Abnormal myosin heavy chain variant associated with avian muscular dystrophy

Rushbrook, Julie Ivory; Yuan, Anna I.; Stracher, Alfred

doi:10.1002/cm.970010402

Cited by 21 publications

(6 citation statements)

References 16 publications

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“…A previous study also found no difference in the myosin heavy chain from the ALD of adult dystrophic chicken when compared to the ALD of adult normal chicken, although different strains were used. 42 In contrast, the PLD and PM of adult dystrophic chickens clearly had abnormal myosin components. Differences between the normal and dystrophic chickens could be observed by 40 days after hatching.…”

Section: Discussionmentioning

confidence: 98%

Myosin components of the latissimus dorsi and the pectoralis major muscles in the dystrophic chicken

Bandman

1984

Muscle and Nerve

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The myosin composition of the anterior latissimus dorsi, the posterior latissimus dorsi, and the pectoralis major muscles was examined in the inbred White Leghorn dystrophic chicken and its isogenic normal line at different ages during development and maturation. Using the biochemical methods of native gel electrophoresis, one- and two-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS PAGE), and peptide mapping, it was found that myosin isozyme changes occurred normally in the anterior latissimus dorsi muscle. However, in the posterior latissimus dorsi muscle, slow myosin components which were not present in the adult normal muscle were present in the adult dystrophic muscle. In addition, the pectoralis major muscle of the dystrophic chicken failed to undergo the neonatal to adult fast myosin isozyme transition. Our data also showed that muscle cell cultures derived from the pectoralis major muscle of dystrophic chickens expressed identical myosin components to cultures derived from normal embryos. However, since these cultures only produced embryonic myosins even after 1 month in culture, it implied that cells in tissue culture were phenotypically normal because present cell culture conditions were insufficient to induce the fetal to adult isozyme changes.

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Section: Discussionmentioning

confidence: 98%

Myosin components of the latissimus dorsi and the pectoralis major muscles in the dystrophic chicken

Bandman

1984

Muscle and Nerve

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“…Evidence for a myosin heavy chain variant which appears to be clearly associated with expression of the dystrophic gene has been presented elsewhere. 21 Of the two LC-1 forms identified, type I predominates in commercially bred White Leghorn birds, whereas type I1 is the major form in birds of The absence of the type I LC-1 allele in the 7 individuals of the Connecticut dystrophic strain is somewhat surprising since the Connecticut dystrophic birds were outcrossed at one time to White Leghorn However, although the Connecticut dystrophic birds have been bred at random in a closed population for the last 15 years, the breeding procedure, which involves selection of only a few males each year, may quite easily have resulted in the loss of an allele for which the birds were at some point heterozygous (Goetinck, P, 1982, personal communication).…”

Section: Muscle and Nervementioning

confidence: 99%

Two major allelic forms of myosin light chain‐1 in strains of normal and dystrophic chickens

1982

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Evidence is presented from electrophoresis and peptide-mapping for the existence of two major allelic forms of myosin light chain-1 in the fast white muscle fibers of domestic chickens. One form predominates in birds of White Leghorn stock, the other in birds of New Hampshire Red stock. The two light chain-1 forms were invariant during development. Variability was not detected in light chains-2 or -3. The distribution of the two forms in two strains homozygous for the am gene for muscular dystrophy--Connecticut dystrophic and line 413--and their controls, White Leghorn and line 412, respectively, while clearly unrelated to avian dystrophy, emphasizes the heterogeneity in background genes of these non-inbred lines and indicates caution in their use in studies of avian dystrophy.

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“…Myosin. Myosin was prepared from the pectoralis major muscle of adult chickens (6 months or older) as described (Rushbrook et al, 1981), employing an extraction buffentissue ratio of 3:1 and a 35-50% saturation ammonium sulfate cut. The red strip (Gauthier & Lowey, 1977) was omitted.…”

Section: Methodsmentioning

confidence: 99%

Variability in the amino-terminus of myosin light chain-1

Rushbrook¹,

Wadewitz²,

Elzinga³

et al. 1988

Biochemistry

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Three naturally occurring variants of myosin light chain 1, type I, II, and III from avian fast-twitch muscle, have been analyzed by reverse-phase HPLC peptide mapping and amino acid sequencing. Difference peptides were absent from accompanying digests of the related protein, myosin light chain 3, indicating that the heterogeneity was located in the N-terminal 50 residues unique to light chain 1. The type II variant possessed the previous published sequence for the protein [Nabeshima Y., Fujii-Kuriyama, Y., Muramatsu, M., & Ogata, K. (1984) Nature (London) 308, 333-338]. The type I variant, which migrates faster than the type II on SDS gene electrophoresis, contained a Pro----Ala substitution at residue 15, turning the Lys-Pro-(Ala)5(Pro-Ala)7 stretch in this region into Lys-Pro-(Ala)7(Pro-Ala)6. The type III variant, which migrates just faster than the type I, had an (Ala)2 deletion in the (Ala)5 run, yielding Lys-Pro-(Ala)3-(Pro-Ala)7. As indicated by the SDS gel migration rates, the type I and III variants are significantly shorter in length than the type II. The benign nature of the changes is consistent with a flexible arm function for the N-terminal region of light chain 1, with the structural changes in the variants occurring in the spacer region of the arm.(ABSTRACT TRUNCATED AT 250 WORDS)

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Abnormal myosin heavy chain variant associated with avian muscular dystrophy

Cited by 21 publications

References 16 publications

Myosin components of the latissimus dorsi and the pectoralis major muscles in the dystrophic chicken

Myosin components of the latissimus dorsi and the pectoralis major muscles in the dystrophic chicken

Two major allelic forms of myosin light chain‐1 in strains of normal and dystrophic chickens

Variability in the amino-terminus of myosin light chain-1

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