A renin-like enzyme in luteal tissue

R. R. Cabrera; D. C. Guardia; E. De Vito

doi:10.1016/0303-7207(86)90120-6

A renin-like enzyme in luteal tissue

R. R. Cabrera, D. C. Guardia, E. De Vito

Research output: Contribution to journal › Article › peer-review

14 Scopus citations

Abstract

The aim of this study was to identify immunologically and biologically a renin-like enzyme (RLE) in rat corpora lutea (CL). The biological activity of partially purified extracts of CL was tested in vivo by injection into anesthetized pentolinium-treated rats, obtaining a pressor response similar to renal renin. The enzyme activity in vitro was inhibited to about 50% by pretreatment with a specific antibody against renal renin. When the extracts were incubated with angiotensinogen, the product was inhibited mainly by angiotensin I antibody. The fact that there was no change in RLE content in 24 or 48 h nephrectomized rats, suggested the idea of a local production rather than an active blood renin sequestration.

Original language	English (US)
Pages (from-to)	269-273
Number of pages	5
Journal	Molecular and Cellular Endocrinology
Volume	47
Issue number	3
DOIs	https://doi.org/10.1016/0303-7207(86)90120-6
State	Published - Oct 1986
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology
Endocrinology

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10.1016/0303-7207(86)90120-6

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title = "A renin-like enzyme in luteal tissue",

abstract = "The aim of this study was to identify immunologically and biologically a renin-like enzyme (RLE) in rat corpora lutea (CL). The biological activity of partially purified extracts of CL was tested in vivo by injection into anesthetized pentolinium-treated rats, obtaining a pressor response similar to renal renin. The enzyme activity in vitro was inhibited to about 50% by pretreatment with a specific antibody against renal renin. When the extracts were incubated with angiotensinogen, the product was inhibited mainly by angiotensin I antibody. The fact that there was no change in RLE content in 24 or 48 h nephrectomized rats, suggested the idea of a local production rather than an active blood renin sequestration.",

author = "Cabrera, {R. R.} and Guardia, {D. C.} and {De Vito}, E.",

note = "Funding Information: This work was supported by a grant from the BID-CONICET Program.",

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doi = "10.1016/0303-7207(86)90120-6",

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T1 - A renin-like enzyme in luteal tissue

AU - Cabrera, R. R.

AU - Guardia, D. C.

AU - De Vito, E.

N1 - Funding Information: This work was supported by a grant from the BID-CONICET Program.

PY - 1986/10

Y1 - 1986/10

N2 - The aim of this study was to identify immunologically and biologically a renin-like enzyme (RLE) in rat corpora lutea (CL). The biological activity of partially purified extracts of CL was tested in vivo by injection into anesthetized pentolinium-treated rats, obtaining a pressor response similar to renal renin. The enzyme activity in vitro was inhibited to about 50% by pretreatment with a specific antibody against renal renin. When the extracts were incubated with angiotensinogen, the product was inhibited mainly by angiotensin I antibody. The fact that there was no change in RLE content in 24 or 48 h nephrectomized rats, suggested the idea of a local production rather than an active blood renin sequestration.

AB - The aim of this study was to identify immunologically and biologically a renin-like enzyme (RLE) in rat corpora lutea (CL). The biological activity of partially purified extracts of CL was tested in vivo by injection into anesthetized pentolinium-treated rats, obtaining a pressor response similar to renal renin. The enzyme activity in vitro was inhibited to about 50% by pretreatment with a specific antibody against renal renin. When the extracts were incubated with angiotensinogen, the product was inhibited mainly by angiotensin I antibody. The fact that there was no change in RLE content in 24 or 48 h nephrectomized rats, suggested the idea of a local production rather than an active blood renin sequestration.

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A renin-like enzyme in luteal tissue

Abstract

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