Matrix metalloproteinase-2, caveolins, focal adhesion kinase and c-Kit in cells of the mouse myocardium.
Matrix metalloproteinase-2 (MMP-2) may play roles at intracellular and extracellular sites of the heart in ischaemia/reperfusion injury. Caveolins (Cav-1, -2 and -3) are lipid raft proteins which play roles in cell sig-nalling. This study examined, using immunohistochemistry and two photon confocal microscopy, if MMP-2 and caveolins co-localize at the plasma membrane of cardiac cells: cardiomyocytes (CM), fibroblasts (FB) and capillary endothelial cells (CEC) in the left ventricle (LV) of the Cav-1(+/+) and Cav-1(-/-) mouse heart. In Cav-1(+/+) mouse LV MMP-2 and Cav-1 co-localized at CM plasma membranes, and at multiple locations in FB and CEC. MMP-2 co-localized with Cav-2 only at CEC. MMP-2 co-localized with Cav-3 at CM plasma membranes and Z-lines, and partially at FB and CEC. In Cav-1(-/-) LV Cav-1 and MMP-2 were absent or reduced everywhere. Cav-2 appeared at CEC despite the absence of Cav-1. Cav-3 appeared at CM plasma membranes and Z-lines, FB and CEC. Also, FAK in FB and c-Kit in interstitial Cajal-like cells (ICLC) were completely absent. By transmission electron microscopy in Cav-1(+/+), regular size caveolae (Cav) were at CEC, irregular size Cav were at CM and a few were at FB. In Cav-1(-/-) there were few Cav at CM and FB and some at CEC. To conclude, MMP-2 is closely associated with caveolins at FB and CEC as well as at CM. Also, MMP-2 is closely associated with FAK at FB and c-Kit at ICLC. Thus, Cav-1 expression is not necessary for Cav-2 expression. Cav-3 or Cav-3 with Cav-2 has the capability to make Cav.
Cho
Woo Jung
WJ
Department of Pharmacology, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Alberta, Canada.
Chow
Ava K
AK
Schulz
Richard
R
Daniel
Edwin E
EE
D000818:Animals; D051242:Caveolin 1 / Q000378:metabolism; D051243:Caveolin 2 / Q000378:metabolism; D051244:Caveolin 3 / Q000378:metabolism; D022461:Caveolins / Q000378:metabolism*; D000070818:Discoidin Domain Receptors; D004730:Endothelium, Vascular / Q000166:cytology / Q000201:enzymology / Q000648:ultrastructure; D005347:Fibroblasts / Q000166:cytology / Q000201:enzymology / Q000648:ultrastructure; D051416:Focal Adhesion Protein-Tyrosine Kinases / Q000378:metabolism*; D008297:Male; D020778:Matrix Metalloproteinase 2 / Q000378:metabolism*; D051379:Mice; D009206:Myocardium / Q000166:cytology* / Q000201:enzymology* / Q000648:ultrastructure; D032383:Myocytes, Cardiac / Q000166:cytology / Q000201:enzymology / Q000648:ultrastructure; D020033:Protein Isoforms / Q000378:metabolism; D021381:Protein Transport; D019009:Proto-Oncogene Proteins c-kit / Q000378:metabolism*; D020794:Receptor Protein-Tyrosine Kinases / Q000378:metabolism; D011975:Receptors, Mitogen / Q000378:metabolism; D014841:von Willebrand Factor / Q000378:metabolism
D051242:Caveolin 1; D051243:Caveolin 2; D051244:Caveolin 3; D022461:Caveolins; D020033:Protein Isoforms; D011975:Receptors, Mitogen; D014841:von Willebrand Factor; D000070818:Discoidin Domain Receptors; D019009:Proto-Oncogene Proteins c-kit; D020794:Receptor Protein-Tyrosine Kinases; D051416:Focal Adhesion Protein-Tyrosine Kinases; D020778:Matrix Metalloproteinase 2