BTCI enhances guanylin-induced natriuresis and promotes renal glomerular and tubular effects
Main Author: | |
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Publication Date: | 2008 |
Other Authors: | , , , , , |
Format: | Article |
Language: | eng |
Source: | Brazilian Journal of Biology |
Download full: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1519-69842008000100021 |
Summary: | Guanylin and uroguanylin are small cysteine-rich peptides involved in the regulation of fluid and electrolyte homeostasis through binding and activation of guanylyl cyclases signaling molecules expressed in intestine and kidney. Guanylin is less potent than uroguanylin as a natriuretic agent and is degraded in vitro by chymotrypsin due to unique structural features in the bioactive moiety of the peptide. Thus, the aim of this study was to verify whether or not guanylin is degraded by chymotrypsin-like proteases present in the kidney brush-border membranes. The isolated perfused rat kidney assay was used in this regard. Guanylin (0.2 µM) induced no changes in kidney function. However, when pretreated by the black-eyed pea trypsin and chymotrypsin inhibitor (BTCI - 1.0 µM; guanylin - 0.2 µM) it promoted increases in urine flow (deltaUF of 0.25 ± 0.09 mL.g-1/min, P < 0.05) and Na+ excretion (% delta ENa+ of 18.20 ± 2.17, P < 0.05). BTCI (1.0 µM) also increased %ENa+ (from 22.8 ± 1.30 to 34.4 ± 3.48, P < 0.05, 90 minutes). Furthermore, BTCI (3.0 µM) induced increases in glomerular filtration rate (GFR; from 0.96 ± 0.02 to 1.28 0.02 mL.g-1/min, P < 0.05, 60 minutes). The present paper strongly suggests that chymotrypsin-like proteases play a role in renal metabolism of guanylin and describes for the first time renal effects induced by a member of the Bowman-Birk family of protease inhibitors. |
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BTCI enhances guanylin-induced natriuresis and promotes renal glomerular and tubular effectsnatriuresiskidneyBowman-Birk protease inhibitorsBTCIcyclic GMPVignia unguiculataGuanylin and uroguanylin are small cysteine-rich peptides involved in the regulation of fluid and electrolyte homeostasis through binding and activation of guanylyl cyclases signaling molecules expressed in intestine and kidney. Guanylin is less potent than uroguanylin as a natriuretic agent and is degraded in vitro by chymotrypsin due to unique structural features in the bioactive moiety of the peptide. Thus, the aim of this study was to verify whether or not guanylin is degraded by chymotrypsin-like proteases present in the kidney brush-border membranes. The isolated perfused rat kidney assay was used in this regard. Guanylin (0.2 µM) induced no changes in kidney function. However, when pretreated by the black-eyed pea trypsin and chymotrypsin inhibitor (BTCI - 1.0 µM; guanylin - 0.2 µM) it promoted increases in urine flow (deltaUF of 0.25 ± 0.09 mL.g-1/min, P < 0.05) and Na+ excretion (% delta ENa+ of 18.20 ± 2.17, P < 0.05). BTCI (1.0 µM) also increased %ENa+ (from 22.8 ± 1.30 to 34.4 ± 3.48, P < 0.05, 90 minutes). Furthermore, BTCI (3.0 µM) induced increases in glomerular filtration rate (GFR; from 0.96 ± 0.02 to 1.28 0.02 mL.g-1/min, P < 0.05, 60 minutes). The present paper strongly suggests that chymotrypsin-like proteases play a role in renal metabolism of guanylin and describes for the first time renal effects induced by a member of the Bowman-Birk family of protease inhibitors.Instituto Internacional de Ecologia2008-02-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1519-69842008000100021Brazilian Journal of Biology v.68 n.1 2008reponame:Brazilian Journal of Biologyinstname:Instituto Internacional de Ecologia (IIE)instacron:IIE10.1590/S1519-69842008000100021info:eu-repo/semantics/openAccessCarvalho,AF.Santos-Neto,MS.Monteiro,HSA.Freitas,SM.Morhy,L.Nascimento,NRF.Fonteles,MC.eng2008-05-05T00:00:00Zoai:scielo:S1519-69842008000100021Revistahttps://www.scielo.br/j/bjb/https://old.scielo.br/oai/scielo-oai.phpbjb@bjb.com.br||bjb@bjb.com.br1678-43751519-6984opendoar:2008-05-05T00:00Brazilian Journal of Biology - Instituto Internacional de Ecologia (IIE)false |
