cDNA and deduced amino acid sequence of mouse matrix gla protein: One of five glutamic acid residues potentially modified to gla is not conserved in the mouse sequence
Autor: | Tateo Icho, Nobuo Tsuchida, Shusaku Yoshiki, Akira Yamaguchi, Tohru Ikeda |
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Rok vydání: | 2009 |
Předmět: |
Endocrinology
Diabetes and Metabolism Molecular Sequence Data Glutamic Acid Cell Line Mice Calcitriol Glutamates Complementary DNA Matrix gla protein Animals Orthopedics and Sports Medicine Amino Acid Sequence RNA Messenger Tyrosine Peptide sequence chemistry.chemical_classification Extracellular Matrix Proteins Osteoblasts Base Sequence biology cDNA library Calcium-Binding Proteins Nucleic acid sequence nutritional and metabolic diseases Glutamic acid Blotting Northern Molecular biology Amino acid chemistry Biochemistry biology.protein |
Zdroj: | Journal of Bone and Mineral Research. 6:1013-1017 |
ISSN: | 0884-0431 |
Popis: | A cDNA library was constructed using the mouse osteoblastic cell line MC3T3-E1 treated with 1 alpha,25-dihydroxyvitamin D3, based on the finding that the treatment increased ninefold the expression of 0.7 kb matrix gla protein (MGP) mRNA. cDNA clones encoding mouse MGP were isolated from the library. The nucleotide sequence showed an open reading frame of 312 nucleotides encoding 104 amino acids. Murine MGP shared 84-89% amino acid sequence homology with bovine, rat, and human MGP. However, there are five glutamic acid residues potentially modified to gamma-carboxyglutamic acid (gla) in those species; in murine MGP, lysine replaced glutamic acid 37. Also, an extra tyrosine was added at the carboxyl terminus. The significance of the substitution is discussed in relation to the gamma-carboxylation sites in MGP protein. |
Databáze: | OpenAIRE |
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