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Striated muscle preferentially expressed genes alpha and beta are two serine/threonine protein kinases derived from the same gene as the aortic preferentially expressed gene-1.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 2000 Nov 24; Vol. 275 (47), pp. 36966-73. - Publication Year :
- 2000
-
Abstract
- Aortic preferentially expressed gene (APEG)-1 is a 1.4-kilobase pair (kb) mRNA expressed in vascular smooth muscle cells and is down-regulated by vascular injury. An APEG-1 5'-end cDNA probe identified three additional isoforms. The 9-kb striated preferentially expressed gene (SPEG)alpha and the 11-kb SPEGbeta were found in skeletal muscle and heart. The 4-kb brain preferentially expressed gene was detected in the brain and aorta. We report here cloning of the 11-kb SPEGbeta cDNA. SPEGbeta encodes a 355-kDa protein that contains two serine/threonine kinase domains and is homologous to proteins of the myosin light chain kinase family. At least one kinase domain is active and capable of autophosphorylation. In the genome, all four isoforms share the middle three of the five exons of APEG-1, and they differ from each other by using different 5'- and 3'-ends and alternative splicing. We show that the expression of SPEGalpha and SPEGbeta is developmentally regulated in the striated muscle during C2C12 myoblast to myotube differentiation in vitro and cardiomyocyte maturation in vivo. This developmental regulation suggests that both SPEGalpha and SPEGbeta can serve as sensitive markers for striated muscle differentiation and that they may be important for adult striated muscle function.
- Subjects :
- Amino Acid Sequence
Animals
Base Sequence
Biomarkers
Cells, Cultured
Cloning, Molecular
Down-Regulation
Male
Mice
Molecular Sequence Data
Molecular Weight
Muscle, Smooth, Vascular enzymology
Myocardium enzymology
Myosin-Light-Chain Kinase chemistry
Protein Serine-Threonine Kinases
Rats
Rats, Sprague-Dawley
Sequence Alignment
Muscle Proteins genetics
Muscle, Skeletal enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 275
- Issue :
- 47
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 10973969
- Full Text :
- https://doi.org/10.1074/jbc.M006028200