Molecular cloning and expression of aminopeptidase A isoforms from rat hippocampus

The full-length cDNA encoding aminopeptidase A (APAL) was cloned from a rat hippocampus cDNA library. A short variant aminopeptidase A (APAS), produced by deletion, was also cloned. In the case of APAL, the longest open reading frame encodes 945 amino acid residues with a calculated molecular mass o...

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Bibliographic Details
Published in:Biochimica et biophysica acta 2000-09, Vol.1493 (1), p.273-278
Main Authors: Lee, Hahn-Jun, Tomioka, Masanori, Takaki, Yoshie, Masumoto, Hajime, Saido, Takaomi C
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Aminopeptidase A
Aminopeptidases - biosynthesis
Aminopeptidases - genetics
Animals
Base Sequence
Brain Chemistry
cDNA
Cloning
Cloning, Molecular
COS Cells
DNA, Complementary - biosynthesis
Gene Expression
Gene Library
Glutamyl Aminopeptidase
Hippocampus
Hippocampus - enzymology
Isoenzymes - biosynthesis
Isoenzymes - genetics
Molecular Sequence Data
Rat
Rats
Reverse Transcriptase Polymerase Chain Reaction
Sequence Alignment
Transfection
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Summary:The full-length cDNA encoding aminopeptidase A (APAL) was cloned from a rat hippocampus cDNA library. A short variant aminopeptidase A (APAS), produced by deletion, was also cloned. In the case of APAL, the longest open reading frame encodes 945 amino acid residues with a calculated molecular mass of 108 kDa, and the deduced amino acid sequence shows 76, 86 and 78% identity with its human, murine and porcine counterparts, respectively. Rat aminopeptidase A mRNAs were detected in the kidney, liver, heart and brain by Northern blot analysis. When overexpressed in COS-1 cells, APAL shows apparent aminopeptidase A activity, whereas APAS does not.
ISSN:0167-4781
0006-3002
1879-2634
DOI:10.1016/S0167-4781(00)00183-4