Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.6.3.14 (ATP synthase)
 7,042 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Our objective in experiments reported here was to identify myofilament proteins of rat hearts either lost or degraded by cardiac ischemia (15- or 60-minute duration) with and without 45 minutes of reperfusion. We correlated these changes with alterations in myofilament sensitivity to Ca2+ and maximum force generation. Protein degradation and loss were assessed by high-performance liquid chromatography, SDS-PAGE, Western blotting analysis, and amino acid sequencing. Compared with nonischemic control hearts, bundles of skinned fibers from hearts subjected to ischemia alone demonstrated a decrease in maximum force generation and an increase in sensitivity to Ca2+. These changes in function were increased with the duration of the ischemia and with reperfusion. With increasing duration of ischemia, there was an increased loss and degradation of myofibrillar alpha-actinin and troponin I (TnI) at its C-terminus. Alpha-actinin and TnI were most susceptible to ischemia, but with 60 minutes of ischemia/reperfusion, there was also degradation of myosin light chain-1 (MLC1) involving a clip of residues 1 to 19. The MLC1 degradation product was detected in the reperfusion effluent (along with troponin T, tropomyosin, and alpha-actinin) but not in the tissue with 60 minutes of ischemia with no reperfusion. Moreover, with ischemia the following proteins became associated with the myofibrils: GAPDH and proteins of the mitochondrial ATP synthase complex. Our results provide new evidence regarding the mechanism by which ischemia/reperfusion causes myocardial injury and support the hypothesis that an important element in the injury is altered activity and structure of the myofilaments.
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PMID:Breakdown and release of myofilament proteins during ischemia and ischemia/reperfusion in rat hearts: identification of degradation products and effects on the pCa-force relation. 946 97

The 14-3-3 protein family is a family of regulatory proteins involved in diverse cellular processes. The presence of 14-3-3 isoforms and the diversity of cellular processes regulated by 14-3-3 isoforms suggest functional specificity of the isoforms. In this study, we report the identification and characterization of a new isoform of the rainbow trout 14-3-3E1 gene generated by alternative splicing. The new isoform contains an insertion of 48 nucleotides (from intron 5) in the coding region of 14-3-3E1 which results in the introduction of a premature stop codon between exon 5 and exon 6. Thus, the alternatively spliced form of 14-3-3E1 (14-3-3E1DeltaC17) lacks 17 amino acid residues at the C terminus encoded by the last exon (exon 6). Reverse-transcription polymerase chain reaction analysis revealed that the wild-type 14-3-3E1 (14-3-3E1wt) is ubiquitously expressed, while 14-3-3E1DeltaC17 shows tissue-specific as well as stage-specific expression during ovarian development and early embryogenesis. Analysis by yeast two-hybrid system demonstrated that 14-3-3E1Delta17 interacts with a number of proteins including ATP synthase, ankyrin repeat domain 13b, cytochrome c subunit VIa, cytochrome c subunit VIb, 60S ribosomal protein L34, solute carrier family 17 member 6 (SLC17A6), troponin I, and an unknown protein. Although all of these proteins except for SLC17A6 also interact with 14-3-3E1wt, 14-3-3E1Delta17 appears to have higher binding affinity with these proteins than 14-3-3E1wt. These findings suggest that alternative splicing affects the function and tissue-specific expression of 14-3-3E1.
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PMID:Identification of a functional splice variant of 14-3-3E1 in rainbow trout. 1959 Sep 24