Cellular and molecular diversities of mammalian skeletal muscle fibers

Pette, Dirk; Staron, Robert S.

doi:10.1007/3540528806_3

Cited by 525 publications

(609 citation statements)

References 598 publications

Supporting

Mentioning

579

Contrasting

Unclassified

Order By: Relevance

“…Histochemical determination of fiber type metabolic characteristics is not sensitive to quantitative variation in metabolic capacity. Considerable metabolic heterogeneity can exist among fibers of identical histochemical characteristics, both within and among species of mammals (31)(32)(33). Thus, although our data indicate that similar fiber type distributions exist among wild, lab, and hybrid mice, they cannot eliminate the possibility that the fiber types of one or more groups may be faster contracting or more oxidative than are homologous fibers in another group.…”

Section: Discussionmentioning

confidence: 58%

Maximal sprint speeds and muscle fiber composition of wild and laboratory house mice

Garland

Gleeson

Aronovitz

et al. 1995

Physiology & Behavior

View full text Add to dashboard Cite

GARLAND, T., JR., T. T. GLEESON, B. A. ARONOVITZ, C. S. RICHARDSON AND M. R. DOHM. Maximal sprint speeds and muscle fiber composition of wiM and laboratory house mice. PHYSIOL BEHAV 58(5) 869-876, 1995.--We compared males from four groups of house mice (Mus domesticus), all bred and raised under common conditions in the laboratory: randombred Hsd:ICR, a wild population from Wisconsin; hybrids from lab dams; hybrids from wild dams.. Wild mice were much faster sprinters (maximal forced sprint speeds over 1.0 m ranged from 2.38 to 3.34 m/s) than were lab mice (range = 0.89-1.68 m/s). Hybrids exhibited intermediate speeds (range = 1.54-2.70 m/s) and body masses, indicating largely additive inheritance. Type-specific mean muscle fiber cross-sectional areas of the gastrocnemius muscle did not differ significantly among groups. Percentage cross-sectional areas occupied by each of the three identified fiber types also did not differ significantly among groups, nor did they covary with body mass. For their body mass, however, lab mice had smaller gastrocnemius muscles than did wild and hybrid mice, which had muscles of similar size. Although we cannot rule out the possibility that smaller gastrocnemius muscles or slight differences in fiber composition account for the lower sprint speeds of the lab mice, we suggest that differences in unmeasured physiological, behavioral or motivational factors are probably the primary cause. This interpretation is supported by a lack of correlation between individual differences in sprint speed and either relative gastrocnemius muscle mass or muscle fiber type composition.

show abstract

Section: Discussionmentioning

confidence: 58%

Maximal sprint speeds and muscle fiber composition of wild and laboratory house mice

Garland

Gleeson

Aronovitz

et al. 1995

Physiology & Behavior

View full text Add to dashboard Cite

show abstract

“…Thus insulin-stimulated glucose uptake was lower in white but not red quadriceps and gastrocnemius muscles. While the metabolic differences between red, which is predominantly oxidative, and white skeletal muscle, which is predominantly glycolytic, have been well characterised [46], the soleus, a pure red muscle did demonstrate insulin resistance. The difference in the responsiveness of different muscles remains unclear.…”

Section: Discussionmentioning

confidence: 98%

Peripheral insulin resistance develops in transgenic rats overexpressing phosphoenolpyruvate carboxykinase in the kidney

