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1 Department of Developmental Biology and Anatomy, University of South Carolina, Columbia, SC, USA
2 Department of Chemistry, University of South Carolina Aiken, Aiken, SC, USA
3 Department of Molecular Cardiovascular Biology, Children's Hospital and Research Foundation, Cincinnati, OH, USA
4 Department of Cardiovascular Division, Harvard University, Boston, MA, USA
5 Department of Biological Sciences, University of Auckland, Auckland, New Zealand
* To whom correspondence should be addressed. E-mail: JackG{at}Aiken.sc.edu.
Integrin-mediated cell-extracellular matrix interactions are essential for multiple cellular processes; however, little is known regarding integrin turnover during these events. Recent studies have demonstrated shedding of cell surface molecules and suggested this as a potential mechanism for integrin turnover. Confocal microscopy of mouse hearts under different physiological conditions demonstrated the presence of 
1 integrin immunoreactive material in the interstitium. Culture media from neonatal rat cardiac myocytes and fibroblasts contained a 55 kDa fragment of 1 integrin. Attachment to ECM components, response to PMA stimulation, and MMP inhibition assays demonstrated that fibroblasts responded differently to the fragment compared to myocytes. The 1 integrin fragment stimulated myocyte attachment to collagen and the fragment itself bound a variety of ECM proteins. These studies indicate that as myocytes and fibroblasts change size and shape, cellular contacts with the ECM are altered resulting in the liberation of a 1 integrin fragment from the cell surface. Integrin shedding may represent a novel mechanism of rapidly modifying cell-ECM contacts during various cellular processes.
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