Contractile differentiation of foetal cattle muscles: intermuscular variability

Gagnière, Hélène; Picard, Brigitte; Geay, Y.

doi:10.1051/rnd:19990510

Cited by 40 publications

(39 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…However, muscles display a variability in the kinetics of differentiation. In particular, BF and MA differentiate later than ST muscle [25]. Interestingly, lower myostatin expression during the last trimester coincides temporally with the acquisition of contractile and metabolic properties of fibres in ST and BF.…”

Section: Differential Expression Between Developing Muscles Accordingmentioning

confidence: 90%

“…An explanation for the absence of detection of mRNA within the first generation can be that primary fibres are the most advanced in their differentiation at the stages we studied. In particular, differentiation is completed at 180 dpc [25,40]. At 90 and 180 dpc, expression in ST was restricted to myotubes containing developmental MHC but not any adult MHC.…”

Section: The Location Of Myostatin Expression Within the Less Differementioning

confidence: 96%

“…For in vitro studies, four Holstein foetuses (tested for the absence of a myostatin mutation) were produced by artificial insemination. They were collected at the gestational age of 100 days, corresponding to a period of intense proliferation of the second myoblast generation [25].…”

Section: Animalsmentioning

confidence: 99%

“…Myosin heavy chain (MHC) isoform content was revealed at development stages by immuno-histochemical staining using the following monoclonal antibodies (MAB) purchased from Biocytex (Marseille, France): MAB S, F36 5B9, specific to slow MHC; MAB R, F113 15F4, specific to fast MHC (MHC 2a and 2b, 2x); MAB F, F158 4C10, specific to foetal MHC; MAB I+IIb+IIx, S5 8H2, specific to both slow and fast 2b and 2x MHC (without any cross-reactivity with 530 V. Deveaux et al The reactivity of all these antibodies has been tested on bovine muscle [25,30].…”

Section: Muscle Fibre-type Determinationmentioning

confidence: 99%

“…Differences in the temporal pattern of myostatin expression may rely on the differential precocity of the muscles. In cattle, proliferation of muscle cells occurs during the first two trimesters of gestation, whereas their contractile and metabolic differentiations occur in the last trimester [25,40]. However, muscles display a variability in the kinetics of differentiation.…”

Section: Differential Expression Between Developing Muscles Accordingmentioning

confidence: 99%

See 4 more Smart Citations

Location of myostatin expression during bovine myogenesis in vivo and in vitro

et al. 2003

Self Cite

View full text Add to dashboard Cite

-Mutations in the myostatin gene lead to double-muscling in cattle indicating that it is a negative regulator of the total number of muscle fibres. Myostatin expression was analysed by RT-PCR in three developing bovine muscles. It decreased during differentiation in Semitendinosus and Biceps femoris, and increased in the late differentiating Masseter during gestation. A combination of in situ hybridisation and immuno-histochemical detection of myosin heavy chains (MHC) allowed us to locate the expression in myofibres containing only developmental MHC at different stages and in fast IIA fibres at the end of gestation. In vitro, myostatin was undetectable during proliferation, peaked at the onset of fusion and decreased during terminal differentiation. It was not detected in myotubes by in situ hybridisation. The inhibition of differentiation by BrdU prevented the decrease in expression. Our results show that the peak in myostatin expression coincides with early differentiation indicating a regulatory role in cattle myogenesis. myostatin [GDF8] / cattle / myogenesis / myoblast culture / in situ hybridisation

show abstract

Section: Differential Expression Between Developing Muscles Accordingmentioning

confidence: 90%

Section: The Location Of Myostatin Expression Within the Less Differementioning

confidence: 96%

Section: Animalsmentioning

confidence: 99%

Section: Muscle Fibre-type Determinationmentioning

confidence: 99%

Section: Differential Expression Between Developing Muscles Accordingmentioning

confidence: 99%

See 3 more Smart Citations

Location of myostatin expression during bovine myogenesis in vivo and in vitro

et al. 2003

Self Cite

View full text Add to dashboard Cite

show abstract

Electrophoretic and immunochemical evidence showing that marsupial limb muscles express the same fast and slow myosin heavy chains as eutherians

et al. 2001

View full text Add to dashboard Cite

Limb muscles of eutherian (placental) mammals express a slow and three fast isoforms of myosin heavy chain (MyHC), but little is known about marsupial MyHCs. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of limb MyHCs from seven marsupial species, spanning two orders, revealed four components, each of which specifically cross-reacted in Western blots with a monoclonal antibody (mAb) against a corresponding eutherian MyHC. For all seven species, the relative mobility of the band identified by each mAb matched that in the rat, suggesting that the four are homologous to eutherian slow, 2B, 2X and 2A MyHCs, respectively, in the order of decreasing mobility. Immunohistochemical analysis of fast marsupial limb muscles identitied four different fiber populations whose relative fiber size spectra (IIA

show abstract

Advancing Technologies for Spatial and Temporal Proteomics

Doherty¹

2011

Methods in Animal Proteomics

View full text Add to dashboard Cite

Contractile differentiation of foetal cattle muscles: intermuscular variability

Cited by 40 publications

References 30 publications

Location of myostatin expression during bovine myogenesis in vivo and in vitro

Location of myostatin expression during bovine myogenesis in vivo and in vitro

Electrophoretic and immunochemical evidence showing that marsupial limb muscles express the same fast and slow myosin heavy chains as eutherians

Advancing Technologies for Spatial and Temporal Proteomics

Contact Info

Product

Resources

About