Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.4.1.2 (glutamate dehydrogenase)
 4,380 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In cultured hepatocytes the turnover of several mitochondrial matrix proteins (e.g. acetyl-CoA acetyltransferase) appears to be initiated by CoA-mediated, sequential transformation into CoA-modified forms. This modification favours the notion that intramitochondrial degradation by a matrix-resident ATP-dependent protease may be preceded by a specific modification by CoA. In a mitochondrial matrix fraction the MgATP-dependent decrease in anti-CoA immunoreactivity coincided with both a decrease in the anti-protein immunoreactivity of acetyl-CoA acetyltransferase and/or of 3-ketoacyl-CoA thiolase, and with the appearance of proteolytic fragments. A closer analysis of the degradation pattern revealed, however, a breakdown of the unmodified acetyl-CoA acetyltransferase and of its CoA-modified form, A1, whereas the form that is more highly modified by CoA, A2, proved to be inaccessible towards an ATP-dependent protease. In mammalian mitochondrial matrix, proteins can be degraded selectively by a matrix-resident ATP-dependent protease. The process of CoA modification results finally in the protection of matrix proteins from degradation. In cultured hepatocytes, leupeptin, an inhibitor of lysosomal proteases, did not affect the steady-state level of the mitochondrial matrix protein acetyl-CoA acetyltransferase. However, leupeptin mediated a specific accumulation of mitochondrial matrix proteins in the cytosolic fractions of hepatocytes cultured over a 24 h period. The levels of acetyl-CoA acetyltransferase, 3-ketoacyl-CoA thiolase and glutamate dehydrogenase proteins increased 1.9-, 2.0- and 2.2-fold respectively. Their status as mature, oligomeric, but enzymically inactive enzymes strongly suggests that they originate from a leakage of autophagosomes, a constituent of the non-selective autophagic/lysosomal pathway for degradation of whole mitochondria.
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PMID:Turnover of matrix proteins in mammalian mitochondria. 1198 1

The obligate intracellular parasite Toxoplasma gondii is an important pathogen of humans and animals. The tachyzoite of T. gondii is the main life-cycle stage that is responsible for toxoplasmosis. Study of the antigenicity of soluble tachyzoite antigen (STAg) is important for discovery of protective antigens which will aid in the detection and prevention of toxoplasmosis. At present, no complete proteome map of T. gondii STAg is established, although a large-scale whole proteomic analysis of tachyzoites is underway. In this study, 1227 protein spots of T. gondii soluble tachyzoite antigen (STAg) were fractionated by 2-dimensional electrophoresis (2-DE) at pH range 3-10. By mass spectrometry (MS) analysis, among the separated 1227 protein spots, 426 were identified by searching the Swissport and NCBI nr databases. Two hundred and thirty of these identified spots (230/426, 54%) were demonstrated to be T. gondii protein by MS. Of the 21 Toxoplasma protein spots identified by Western blot with rabbit anti-T. gondii serum, 16 had immunoregulatory functions and five had immune defense functions. Due to multiple spots for a single protein, these 16 spots represented 11 proteins: a putative protein disulfide isomerase (PDI), heat shock protein 60 (Hsp60), a pyruvate kinase (PK), a putative glutamate dehydrogenase (GDH), a coronin, a heat shock protein 70 (Hsp70), a protein kinase C receptor 1 (RACK1), a malate dehydrogenase (MDH), a major surface antigen 1 (SAG1), an uridine phosphorylase (UPase) and a peroxiredoxin (Prx). Among the identified 11 proteins, except that the antigenicity and immunogenicity of the SAG1 has been reported and antigenicity of Hsp70 has been disputed, the remaining antigenic proteins were first identified in this study. In conclusion, we obtained nine novel types of immunogenic proteins that might be potential candidates of vaccine development for toxoplasmosis, which we will confirm in later studies.
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PMID:Toxoplasma gondii: proteomic analysis of antigenicity of soluble tachyzoite antigen. 1954 23