REGULATION OF RAT AMP DEAMINASE 3 (ISOFORM C) BY DEVELOPMENT AND SKELETAL MUSCLE FIBRE TYPE

作者: Donna K. MAHNKE-ZIZELMAN , Jonathan D'CUNHA , Jean M. WOJNAR , Michele A. BROGLEY , Richard L. SABINA

DOI: 10.1042/BJ3260521

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摘要: AMP deaminase (AMPD) is characterized by a multigene family in rodents and man. Highly conserved rat human AMPD1 AMPD2 genes produce protein products that exhibit cross-species immunoreactivities (AMPD1, isoform A M; AMPD2, B L). third gene, AMPD3, has been described humans, but antisera raised against its purified product (isoform E) reportedly does not cross-react with activity from tissues C). This study was designed to address this latter issue cloning, sequencing expressing AMPD3 cDNA species. Similarly the gene produces multiple transcripts differ at or near their 5' ends. The boundary which these alternative sequences diverge precisely both Across region common all species, nucleotide predicted amino acid are 89% 93% identical respectively, although open reading frame lacking two separate in-frame codons end. Extreme regions between species entirely divergent, one sequence confer least 36 additional N-terminal residues encoded polypeptide. comparison of 3' untranslated indicates 250 bp longer contains consensus polyadenylation signals. Examination relative expression shows (1) variable patterns mRNA abundance across adult tissues, (2) developmental regulation skeletal muscle liver, (3) greater red (soleus) than mixed (plantaris) white (outer gastrocnemius) muscle. Finally, baculoviral proteins enzymes chromatographically kinetically similar. Moreover, recombinant activities immunoreact anti-C anti-E serum. These combined results demonstrate C E homologous proteins.

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