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Am J Physiol Heart Circ Physiol (March 20, 2003). doi:10.1152/ajpheart.00946.2002
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Submitted on November 4, 2002
Accepted on March 13, 2003

Caveolae-associated Proteins in cardiomyocytes: Caveolin-2 expression and interactions with Caveolin-3

Vitalyi O Rybin1, Peter W Grabham1, Hasnae Elouardighi1, and Susan F Steinberg2*

1 Department of Pharmacology, College of Physicians and Surgeons, Columbia University, New York, NY, USA
2 Department of Pharmacology, College of Physicians and Surgeons, Columbia University, New York, NY, USA; Department of Medicine, College of Physicians and Surgeons, Columbia University, New York, NY, USA

* To whom correspondence should be addressed. E-mail: sfs1{at}columbia.edu.

Caveolin-3, the muscle-specific caveolin isoform, acts like the more ubiquitously expressed caveolin-1 to sculpt caveolae, specialized membrane microdomains that serve as platforms to organize signal transduction pathways. Caveolin-2 is a structurally related isoform that alone does not drive caveolae biogenesis; rather, caveolin-2 cooperates with caveolin-1 to form caveolae in non-muscle cells. While caveolin-2 might be expected to interact in an analogous fashion with caveolin-3, it generally has not been detected in cardiomyocytes. This study shows that caveolin-2 and caveolin-3 are detected at low levels in ventricular myocardium, and increase dramatic with age or when neonatal cardiomyocytes are placed in culture. In contrast, flotillins (caveolin functional homologs) are expressed at relatively constant levels in these preparations. In neonatal cardiac cultures, caveolin-2 and -3 expression is not influenced by thyroid hormone (a post-natal regulator of other cardiac gene products). The further evidence that caveolin-2 co-immunoprecipitates with caveolin-3 and floats with caveolin-3 by isopycnic centrifugation in cardiomyocyte cultures suggests that caveolin-2 may contribute to caveolae biogenesis and influence cardiac muscle physiology.




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