dc.title.none.fl_str_mv |
BTCI enhances guanylin-induced natriuresis and promotes renal glomerular and tubular effects |
title |
BTCI enhances guanylin-induced natriuresis and promotes renal glomerular and tubular effects |
spellingShingle |
BTCI enhances guanylin-induced natriuresis and promotes renal glomerular and tubular effects Carvalho,AF. natriuresis kidney Bowman-Birk protease inhibitors BTCI cyclic GMP Vignia unguiculata |
title_short |
BTCI enhances guanylin-induced natriuresis and promotes renal glomerular and tubular effects |
title_full |
BTCI enhances guanylin-induced natriuresis and promotes renal glomerular and tubular effects |
title_fullStr |
BTCI enhances guanylin-induced natriuresis and promotes renal glomerular and tubular effects |
title_full_unstemmed |
BTCI enhances guanylin-induced natriuresis and promotes renal glomerular and tubular effects |
title_sort |
BTCI enhances guanylin-induced natriuresis and promotes renal glomerular and tubular effects |
author |
Carvalho,AF. |
author_facet |
Carvalho,AF. Santos-Neto,MS. Monteiro,HSA. Freitas,SM. Morhy,L. Nascimento,NRF. Fonteles,MC. |
author_role |
author |
author2 |
Santos-Neto,MS. Monteiro,HSA. Freitas,SM. Morhy,L. Nascimento,NRF. Fonteles,MC. |
author2_role |
author author author author author author |
dc.contributor.author.fl_str_mv |
Carvalho,AF. Santos-Neto,MS. Monteiro,HSA. Freitas,SM. Morhy,L. Nascimento,NRF. Fonteles,MC. |
dc.subject.por.fl_str_mv |
natriuresis kidney Bowman-Birk protease inhibitors BTCI cyclic GMP Vignia unguiculata |
topic |
natriuresis kidney Bowman-Birk protease inhibitors BTCI cyclic GMP Vignia unguiculata |
description |
Guanylin and uroguanylin are small cysteine-rich peptides involved in the regulation of fluid and electrolyte homeostasis through binding and activation of guanylyl cyclases signaling molecules expressed in intestine and kidney. Guanylin is less potent than uroguanylin as a natriuretic agent and is degraded in vitro by chymotrypsin due to unique structural features in the bioactive moiety of the peptide. Thus, the aim of this study was to verify whether or not guanylin is degraded by chymotrypsin-like proteases present in the kidney brush-border membranes. The isolated perfused rat kidney assay was used in this regard. Guanylin (0.2 µM) induced no changes in kidney function. However, when pretreated by the black-eyed pea trypsin and chymotrypsin inhibitor (BTCI - 1.0 µM; guanylin - 0.2 µM) it promoted increases in urine flow (deltaUF of 0.25 ± 0.09 mL.g-1/min, P < 0.05) and Na+ excretion (% delta ENa+ of 18.20 ± 2.17, P < 0.05). BTCI (1.0 µM) also increased %ENa+ (from 22.8 ± 1.30 to 34.4 ± 3.48, P < 0.05, 90 minutes). Furthermore, BTCI (3.0 µM) induced increases in glomerular filtration rate (GFR; from 0.96 ± 0.02 to 1.28 0.02 mL.g-1/min, P < 0.05, 60 minutes). The present paper strongly suggests that chymotrypsin-like proteases play a role in renal metabolism of guanylin and describes for the first time renal effects induced by a member of the Bowman-Birk family of protease inhibitors. |
publishDate |
2008 |
dc.date.none.fl_str_mv |
2008-02-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1519-69842008000100021 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1519-69842008000100021 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S1519-69842008000100021 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Instituto Internacional de Ecologia |
publisher.none.fl_str_mv |
Instituto Internacional de Ecologia |
dc.source.none.fl_str_mv |
Brazilian Journal of Biology v.68 n.1 2008 reponame:Brazilian Journal of Biology instname:Instituto Internacional de Ecologia (IIE) instacron:IIE |
instname_str |
Instituto Internacional de Ecologia (IIE) |
instacron_str |
IIE |
institution |
IIE |
reponame_str |
Brazilian Journal of Biology |
collection |
Brazilian Journal of Biology |
repository.name.fl_str_mv |
Brazilian Journal of Biology - Instituto Internacional de Ecologia (IIE) |
repository.mail.fl_str_mv |
bjb@bjb.com.br||bjb@bjb.com.br |
_version_ |
1752129876793491456 |