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In cardiac myocytes, Ca(2+) concentrations alternate between high levels during contraction and low levels during relaxation. The increase in Ca(2+) concentration during contraction is primarily due to release of Ca(2+) from intracellular stores. However, some Ca(2+) also enters the cell through the sarcolemma(plasma membrane). During relaxation, Ca(2+) is sequestered within the intracellular stores. To prevent overloading of intracellular stores, the Ca(2+) that entered across the sarcolemma

This gene encodes ubiquitin, one of the most conserved proteins known. Ubiquitin has a major role in targeting cellular proteins for degradation by the 26S proteosome. It is also involved in the maintenance of chromatin structure, the regulation of gene expression, and the stress response. Ubiquitin is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin moiety fused to an unrelated protein. This gene consists of three direct repeats of the ubiquit

This gene encodes ubiquitin, one of the most conserved proteins known. Ubiquitin has a major role in targeting cellular proteins for degradation by the 26S proteosome. It is also involved in the maintenance of chromatin structure, the regulation of gene expression, and the stress response. Ubiquitin is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin moiety fused to an unrelated protein. This gene consists of three direct repeats of the ubiquit

PAI1 (plasminogen activator inhibitor 1) is originally cloned from human endothelial cell (Pannekoek 1986, Ginsburg 1986) and rat hepatoma cell 3 cDNA libraries. As a member of the serpin family of serine protease inhibitors, PAI1 inhibits both tissue type plasminogen activator (tPA) and urokinase type plasminogen activator (uPA). High PAI1 levels are associated with an increased risk of thromboembolic disease while PAI1 deficiency may represent an inherited autosomal recessive bleeding disor

PAI1 (plasminogen activator inhibitor 1) is originally cloned from human endothelial cell (Pannekoek 1986, Ginsburg 1986) and rat hepatoma cell 3 cDNA libraries. As a member of the serpin family of serine protease inhibitors, PAI1 inhibits both tissue type plasminogen activator (tPA) and urokinase type plasminogen activator (uPA). High PAI1 levels are associated with an increased risk of thromboembolic disease while PAI1 deficiency may represent an inherited autosomal recessive bleeding disor

PAI1 (plasminogen activator inhibitor 1) is originally cloned from human endothelial cell (Pannekoek 1986, Ginsburg 1986) and rat hepatoma cell 3 cDNA libraries. As a member of the serpin family of serine protease inhibitors, PAI1 inhibits both tissue type plasminogen activator (tPA) and urokinase type plasminogen activator (uPA). High PAI1 levels are associated with an increased risk of thromboembolic disease while PAI1 deficiency may represent an inherited autosomal recessive bleeding disor