Cloning and tissue distribution of human membrane-bound aminopeptidase P.
Complementary DNA clones encoding human membrane-bound aminopeptidase P (AmP) were isolated by reverse transcription-polymerase chain reaction (RT-PCR) of human kidney and lung poly (A)+ RNA. Comparison of the human AmP sequence to that of the pig shows significant evolutionary divergence with only 83% amino acid sequence identity between the two species. Northern hybridization analysis and RT-PCR suggests that the soluble and membrane-bound forms of human AmP are products of two distinct genes or, through alternative splicing, have different C-terminal sequences.
Venema
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RC
Vascular Biology Center, Medical College of Georgia, Augusta 30912-2500, USA.
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Zou
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Venema
V J
VJ
Ryan
J W
JW
D017398:Alternative Splicing; D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000235:genetics* / Q000378:metabolism; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary; D006801:Humans; D007668:Kidney / Q000201:enzymology; D008168:Lung / Q000201:enzymology; D008565:Membrane Proteins / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D012333:RNA, Messenger / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D013552:Swine
D018076:DNA, Complementary; D008565:Membrane Proteins; D012333:RNA, Messenger; D000626:Aminopeptidases; C022750:X-Pro aminopeptidase