Placental Aminopeptidase A as a Possible Barrier of Angiotensin II between Mother and Fetus

Placenta ◽  
2000 ◽  
Vol 21 (7) ◽  
pp. 621-627 ◽  
Author(s):  
Y. Hariyama ◽  
A. Itakura ◽  
M. Okamura ◽  
M. Ito ◽  
Y. Murata ◽  
...  
Keyword(s):  
Angiotensin Ii ◽  
Aminopeptidase A

scholarly journals Hypertension and Angiotensin II Hypersensitivity in Aminopeptidase A—deficient Mice

2003 ◽  
Vol 9 (1-2) ◽  
pp. 57-62 ◽  
Author(s):  
Takashi Mitsui ◽  
Seiji Nomura ◽  
Mayumi Okada ◽  
Yasumasa Ohno ◽  
Honami Kobayashi ◽  
...  
Keyword(s):  
Angiotensin Ii ◽  
Aminopeptidase A ◽  
Deficient Mice

Purification of aminopeptidase a in human serum and degradation of angiotensin II by the purified enzyme

1970 ◽  
Vol 198 (2) ◽  
pp. 255-270 ◽  
Author(s):  
Ikuko Nagatsu ◽  
Toshiharu Nagatsu ◽  
Tomiko Yamamoto ◽  
George G. Glenner ◽  
John W. Mehl
Keyword(s):  
Angiotensin Ii ◽  
Human Serum ◽  
Aminopeptidase A

Rat kidney glutamyl aminopeptidase (aminopeptidase A): molecular identity and cellular localization

1994 ◽  
Vol 267 (4) ◽  
pp. F546-F557 ◽  
Author(s):  
L. Song ◽  
M. Ye ◽  
M. Troyanovskaya ◽  
E. Wilk ◽  
S. Wilk ◽  
...  
Keyword(s):  
Amino Acid ◽  
Angiotensin Ii ◽  
Cellular Localization ◽  
Mesangial Cells ◽  
Rat Kidney ◽  
Blot Hybridization ◽  
Northern Blot Hybridization ◽  
Glomerular Mesangial Cells ◽  
Partial Cdna ◽  
Aminopeptidase A

Glutamyl aminopeptidase [aminopeptidase A (EAP), EC 3.4.11.7] is an ectoenzyme that selectively hydrolyzes acidic amino acid residues from the amino terminus of oligopeptides. EAP activity is highest within the kidney and small intestine. The murine pre-B cell BP-1/6C3 and the human kidney glycoprotein gp160 differentiation antigens have been reported to have biochemical properties indistinguishable from EAP. It is not known, however, if rat kidney EAP is a homologue of these antigens or molecularly distinct. Using the reverse transcription-polymerase chain reaction method with oligonucleotide primers based on the BP-1/6C3 nucleotide sequence, we isolated a 450-bp partial cDNA from rat kidney poly(A)+ RNA. The partial cDNA encoded a predicted protein that was 92% and 86% identical to the murine BP-1/6C3 and human gp160 antigens, respectively; the amino acid sequence within the zinc-binding domain was completely conserved. Purification of EAP from rat kidney and microsequence analysis of a tryptic digest peptide fragment (18-mer) indicated that the fragment was highly similar to a region within the BP-1/6C3 and gp160 proteins. Northern blot hybridization and immunoblot analyses were also consistent with labeling of products the same size as reported for the BP-1/6C3 and gp160 antigens. There was a good correlation between the cellular distribution of EAP mRNA and EAP immunoreactivity, with proximal tubules and glomerular mesangial cells having the highest densities. These results indicate that rat kidney EAP is a species homologue of the murine BP-1/6C3 and human gp160 antigens. Furthermore, on the basis of its cellular localization, rat kidney EAP is likely to be involved in degradation of oligopeptides within the glomerulus and the glomerular filtrate. Since cells that express EAP also express receptors for angiotensin II, an intrarenal vasoactive hormone that is a substrate for EAP, these results further suggest that EAP may play a role in modulating the activity of intrarenal angiotensin II.

Inhibition of aminopeptidase A activity causes an acute albuminuria in mice: an angiotensin II-mediated effect?

1996 ◽  
Vol 11 (11) ◽  
pp. 2163-2169 ◽  
Author(s):  
S. Mentzel ◽  
K. J. M. Assmann ◽  
H. B. P. M. Dijkman ◽  
A. S. de Jong ◽  
J. P. H. F. van Son ◽  
...  
Keyword(s):  
Angiotensin Ii ◽  
Aminopeptidase A
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