myosin isoenzyme
Recently Published Documents


TOTAL DOCUMENTS

60
(FIVE YEARS 0)

H-INDEX

17
(FIVE YEARS 0)

1998 ◽  
Vol 30 (02) ◽  
pp. 84-87 ◽  
Author(s):  
G. Morris ◽  
S. Melton ◽  
M. Hegsted ◽  
W. Bartlett


1997 ◽  
Vol 29 (Supplement) ◽  
pp. 94
Author(s):  
G. S. Morris ◽  
S. A. Melton ◽  
M. J. Keenan ◽  
M. Hegsted Texas




Life Sciences ◽  
1996 ◽  
Vol 58 (10) ◽  
pp. 833-838 ◽  
Author(s):  
G.Stephen Morris ◽  
Michael C. Prevost ◽  
Arnold G. Nelson


1990 ◽  
Vol 259 (3) ◽  
pp. H866-H871 ◽  
Author(s):  
A. Malhotra ◽  
P. Buttrick ◽  
J. Scheuer

Previous studies have demonstrated a role for sex hormones in maintaining normal heart weight and myosin isoenzyme balance in the rat. To determine if sex hormones were necessary to elicit cardiac adaptations to the chronic loads of swimming or hypertension, female rats were gonadectomized (X) and then exposed either to a chronic swimming program (Sw) or to renal hypertension for 8-10 wk. Because gonadectomy in females increased heart and body weight, separate groups of food-restricted sedentary and Sw gonadectomized females (XFR) were included. Swimming resulted in significant increases in both heart weight and in the percent ventricular V1 isomyosin in female controls (C), X, and XFR. Hypertension was studied in C, X, and X with estrogen replacement. Cardiac hypertrophy developed in all groups, but estrogen therapy attenuated the decline in percent V1 isomyosin in both normotensive and hypertensive X animals. Swimming, which is generally not associated with cardiac hypertrophy in males, was also studied in that sex. Gonadectomy did not alter either the heart weight or the myosin isoenzyme response to Sw, although testosterone replacement in gonadectomized males restored ventricular V1 myosin levels to or above normal. Measures of serum thyroid levels and of myocardial catecholamines failed to demonstrate a causal relationship between these hormones and the various results. Therefore, although sex hormones are important for maintaining normal heart weights and myosin isoenzyme balance in rats, they do not appear to be important in the adaptations hearts exhibit when exposed to physiological or pathological loads.



1990 ◽  
Vol 265 (2) ◽  
pp. 525-532 ◽  
Author(s):  
P Gregory ◽  
J Gagnon ◽  
D A Essig ◽  
S K Reid ◽  
G Prior ◽  
...  

Overload hypertrophy of the chicken anterior latissimus dorsi muscle is accompanied by a replacement of one myosin isoenzyme (slow myosin-1, SM1) by another (slow myosin-2, SM2). To investigate the molecular mechanisms by which these changes occur, we measured the fractional synthesis rates (ks) in vivo of individual myosin-heavy-chain isoenzymes, total actin and total protein during the first 72 h of muscle growth. Although the ks of total protein and actin were doubled at 24 h, the ks for SM1 and SM2 were depressed. However, the ks of both isomyosins were nearly tripled by 72 h. Despite the increase in muscle size observed at 72 h, the amount of SM1 was reduced by half, indicating increased degradation of SM1. Results of translation of polyribosomes in vitro paralleled the results obtained in vivo. The proportion of total polyadenylylated mRNA in total RNA was increased at 48 and 72 h, but unchanged at 24 h despite the increase in protein synthesis at 24 h. Nuclease-protection analyses indicate that the level of specific SM1 and SM2 mRNAs change in a reciprocal fashion during overload. We conclude that gene-specific and temporal differences exist in the regulatory mechanisms that control overload-induced muscle growth.



1989 ◽  
Vol 256 (4) ◽  
pp. R976-R981
Author(s):  
G. S. Morris ◽  
R. E. Herrick ◽  
K. M. Baldwin

Although food restriction reduces the relative expression of the rodent cardiac myosin isoenzyme V1, the contribution of accompanying metabolic changes to the induction and maintenance of this isoenzyme shift remains unknown. Hence, this study was undertaken to determine the role of carbohydrate (CHO) utilization in the regulation of cardiac myosin isoenzyme distribution in food-restricted rats. Female Sprague-Dawley rats received either a mixed diet (55% of calories as CHO, M) or a high-carbohydrate diet (75% of calories as CHO, HC). Additional animals in each dietary group received daily injections of triiodothyronine (T3; 0.075 microgram/100 microM + T3, HC + T3). Three weeks of food restriction reduced left ventricular Ca2+-activated myofibrillar adenosinetriphosphatase activity by 24% and the relative amount of the myosin V1 isoenzyme by 57% in the M group relative to free-eating controls (P less than 0.05). In contrast, these measures were reduced by only 9 and 21%, respectively, in the HC group. Administration of T3 exerted no apparent effect on V1 expression, regardless of diet. Furthermore, the increased expression of V1 in both HC and HC + T3 groups occurred independently of changes in several measures of thyroid status including serum T3 levels, O2 consumption, heart rate, and systemic blood pressure. These results further suggest that metabolic factors, specifically those associated with CHO utilization, can influence cardiac myosin isoenzyme expression.



1989 ◽  
Vol 256 (4) ◽  
pp. E453-E458 ◽  
Author(s):  
N. Afzal ◽  
G. N. Pierce ◽  
V. Elimban ◽  
R. E. Beamish ◽  
N. S. Dhalla

The effects of verapamil on cardiac myofibrillar adenosinetriphosphatase (ATPase) activity, myosin ATPase, and myosin isoenzyme profile as well as sarcoplasmic reticular Ca2+ uptake and ATPase activities were examined in Sprague-Dawley rats made diabetic with a single injection of streptozotocin (65 mg/kg). Myofibrillar ATPase activity and myosin Ca2+ ATPase activity as well as Ca2+ uptake and Ca2+-stimulated ATPase activities of the sarcoplasmic reticulum were significantly decreased in diabetic hearts in comparison to the control values. The myosin isoenzyme component V3 was prominent in diabetic hearts, whereas V1 isoenzyme was the major myosin component in control hearts. Chronic treatment of diabetic rats with verapamil (8 mg/kg daily for 4-8 wk) resulted in an improvement of the altered myofibrillar ATPase activity, myosin ATPase, myosin isoenzyme distribution, and sarcoplasmic reticular Ca2+-pump activities in ventricular tissue. The ability of verapamil to normalize the observed defects in the subcellular organelles in diabetic cardiomyopathy may be related to its effects in controlling the entry of Ca2+ into the cardiac cell.



1989 ◽  
Vol 21 (Supplement) ◽  
pp. S28
Author(s):  
M. M. Sopper ◽  
E. G. Noble ◽  
P. A. Merrifield
Keyword(s):  


Sign in / Sign up

Export Citation Format

Share Document