a2) promoter-controlled tamoxifen-inducible Cre recombinase gene and homozygous for loxP-beta1 integrin were injected with tamoxifen or corn oil to generate mice deleted or not for beta1 integrin. Pancreata derived from these male mice were analyzed by quantitative reverse transcriptase-polymerase chain reaction, western blot and immunofluorescence. Our results showed that beta1 integrin-deficient mice displayed a significant decrease in pancreas weight with a significant reduction of amylase, regenerating islet-derived protein II and carboxypeptidase-A expression (P<0.05-0.01). Compared with control pancreata, beta1 integrin-deficient pancreata showed reduced mRNA expression of extracellular matrix (collagen type Ialpha2, fibronectin and laminin) genes (P<0.05), detached acini clusters and lost focal adhesion structure. Moreover, beta1 integrin-deficient pancreatic acinar cells displayed decreased proliferation (P<0.05) and increased apoptosis (P<0.001). Apoptosis was reduced to that of controls when isolated exocrine clusters were cultured in media supplemented with extracellular matrix proteins. Taken together, these results implicate beta1 integrin as an essential component for maintaining exocrine pancreatic structure and function. |