Abstract
We looked for the presence of prorenin in erythrocytes from normal subjects (n = 8), hypertensive patients (n = 8), and pregnant women (n = 8). Angiotensin I generation was measured at 37°C, pH 5.7, in the presence of homologous substrate (1400 ng/mL) before and after trypsin activation (100 χ/mL) in (A) haemolyzed erythrocytes, (B) supernatants of haemolyzed erythrocytes, and (C) in the sixth washing of erythrocytes diluted 1:1 with a 0.1 M Tris buffer containing 0.5% bovine serum albumin and protease inhibitors. Haemolyzed erythrocytes generated angiotensin I only after trypsin treatment, and the rate of generation was the same (A) before and (B) after centrifugation at 20,000g, indicating the absence of prorenin bound to the cell membranes. When aliquots of the last washing of erythrocytes (C) were tested for angiotensin I generation before and after trypsin, they did not generate angiotensin I, indicating that residual prorenin from the plasma was no longer present in our preparation. Angiotensin I generation by trypsin-treated A and B was completely abolished by preincubation with anti-renin serum. The level of prorenin was not significantly different in the erythrocytes from normal, hypertensive, and pregnant subjects (68 ± 10, 58 ± 7 and 107 ± 17 pg angiotensin I · mL-1 · h-1, ns) in spite of their very different plasma levels (21 ± 2.5, 17 ± 2.4 and 110 ± 12 ng angiotensin I · mL-1 · h-1, p <0.01 for pregnant women compared with both normal and hypertensive subjects). Our data show that prorenin is present in human erythrocytes in fairly constant and clearly detectable amounts, thus suggesting a possible intracellular role for it.
| Original language | English |
|---|---|
| Pages (from-to) | 1394-1397 |
| Number of pages | 4 |
| Journal | Canadian Journal of Physiology and Pharmacology |
| Volume | 69 |
| Issue number | 9 |
| Publication status | Published - 1991 |
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Keywords
- Erythrocytes
- Inactive renin
- Intracellular prorenin
- Prorenin
ASJC Scopus subject areas
- Physiology
- Pharmacology
Cite this
Prorenin is present in human red blood cells. / Troffa, C.; Tonolo, G.; Manunta, P.; Pazzola, A.; Soro, A.; Madeddu, P.; Pala, F.; Melis, M. G.; PinnaParpaglia, P.; Patteri, G.; Bacciu, S.; Sabino, G.; Glorioso, N.
In: Canadian Journal of Physiology and Pharmacology, Vol. 69, No. 9, 1991, p. 1394-1397.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Prorenin is present in human red blood cells
AU - Troffa, C.
AU - Tonolo, G.
AU - Manunta, P.
AU - Pazzola, A.
AU - Soro, A.
AU - Madeddu, P.
AU - Pala, F.
AU - Melis, M. G.
AU - PinnaParpaglia, P.
AU - Patteri, G.
AU - Bacciu, S.
AU - Sabino, G.
AU - Glorioso, N.
PY - 1991
Y1 - 1991
N2 - We looked for the presence of prorenin in erythrocytes from normal subjects (n = 8), hypertensive patients (n = 8), and pregnant women (n = 8). Angiotensin I generation was measured at 37°C, pH 5.7, in the presence of homologous substrate (1400 ng/mL) before and after trypsin activation (100 χ/mL) in (A) haemolyzed erythrocytes, (B) supernatants of haemolyzed erythrocytes, and (C) in the sixth washing of erythrocytes diluted 1:1 with a 0.1 M Tris buffer containing 0.5% bovine serum albumin and protease inhibitors. Haemolyzed erythrocytes generated angiotensin I only after trypsin treatment, and the rate of generation was the same (A) before and (B) after centrifugation at 20,000g, indicating the absence of prorenin bound to the cell membranes. When aliquots of the last washing of erythrocytes (C) were tested for angiotensin I generation before and after trypsin, they did not generate angiotensin I, indicating that residual prorenin from the plasma was no longer present in our preparation. Angiotensin I generation by trypsin-treated A and B was completely abolished by preincubation with anti-renin serum. The level of prorenin was not significantly different in the erythrocytes from normal, hypertensive, and pregnant subjects (68 ± 10, 58 ± 7 and 107 ± 17 pg angiotensin I · mL-1 · h-1, ns) in spite of their very different plasma levels (21 ± 2.5, 17 ± 2.4 and 110 ± 12 ng angiotensin I · mL-1 · h-1, p <0.01 for pregnant women compared with both normal and hypertensive subjects). Our data show that prorenin is present in human erythrocytes in fairly constant and clearly detectable amounts, thus suggesting a possible intracellular role for it.
AB - We looked for the presence of prorenin in erythrocytes from normal subjects (n = 8), hypertensive patients (n = 8), and pregnant women (n = 8). Angiotensin I generation was measured at 37°C, pH 5.7, in the presence of homologous substrate (1400 ng/mL) before and after trypsin activation (100 χ/mL) in (A) haemolyzed erythrocytes, (B) supernatants of haemolyzed erythrocytes, and (C) in the sixth washing of erythrocytes diluted 1:1 with a 0.1 M Tris buffer containing 0.5% bovine serum albumin and protease inhibitors. Haemolyzed erythrocytes generated angiotensin I only after trypsin treatment, and the rate of generation was the same (A) before and (B) after centrifugation at 20,000g, indicating the absence of prorenin bound to the cell membranes. When aliquots of the last washing of erythrocytes (C) were tested for angiotensin I generation before and after trypsin, they did not generate angiotensin I, indicating that residual prorenin from the plasma was no longer present in our preparation. Angiotensin I generation by trypsin-treated A and B was completely abolished by preincubation with anti-renin serum. The level of prorenin was not significantly different in the erythrocytes from normal, hypertensive, and pregnant subjects (68 ± 10, 58 ± 7 and 107 ± 17 pg angiotensin I · mL-1 · h-1, ns) in spite of their very different plasma levels (21 ± 2.5, 17 ± 2.4 and 110 ± 12 ng angiotensin I · mL-1 · h-1, p <0.01 for pregnant women compared with both normal and hypertensive subjects). Our data show that prorenin is present in human erythrocytes in fairly constant and clearly detectable amounts, thus suggesting a possible intracellular role for it.
KW - Erythrocytes
KW - Inactive renin
KW - Intracellular prorenin
KW - Prorenin
UR - http://www.scopus.com/inward/record.url?scp=0025718480&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025718480&partnerID=8YFLogxK
M3 - Article
C2 - 1756445
AN - SCOPUS:0025718480
VL - 69
SP - 1394
EP - 1397
JO - Canadian Journal of Physiology and Pharmacology
JF - Canadian Journal of Physiology and Pharmacology
SN - 0008-4212
IS - 9
ER -