A comparison of fibroblast and smooth muscle myosins

Burridge, Keith

doi:10.1016/0014-5793(74)80799-4

Cited by 30 publications

(10 citation statements)

References 12 publications

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“…Onedimensional analysis shows that it contains a single alkali type light chain (G2 in Fig. 1) of electrophoretic mobility comparable with that of fast skeletal muscle MLC3F (Burridge, 1974). In chicken the 17 kDa smooth muscle myosin alkali light chain isoform from gizzard has been sequenced and consists of 150 amino acids (cf.…”

Section: The Myosin Alkali Light Chain Isoforms and Their Genesmentioning

confidence: 97%

The myosin alkali light chain proteins and their genes

Barton¹,

Buckingham²

1985

Biochemical Journal

171

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Section: The Myosin Alkali Light Chain Isoforms and Their Genesmentioning

confidence: 97%

The myosin alkali light chain proteins and their genes

Barton¹,

Buckingham²

1985

Biochemical Journal

171

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“…Although it is not exactly the same as its counterpart in muscle (Burridge, 1974), it co-migrates with muscle myosin on sodium dodecyl sulphate-polyacrylamide gels (Plate la). If this band consisted entirely of the heavy chain of muscle myosin then its amount, estimated in the above fashion, would be 2.5% of the total protein.…”

Section: Discussionmentioning

confidence: 99%

The actin content of fibroblasts

Bray¹,

Thomas²

1975

Biochemical Journal

107

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Cultures of chick skin fibroblasts were dissolved in solutions of sodium dodecyl sulphate, and their entire protein content was examined by gel electrophoresis. The most abundant species migrated in the same position as muscle actin. It gave a similar pattern of iodinated peptides after reaction with radioactive sodium iodide and digestion with proteinases, and contained comparable amounts of N-methylhistidine. Its amount was estimated by quantitative densitometry of stained gels with bovine serum albumin as an internal standard, and by radioactive assay ofcultures that had been grown in the presence of [35S]methionine. The values obtained ranged from 7 to 14% of the total cellular protein, with an average of 8.5 %. A protein band in the position of muscle myosin was also present and accounted for about 2.5 % of the total protein. Both this and the actin band increased in relative amount with the age of the cultures.

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“…Plasmid 161 does not hybridize with mRNA from stomach muscle, which contains a form of LC1 similar or identical to the nonmuscle type (32) (Fig. 3, lane j), nor with mRNA from mouse brain (not shown) nor mRNA from undifferentiated cells ofmyogenic cell lines (Fig.…”

Section: Preparationmentioning

confidence: 98%

cDNA recombinant plasmid complementary to mRNAs for light chains 1 and 3 of mouse skeletal muscle myosin.

Robert¹,

Weydert²,

Caravatti³

et al. 1982

Proc. Natl. Acad. Sci. U.S.A.

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A recombinant plasmid with a cDNA sequence transcribed from mouse skeletal muscle RNA is shown to hybridize with mRNAs for myosin light chains LC1F and LC3F. The inserted fragment corresponds exclusively to the 3'-noncoding region ofthe mRNA. It hybridizes almost exclusively with the two light chain messengers from fast skeletal muscle RNA of adult mouse. Slight hybridization is seen with RNA from heart muscle and embryonic skeletal muscle. The implications ofthe conservation ofthe 3'-noncoding regions between the two mRNAs are discussed.

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A comparison of fibroblast and smooth muscle myosins

Cited by 30 publications

References 12 publications

The myosin alkali light chain proteins and their genes

The myosin alkali light chain proteins and their genes

The actin content of fibroblasts

cDNA recombinant plasmid complementary to mRNAs for light chains 1 and 3 of mouse skeletal muscle myosin.

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