Glomeruli isolated from human kidney split angiotensin II: further evidence that renal “aminopeptidase A” (APA) is an angiotensinase

1988 ◽  
Vol 330 (4-5) ◽  
pp. 429-430 ◽  
Author(s):  
G. Wolf ◽  
J. E. Scherberich ◽  
W. Schoeppe
Keyword(s):  
Angiotensin Ii ◽  
Human Kidney ◽  
Aminopeptidase A

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

Abstract 196: Involvement of Peroxynitrite Formation in Angiotensin II Induced Changes in Na+K+ATPase Activity in HK2 Cells

Hypertension ◽  
2012 ◽  
Vol 60 (suppl_1) ◽  
Author(s):  
Arpan K Maiti ◽  
Mohammed T Islam ◽  
Ryosuke Satou ◽  
Dewan S Majid
Keyword(s):  
Angiotensin Ii ◽  
Colorimetric Assay ◽  
Renin Angiotensin System ◽  
Human Kidney ◽  
Protective Role ◽  
Renal Tubules ◽  
Proximal Tubule Cell ◽  
Wide Range ◽  
Induced Changes ◽  
Hk2 Cells

Angiotensin II (AngII) induces both superoxide (O 2 - ) and nitric oxide (NO) generation forming peroxynitrite (ONOO - ) in biological systems. To determine the role of ONOO - in AngII induced sodium excretory responses, we examined Na + K + ATPase (NKA) activity in cultured HK2 cells (human kidney proximal tubule cell line) incubated for 30 min with a wide range (10 pM to 200 μM) of AngII concentrations (conc) in the presence or absence of a ONOO - scavenger, mercapto-ethyl-guanadine (MEG; 200μM). Post incubation HK2 cellular membrane fractions were used for measurement of NKA activity via colorimetric assay capable of detecting inorganic phosphate (Pi). Baseline value of NKA activity in these HK2 cells was measured as 10.3 ±0.7 μmoles of Pi liberated/mg protein/hr (n=12). AngII exerts dose-dependent differential effects on NKA activity. Compared to the baseline value, NKA activity was increased at lower conc (13.7±1.3% at 10 pM to 19.6±1.5% at 100nM) and decreased at higher conc (-6.0±0.8% at 1 μM to -38±2.1% at 200 μM ) without any significant effect at 500 nM conc (-1.2±0.6%) of AngII. Interestingly, MEG treatment markedly attenuated these AngII induced changes in NKA activity, both at lower conc (activity increased only to 7.8±0.67% at 10 pM and to 8.9±0.57% at 100nM; an average reduction of 33.2±2.4% in stimulatory effects) and at higher conc (activity decreased to -3.0±0.7% at 1 μM and to -20±0.57% at 200 μM; an average reduction of 54.4±4.1% in inhibitory effects). Co-incubation with O 2 - scavenger, tempol (1 mM) or NO synthase inhibitor, nitro-L-arginine methyl ester (100 μM) did not alter these AngII induced responses in HK2 cells indicating that neither O 2 - , nor NO, was directly involved in mediating these responses. AT 1 receptor (AT 1 R) blocker, losartan (10μM) treatment prevented these AngII induced changes on NKA activity confirming the involvement of AT 1 R signaling in these responses. These findings demonstrate a direct contributory role for concomitant ONOO - generation in mediating AngII induced changes in NKA activity in the proximal tubular cells. These data also suggest a reno-protective role for ONOO - in minimizing sodium retaining action of AngII by the renal tubules, particularly in the conditions associated with enhanced renin-angiotensin system.

β-Adrenergic, Angiotensin II, and Bradykinin Receptors Enhance Neurotransmission in Human Kidney

Hypertension ◽  
1995 ◽  
Vol 26 (3) ◽  
pp. 445-451 ◽  
Author(s):  
Lars C. Rump ◽  
Christine Bohmann ◽  
Ulrike Schaible ◽  
Wolfgang Schultze-Seemann ◽  
Peter J. Schollmeyer
Keyword(s):  
Angiotensin Ii ◽  
Human Kidney ◽  
Bradykinin Receptors

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

scholarly journals Determination of an Angiotensin II-regulated Proteome in Primary Human Kidney Cells by Stable Isotope Labeling of Amino Acids in Cell Culture (SILAC)

2013 ◽  
Vol 288 (34) ◽  
pp. 24834-24847 ◽  
Author(s):  
Ana Konvalinka ◽  
Joyce Zhou ◽  
Apostolos Dimitromanolakis ◽  
Andrei P. Drabovich ◽  
Fei Fang ◽  
...  
Keyword(s):  
Amino Acids ◽  
Cell Culture ◽  
Angiotensin Ii ◽  
Stable Isotope ◽  
Isotope Labeling ◽  
Human Kidney ◽  
Stable Isotope Labeling ◽  
Kidney Cells

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.

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