Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P62988 (Ubiquitin)
 4,326 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To elucidate the molecular basis of muscle atrophy, we have performed the serial analysis of gene expression (SAGE) method with control and immobilized muscles of 10 rats. The genes that expressed >0.5% in muscle are involved in the following three functions: 1) contraction (troponin I, C and T; myosin light chain 1-3; actin; tropomyosin; and parvalbumin), 2) energy metabolism (cytochrome c oxidase I and III, creatine kinase, glyceraldehyde-3-phosphate-dehydrogenase, phosphoglycerate mutase, ATPase 6, and aldolase A), and 3) housekeeping (lens epithelial protein). Muscle atrophy appears to be caused by changes in mRNA levels of specific regulators of proteolysis, protein synthesis, and contractile apparatus assembling, such as polyubiquitin, elongation factor 2, and nebulin. Immobilization has produced a decrease more than threefold in gene expression of enzymes involved in energy metabolism, especially ATPase, cytochrome c oxidase, NADH dehydrogenase, and protein phosphatase 1. Differential gene expressions of selenoprotein W and uroporphyrinogen decarboxylase, which can be involved in oxidative stress, were also observed. Other genes with various functions, such as cholesterol metabolism and growth factors, were also differentially expressed. Moreover, novel genes regulated by immobilization were discovered. Thus, the current study allows a better understanding of global muscle characteristics and the molecular mechanisms of sedentarity and sarcopenia.
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PMID:Characterization of control and immobilized skeletal muscle: an overview from genetic engineering. 1125 86

Incubation of rat brain mitochondria with ubiquitin and ATP followed by subsequent mitochondria sedimentation was accompanied by reduction of ubiquitin content in the supernatant. This decrease was more pronounced in the presence of ATP-regenerating system in the incubation medium (creatine phosphate/creatine phosphokinase). This ubiquitin incorporation into brain mitochondria observed only in the presence of ATP in the incubation medium increased sensitivity of monoamine oxidases (MAO) A and B to proteolytic inactivation by trypsin and papain, respectively. (Ubiquitin did not influence sensitivity of MAO B to trypsin and MAO A to papain). The data obtained suggest that ubiquitin incorporation into rat brain mitochondria increases susceptibility of MAOs to certain exogenous proteases, however, it remains unclear whether these changes stem from direct MAO-ubiquitin conjugation or reflect alterations in the membrane environment of these enzymes.
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PMID:[Ubiquitin causes selective increase in the sensitivity of rat brain mitochondrial monoamine oxidases to various proteases]. 1807 75