PubMed · 4946077
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G Muiesan, C A Sorbini, V Grassi. Respiratory function in the aged.. https://pubmed.ncbi.nlm.nih.gov/4946077/
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BACKGROUND: Coronary revascularization provides the greatest survival advantage in those patients with the greatest mortality risk. This study examines the relationship between variables that predict mortality and the use of angiography and revascularization after acute myocardial infarction. METHODS: Study of 4823 survivors of acute myocardial infarction, who underwent angiography between 6 hours and 5 days of admission, to determine the relationship between factors that predict mortality and the use of angiography (n = 2274), angioplasty (n = 692), and bypass surgery (n = 469). RESULTS: Except for recurrent angina, clinical factors that predict higher mortality were associated with a lower use of angiography (the multivariable adjusted odds ratio was 0.47 for older age, 0.85 for a history of infarction, 0.50 for patients not receiving thrombolytic medications, 0.64 for new heart failure, and 2.75 for recurrent angina [P < .001 for all factors]). A similar relationship was observed among patients selected for angioplasty (the odds ratio was 0.51 for an ejection fraction of < 40%, 0.72 for those patients not receiving thrombolytic medications, 0.74 for a history of infarction, and 1.94 for recurrent angina [P < .001 for all factors]). In contrast, patients with unfavorable prognostic profiles were much more likely to undergo coronary bypass surgery (the odds ratio was 1.46 for recurrent angina, 1.28 for older age groups, 2.23 for new heart failure, 1.28 for patients not receiving thrombolytic medications, and 1.46 for a history of infarction [P < .001 for all factors]). CONCLUSIONS: These data suggest that aside from symptoms of recurrent angina, the use of angiography and angioplasty is not driven by mortality risk stratification. In contrast, bypass surgery is preferentially performed in patients at increased risk for mortality.
The multicatalytic proteinase complex (MPC) (proteasome) is a high-molecular-weight proteolytic enzyme found in eukaryotic cells and archaebacteria. Regulatory proteins that inhibit or activate the MPC have been described. Association with an ATPase complex alters the specificity of the multicatalytic proteinase complex to permit cleavage of ubiquitinylated proteins. Unidentified proteins have been observed in highly purified preparations of the multicatalytic proteinase complex. Based on immunoreactivity and N-terminal sequencing, we have identified heat-shock protein 90 as a major component of the multicatalytic proteinase complex prepared from 1-month, but not 2-year bovine lenses. alpha-Crystallin, a lens structural protein with chaperone activity, is also found in multicatalytic proteinase complex preparations. Both heat-shock protein 90 and alpha-crystallin inhibit hydrolysis of Cbz-Leu-Leu-Leu-MCA by the multicatalytic proteinase complex at a stoichiometry of 1 mol heat-shock protein per mole of MPC. Heat-shock proteins may interact with denatured proteins and facilitate their degradation. These studies give evidence for the involvement of heat-shock proteins in proteolysis by direct interaction with the multicatalytic proteinase complex.