Hypotonic stimulation of the Na⁺ active transport in frog skeletal muscle: role of the cytoskeleton
- Autores
- Venosa, Roque Alberto
- Año de publicación
- 2003
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Hypotonicity produces a marked activation of the Na⁺ pump in frog sartorius muscle. The increase in net Na⁺ efflux under hypotonic conditions occurs despite the reductions in [Na⁺]i that are due to fibre swelling and Na⁺ loss. The pump density (ouabain binding) increases not only upon reduction of the medium osmotic pressure (π) from its normal value (π = 1) to one-half (π = 0.5), but also in muscles that are returned to π = 1 after equilibration in π = 2 medium. The equilibration in π = 2 medium does not affect pump density. Ouabain-binding increments cannot be ascribed to a rise in the Na⁺–K⁺ exchange rate of a fixed number of pumps: they also occurred in the continued presence of a saturating concentration of ouabain (50 μM). Under those conditions, the π = 1 → π = 0.5 transfer produced a 43 % increase in pump sites, while the π = 2 → π = 1 transfer induced a rise of 46 %. Actinomycin D did not alter the stimulation of Na⁺ extrusion elicited by hypotonicity, suggesting that de novo synthesis of pumps was not involved in the increase of the apparent number of pump sites. Disruption of microtubules by colchicine (100 μM) and intermediate filaments by acrylamide (4 mM) did not alter the hypotonic effect. Likewise, genistein (100 μM), a specific inhibitor of tyrosine kinase, did not affect significantly the hypotonic response. Microfilament-disrupting agents like cytochalasin B (5 μM) and latrunculin B (10 μM) reduced the increase in Na⁺ efflux induced by π = 1 → π = 0.5 transfer by about 35 % and 72 %, respectively. Latrunculin B reduced the increases in pump density generated by π = 1 → π = 0.5 and π = 2 → π = 1 transfers by about 79 % and 91 %, respectively. The results suggest that the membrane stretch due to hypotonic fibre volume increase would promote a microfilament-mediated insertion of submembranous spare Na⁺ pumps in the sarcolemma and, consequently, the rise in active Na⁺ transport.
Facultad de Ciencias Médicas
Centro de Investigaciones Cardiovasculares - Materia
-
Medicina
hypotonicity
frog
sartorius muscle
Na⁺ active transport
cytoskeleton - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by-nc-sa/4.0/
- Repositorio
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/127112
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Hypotonic stimulation of the Na⁺ active transport in frog skeletal muscle: role of the cytoskeletonVenosa, Roque AlbertoMedicinahypotonicityfrogsartorius muscleNa⁺ active transportcytoskeletonHypotonicity produces a marked activation of the Na⁺ pump in frog sartorius muscle. The increase in net Na⁺ efflux under hypotonic conditions occurs despite the reductions in [Na⁺]<sub>i</sub> that are due to fibre swelling and Na⁺ loss. The pump density (ouabain binding) increases not only upon reduction of the medium osmotic pressure (π) from its normal value (π = 1) to one-half (π = 0.5), but also in muscles that are returned to π = 1 after equilibration in π = 2 medium. The equilibration in π = 2 medium does not affect pump density. Ouabain-binding increments cannot be ascribed to a rise in the Na⁺–K⁺ exchange rate of a fixed number of pumps: they also occurred in the continued presence of a saturating concentration of ouabain (50 μM). Under those conditions, the π = 1 → π = 0.5 transfer produced a 43 % increase in pump sites, while the π = 2 → π = 1 transfer induced a rise of 46 %. Actinomycin D did not alter the stimulation of Na⁺ extrusion elicited by hypotonicity, suggesting that <i>de novo</i> synthesis of pumps was not involved in the increase of the apparent number of pump sites. Disruption of microtubules by colchicine (100 μM) and intermediate filaments by acrylamide (4 mM) did not alter the hypotonic effect. Likewise, genistein (100 μM), a specific inhibitor of tyrosine kinase, did not affect significantly the hypotonic response. Microfilament-disrupting agents like cytochalasin B (5 μM) and latrunculin B (10 μM) reduced the increase in Na⁺ efflux induced by π = 1 → π = 0.5 transfer by about 35 % and 72 %, respectively. Latrunculin B reduced the increases in pump density generated by π = 1 → π = 0.5 and π = 2 → π = 1 transfers by about 79 % and 91 %, respectively. The results suggest that the membrane stretch due to hypotonic fibre volume increase would promote a microfilament-mediated insertion of