Stretch-induced transformations in myosin expression of quail anterior latissimus dorsi muscle. 1995

W J Roman, and S E Alway
Department of Exercise Science, Ohio State University, Columbus 43210, USA.

We have previously found alterations in expression of native myosin isoforms during adaptations to 30 d of stretch-induced hypertrophy in the quail anterior latissimus dorsi muscle (ALD). However, myosin heavy and light chain expression have not been studied during adaptations to stretch. In the current study, expression of myosin heavy and light chains and native myosin isoforms were characterized after placing a weight on one wing of Japanese quail for 0, 7, 14, or 21 d (N = 8 birds.d-1). ALD muscle mass was significantly greater at days 14 (67.0 +/- 4.4%) and 21 (70.2 +/- 4.0%) of stretch compared to day 7 (53.6 +/- 2.9%) of stretch. Native slow myosin-2 (SM2) expression increased from 43.1 +/- 17% in control muscles to 55 +/- 1.2% in stretch muscles, relative to the total myosin pool. The increase in native SM2 expression (approximately 12%) was observed at all three time points of stretch. In contrast, native slow myosin-1 (SM1) expression significantly decreased from 34.1% +/- 1.7% in the control muscles to 24.6 +/- 1.2% in the stretch muscles, relative to the total myosin pool. There was an increased expression of slowly heavy chain-two (SHC2) concurrent with a downregulation of the slow heavy chain-1 (shc1). There was no change in the relative percentages of either slow or fast myosin light chains in overloaded muscles at any of the time points following stretch. These results demonstrate that changes in myosin heavy chain expression, but not myosin light chain expression accompany stretch-induced hypertrophy in the quail ALD.

UI MeSH Term Description Entries
D003370 Coturnix A genus of BIRDS in the family Phasianidae, order GALLIFORMES, containing the common European and other Old World QUAIL. Japanese Quail,Coturnix japonica,Japanese Quails,Quail, Japanese,Quails, Japanese
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D018482 Muscle, Skeletal A subtype of striated muscle, attached by TENDONS to the SKELETON. Skeletal muscles are innervated and their movement can be consciously controlled. They are also called voluntary muscles. Anterior Tibial Muscle,Gastrocnemius Muscle,Muscle, Voluntary,Plantaris Muscle,Skeletal Muscle,Soleus Muscle,Muscle, Anterior Tibial,Muscle, Gastrocnemius,Muscle, Plantaris,Muscle, Soleus,Muscles, Skeletal,Muscles, Voluntary,Skeletal Muscles,Tibial Muscle, Anterior,Voluntary Muscle,Voluntary Muscles
D018994 Myosin Light Chains The smaller subunits of MYOSINS that bind near the head groups of MYOSIN HEAVY CHAINS. The myosin light chains have a molecular weight of about 20 KDa and there are usually one essential and one regulatory pair of light chains associated with each heavy chain. Many myosin light chains that bind calcium are considered "calmodulin-like" proteins. Myosin Alkali Light Chains,Myosin Alkali Light Chain,Myosin Essential Light Chain,Myosin Essential Light Chains,Myosin Light Chain,Myosin Regulatory Light Chain,Myosin Regulatory Light Chains,Light Chain, Myosin,Light Chains, Myosin
D018995 Myosin Heavy Chains The larger subunits of MYOSINS. The heavy chains have a molecular weight of about 230 kDa and each heavy chain is usually associated with a dissimilar pair of MYOSIN LIGHT CHAINS. The heavy chains possess actin-binding and ATPase activity. Myosin Heavy Chain,Heavy Chain, Myosin,Heavy Chains, Myosin

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