| Human brain glycogen phosphorylase. Cloning, sequence analysis, chromosomal mapping, tissue expression, and comparison with the human liver and muscle isozymes. | |
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MedLine Citation:
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PMID: 3346228 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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We have cloned the cDNA encoding a new isozyme of glycogen phosphorylase (1,4-D-glucan:orthosphosphate D-glucosyltransferase, EC 2.4.1.1) from a cDNA library prepared from a human brain astrocytoma cell line. Blot-hybridization analysis reveals that this message is preferentially expressed in human brain, but is also found at a low level in human fetal liver and adult liver and muscle tissues. Although previous studies have suggested that the major isozyme of phosphorylase found in all fetal tissues is the brain type, our data show that the predominant mRNA in fetal liver (24-week gestation) is the adult liver form. The protein sequence deduced from the nucleotide sequence of the brain phosphorylase cDNA is 862 amino acids long compared with 846 and 841 amino acids for the liver and muscle isozymes, respectively; the greater length of brain phosphorylase is entirely due to an extension at the far C-terminal portion of the protein. The muscle and brain isozymes share greater identity with regard to nucleotide and deduced amino acid sequences, codon usage, and nucleotide composition than either do with the liver sequence, suggesting a closer evolutionary relationship between them. Spot blot hybridization of the brain phosphorylase cDNA to laser-sorted human chromosome fractions, and Southern blot analysis of hamster/human hybrid cell line DNA reveals that the exact homolog of the newly cloned cDNA maps to chromosome 20, but that a slightly less homologous gene is found on chromosome 10 as well. The liver and muscle genes have previously been localized to chromosomes 14 and 11, respectively. This suggests that the phosphorylase genes evolved by duplication and translocation of a common ancestral gene, leading to divergence of elements controlling gene expression and of structural features of the phosphorylase proteins that confer tissue-specific functional properties. |
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Authors:
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C B Newgard; D R Littman; C van Genderen; M Smith; R J Fletterick |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 263 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 1988 Mar |
Date Detail:
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Created Date: 1988-04-14 Completed Date: 1988-04-14 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 3850-7 Citation Subset: IM |
Affiliation:
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Department of Biochemistry, University of California, San Francisco 94143. |
| Data Bank Information | |
Bank Name/Acc. No.:
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GENBANK/J03544 |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Astrocytoma / genetics Base Sequence Brain / enzymology* Brain Neoplasms / genetics Cell Line Chromosome Mapping Chromosomes, Human, Pair 10* Chromosomes, Human, Pair 20* Cloning, Molecular Humans Isoenzymes / genetics* Liver / enzymology* Molecular Sequence Data Muscles / enzymology* Organ Specificity Phosphorylases / genetics* Transcription, Genetic* |
| Grant Support | |
ID/Acronym/Agency:
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AI 23513/AI/NIAID NIH HHS; AM 32822/AM/NIADDK NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Isoenzymes; EC 2.4.1.-/Phosphorylases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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