et al. 2003

View full text Add to dashboard Cite

Aims/hypothesis. To study the secondary consequences of impaired suppression of endogenous glucose production (EGP) we have created a transgenic rat overexpressing the gluconeogenic enzyme phosphoenolpyruvate carboxykinase (PEPCK) in the kidney. The aim of this study was to determine whether peripheral insulin resistance develops in these transgenic rats. Methods. Whole body rate of glucose disappearance (R d ) and endogenous glucose production were measured basally and during a euglycaemic/hyperinsulinaemic clamp in phosphoenolpyruvate carboxykinase transgenic and control rats using [6-3 H]-glucose. Glucose uptake into individual tissues was measured in vivo using 2-[1-14 C]-deoxyglucose. Results. Phosphoenolpyruvate carboxykinase transgenic rats were heavier and had increased gonadal and infrarenal fat pad weights. Under basal conditions, endogenous glucose production was similar in phosphoenolpyruvate carboxykinase transgenic and control rats (37.4±1.1 vs 34.6±2.6 µmol/kg/min). Moderate hyperinsulinaemia (810 pmol/l) completely suppressed EGP in control rats (−0.6±5.5 µmol/kg/min, p<0.05) while there was no suppression in phosphoenolpyruvate carboxykinase rats (45.2±7.9 µmol/kg/min). Basal R d was comparable between PEPCK transgenic and control rats (37.4±1.1 vs 34.6±2.6 µmol/kg/min) but under insulin-stimulated conditions the increase in R d was greater in control compared to phosphoenolpyruvate carboxykinase transgenic rats indicative of insulin resistance (73.4±11.2 vs 112.0±8.0 µmol/kg/min, p<0.05). Basal glucose uptake was reduced in white and brown adipose tissue, heart and soleus while insulin-stimulated transport was reduced in white and brown adipose tissue, white quadriceps, white gastrocnemius and soleus in phosphoenolpyruvate carboxykinase transgenic compared to control rats. The impairment in both white and brown adipose tissue glucose uptake in phosphoenolpyruvate carboxykinase transgenic rats was associated with a decrease in GLUT4 protein content. In contrast, muscle GLUT4 protein, triglyceride and long-chain acylCoA levels were comparable between PEPCK transgenic and control rats. Conclusions/interpretation. A primary defect in suppression of EGP caused adipose tissue and muscle insulin resistance. [Diabetologia (2003[Diabetologia ( ) 46:1338[Diabetologia ( -1347

show abstract

“…Newly formed muscle fibers are soon innervated by motor neurons and subsequently undergo contractile excitation, extensive growth through continued myoblast fusion, and activity-and hormonedependent modifications in muscle gene expression patterns, resulting in the formation of several physiologically and biochemically specialized adult fiber types (Kelly and Rubinstein, 1994). Slow (type I) and fast (type II) fibers differentially express related genes encoding "slow" and "fast" isoforms of many muscle proteins, including myosin and troponin subunits (Pette and Staron, 1990;Schiaffino and Reggiani, 1996). Most muscle gene families include a single fast isoform gene expressed in all fast fibers.…”

Section: Introductionmentioning

confidence: 99%

TnIfast IRE enhancer: Multistep developmental regulation during skeletal muscle fiber type differentiation

Hallauer

Hastings

2002

Developmental Dynamics

View full text Add to dashboard Cite

To identify developmental steps leading to adult skeletal muscle fiber-type-specific gene expression, we carried out transgenic mouse studies of the IRE enhancer of the quail TnIfast gene. Histochemical analysis of IRE/herpesvirus tk promoter/␤-galactosidase reporter transgene expression in adult muscle directly demonstrated IRE-driven fast vs. slow fiber-type specificity, and IIB>IIX>IIA differential expression among the fast fiber types: patterns similar to those of native-promoter TnIfast constructs. These tissue-and cell-type specificities are autonomous to the IRE and do not depend on interactions with a muscle gene promoter. Developmental studies showed that the adult pattern of IRE-driven transgene expression emerges in three steps: (1) activation during the formation of primary embryonic (presumptive slow) muscle fibers; (2) activation, to markedly higher levels, during formation of secondary (presumptive fast) fibers, and (3) differential augmentation of expression during early postnatal maturation of the IIB, IIX, IIA fast fiber types. These results provide insight into the roles of gene activation and gene repression mechanisms in fiber-type specificity and can account for apparently disparate results obtained in previous studies of TnI isoform expression in development. Each of the three IRE-driven developmental steps is spatiotemporally associated with a different major regulatory event at the fast myosin heavy chain gene cluster, suggesting that diverse muscle gene families respond to common, or tightly integrated, regulatory signals during multiple steps of muscle fiber differentiation.

show abstract

Cellular and molecular diversities of mammalian skeletal muscle fibers

Cited by 525 publications

References 598 publications

Maximal sprint speeds and muscle fiber composition of wild and laboratory house mice

Maximal sprint speeds and muscle fiber composition of wild and laboratory house mice

Peripheral insulin resistance develops in transgenic rats overexpressing phosphoenolpyruvate carboxykinase in the kidney

TnIfast IRE enhancer: Multistep developmental regulation during skeletal muscle fiber type differentiation

Contact Info

Product

Resources

About