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Determination of P2X 1 α‐sarcoglycan (adhalin) expression levels in failing human dilated cardiomyopathic left ventricles
Author(s) -
Berry Desiree A.,
Balcar Vladimir J.,
Barden Julian A.,
Keogh Anne,
dos Remedios Cristobal G.
Publication year - 2000
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/1522-2683(200011)21:17<3857::aid-elps3857>3.0.co;2-r
Subject(s) - dilated cardiomyopathy , dystrophin , sarcolemma , ventricle , medicine , cardiomyopathy , receptor , downregulation and upregulation , endocrinology , biology , left ventricles , myocyte , duchenne muscular dystrophy , cardiology , heart failure , biochemistry , gene
This study is concerned with the molecular basis of human idiopathic dilated cardiomyopathy (DCM). This disorder affects the entire heart including both atria and ventricles. It is characterized by a progressive dilatation of the ventricles and loss of contractile power that results in an impaired cardiac output. Changes in cellular levels of dystrophin have been reported in patients with muscular dystrophies (Beckers and Duchenne) which manifest as DCM. However, previous studies using Western blots dos Remedios et al. , Electrophoresis 1996, 17 , 235—238) of samples of left ventricles from DCM patients showed no abnormalities in dystrophin content. P2X receptors are ATP‐gated cation channels located in the sarcolemma. They are upregulated by a factor of about two in the atria of DCM patients compared with nondiseased control samples. A dystrophin‐associated protein, α‐sarcoglycan, has recently been shown to be an ecto‐ATPase (an extracellular ATPase) capable of regulating ATP concentrations in the space between the cardiomyocytes. In this report we examine the relationship between changes in P2X 1 receptors in left ventricle samples from DCM patients and the concentration of α‐sarcoglycan. We found no evidence for upregulation of P2X 1 receptors nor was the expression of α‐sarcoglycan significantly altered.