Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.25.1 (proteasome)
 28,817 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The ubiquitin-proteasome cycle is a complex, non-lysosomal biochemical process for intracellular protein degradation. This process involves many enzymes. One enzyme involved in this process is ubiquitin carboxyl-terminal hydrolase L5 (UCHL5), which deubiquitylates the polyubiquitin chain into ubiquitin. In this report, we isolated, sequenced, and characterized the channel catfish UCHL5 cDNA. The complete nucleic acid sequence of the channel catfish UCHL5 cDNA is comprised of 1,357 nucleotides, including an open reading frame, which appears to encode a putative peptide of 329 amino acid residues. The estimated molecular mass and pI of this peptide are 37.6 kDa and 4.84 at pH 7.0, respectively. The degree of conservation of the channel catfish UCHL5 amino acid sequence in comparison to other species ranged from 85% (vs. mouse) to 92% (vs. zebrafish and spotted green pufferfish). The channel catfish UCHL5 transcript was detected by RT-PCR in spleen, head kidney, liver, intestine, skin and gill, suggesting the UCHL5 transcript is constitutively expressed. This research provides important information for further elucidating UCHL5 in the channel catfish ubiquitin-proteasome pathway.
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PMID:Characterization and tissue expression of channel catfish (Ictalurus punctatus Rafinesque, 1818) ubiquitin carboxyl-terminal hydrolase L5 (UCHL5) cDNA. 1926 12

Studies on alcoholic liver injury mechanisms show a significant inhibition of the proteasome activity. To investigate this phenomenon, we isolated proteasome complexes from the liver of rats fed ethanol chronically, and from the liver of their pair-fed controls, using a non-denaturing multiple centrifugations procedure to preserve proteasome-interacting proteins (PIPs). ICAT and MS/MS spectral counting, further confirmed by Western blot, showed that the levels of several PIPs were significantly decreased in the isolated ethanol proteasome fractions. This was the case of PA28alpha/beta proteasome activator subunits, and of three proteasome-associated deubiquitinases, Rpn11, ubiquitin C-terminal hydrolase 14, and ubiquitin carboxyl-terminal hydrolase L5. Interestingly, Rpn13 C-terminal end was missing in the ethanol proteasome fraction, which probably altered the linking of ubiquitin carboxyl-terminal hydrolase L5 to the proteasome. 20S proteasome and most 19S subunits were however not changed but Ecm29, a protein known to stabilize the interactions between the 20S and its activators, was decreased in the isolated ethanol proteasome fractions. It is proposed that ethanol metabolism causes proteasome inhibition by several mechanisms, including by altering PIPs and proteasome regulatory complexes binding to the proteasome.
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PMID:Chronic ethanol feeding affects proteasome-interacting proteins. 1960 68