Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.6.4.1 (myosin ATPase)
 1,140 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Postoperative pulmonary complication and respiratory failure, frequently seen in undernourished patients such as those with esophageal cancer, were suspected to be due to respiratory muscle wasting caused by nutritional depletion. Based on this idea, the respiratory muscles obtained by biopsies during operation from diaphragm, external intercostal muscle, and rectus abdominis muscle were assessed histochemically in 32 patients. The specimens were stained for myosin ATPase to differentiate the types of muscle fibers, and then the size and distribution of the muscle fibers of each type were measured. In diaphragm muscle, cross-sectional areas of type 1 & 2 and the ratio of the area occupied by each fiber were usually the same; in external intercostal muscle, however, type 1 fibers were dominant and in rectus abdominis muscle, type 2 fibers were dominant. The cross-sectional area of each respiratory muscle fiber well correlated with certain anthropometrical indexes, and the nutritionally depleted cases, the muscle fibers were of a smaller size suggesting less respiratory muscle strength. The ratio of the area occupied by type 1 fibers in diaphragm muscle was linearly related to serum albumin, total cholesterol, and PNI (prognostic nutritional index). Type 2 fibers were dominant in malnourished patients, suggesting greater fatigue compared to well-nourished cases. Opposite findings were obtained in external intercostal muscle and rectus abdominis muscle, and the ratio of the area occupied by type 2 fibers was smaller in the undernourished cases, suggesting reduced maximum strength of these muscles.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Histochemical analysis of respiratory muscles of patients with esophageal cancer--with special reference to the preoperative nutritional state]. 214 8

Vitamin D deficiency leads to muscle wasting in both animals and humans. A vitamin D-deficient rat model was created using Sprague Dawley male rats. We studied the involvement of the ubiquitin proteasome and other proteolytic pathways in vitamin D deficiency-induced muscle atrophy. To delineate the effect of hypocalcemia that accompanies D deficiency, a group of deficient rats was supplemented with high calcium alone. Total protein degradation in muscle was assessed by release of tyrosine; proteasomal, lysosomal, and calpain enzyme activities were studied using specific substrates by fluorometry, and E2 enzyme expression was assessed by Western blot analysis. Muscle histology was done by myosin ATPase staining method, whereas 3-methylhistidine in the urine was estimated using HPLC. Muscle gene expression was measured by semiquantitative RT-PCR. Total protein degradation in muscle and the level of 3-methylhistidine in urine were increased in the deficient group compared with the control group. Proteasomal enzyme activities, expression of the E2 ubiquitin conjugating enzyme, and ubiquitin conjugates were increased in the deficient group compared with controls. On the other hand, lysosomal and calpain activities were not altered. Type II fiber area, a marker for muscle atrophy, was decreased in the deficient muscle compared with control muscle. Muscle atrophy marker genes and proteasomal subunit genes were up-regulated, whereas myogenic genes were down-regulated in D-deficient muscle. From the results it appears that the ubiquitin proteasome pathway is the major pathway involved in vitamin D deficiency-induced muscle protein degradation and that calcium supplementation alone in the absence of vitamin D partially corrects the changes.
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PMID:Vitamin D deficiency-induced muscle wasting occurs through the ubiquitin proteasome pathway and is partially corrected by calcium in male rats. 2414 94