submembranous spare Na⁺ pumps in the sarcolemma and, consequently, the rise in active Na⁺ transport.Facultad de Ciencias MédicasCentro de Investigaciones Cardiovasculares2003-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf451-459http://sedici.unlp.edu.ar/handle/10915/127112enginfo:eu-repo/semantics/altIdentifier/url/https://physoc.onlinelibrary.wiley.com/doi/10.1111/j.1469-7793.2003.00451.xinfo:eu-repo/semantics/altIdentifier/issn/0022-3751info:eu-repo/semantics/altIdentifier/issn/1469-7793info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:30:42Zoai:sedici.unlp.edu.ar:10915/127112Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:30:43.16SEDICI (UNLP) - Universidad Nacional de La Platafalse |
dc.title.none.fl_str_mv |
Hypotonic stimulation of the Na⁺ active transport in frog skeletal muscle: role of the cytoskeleton |
title |
Hypotonic stimulation of the Na⁺ active transport in frog skeletal muscle: role of the cytoskeleton |
spellingShingle |
Hypotonic stimulation of the Na⁺ active transport in frog skeletal muscle: role of the cytoskeleton Venosa, Roque Alberto Medicina hypotonicity frog sartorius muscle Na⁺ active transport cytoskeleton |
title_short |
Hypotonic stimulation of the Na⁺ active transport in frog skeletal muscle: role of the cytoskeleton |
title_full |
Hypotonic stimulation of the Na⁺ active transport in frog skeletal muscle: role of the cytoskeleton |
title_fullStr |
Hypotonic stimulation of the Na⁺ active transport in frog skeletal muscle: role of the cytoskeleton |
title_full_unstemmed |
Hypotonic stimulation of the Na⁺ active transport in frog skeletal muscle: role of the cytoskeleton |
title_sort |
Hypotonic stimulation of the Na⁺ active transport in frog skeletal muscle: role of the cytoskeleton |
dc.creator.none.fl_str_mv |
Venosa, Roque Alberto |
author |
Venosa, Roque Alberto |
author_facet |
Venosa, Roque Alberto |
author_role |
author |
dc.subject.none.fl_str_mv |
Medicina hypotonicity frog sartorius muscle Na⁺ active transport cytoskeleton |
topic |
Medicina hypotonicity frog sartorius muscle Na⁺ active transport cytoskeleton |
dc.description.none.fl_txt_mv |
Hypotonicity produces a marked activation of the Na⁺ pump in frog sartorius muscle. The increase in net Na⁺ efflux under hypotonic conditions occurs despite the reductions in [Na⁺]<sub>i</sub> that are due to fibre swelling and Na⁺ loss. The pump density (ouabain binding) increases not only upon reduction of the medium osmotic pressure (π) from its normal value (π = 1) to one-half (π = 0.5), but also in muscles that are returned to π = 1 after equilibration in π = 2 medium. The equilibration in π = 2 medium does not affect pump density. Ouabain-binding increments cannot be ascribed to a rise in the Na⁺–K⁺ exchange rate of a fixed number of pumps: they also occurred in the continued presence of a saturating concentration of ouabain (50 μM). Under those conditions, the π = 1 → π = 0.5 transfer produced a 43 % increase in pump sites, while the π = 2 → π = 1 transfer induced a rise of 46 %. Actinomycin D did not alter the stimulation of Na⁺ extrusion elicited by hypotonicity, suggesting that <i>de novo</i> synthesis of pumps was not involved in the increase of the apparent number of pump sites. Disruption of microtubules by colchicine (100 μM) and intermediate filaments by acrylamide (4 mM) did not alter the hypotonic effect. Likewise, genistein (100 μM), a specific inhibitor of tyrosine kinase, did not affect significantly the hypotonic response. Microfilament-disrupting agents like cytochalasin B (5 μM) and latrunculin B (10 μM) reduced the increase in Na⁺ efflux induced by π = 1 → π = 0.5 transfer by about 35 % and 72 %, respectively. Latrunculin B reduced the increases in pump density generated by π = 1 → π = 0.5 and π = 2 → π = 1 transfers by about 79 % and 91 %, respectively. The results suggest that the membrane stretch due to hypotonic fibre volume increase would promote a microfilament-mediated insertion of submembranous spare Na⁺ pumps in the sarcolemma and, consequently, the rise in active Na⁺ transport. Facultad de Ciencias Médicas Centro de Investigaciones Cardiovasculares |
description |
Hypotonicity produces a marked activation of the Na⁺ pump in frog sartorius muscle. The increase in net Na⁺ efflux under hypotonic conditions occurs despite the reductions in [Na⁺]<sub>i</sub> that are due to fibre swelling and Na⁺ loss. The pump density (ouabain binding) increases not only upon reduction of the medium osmotic pressure (π) from its normal value (π = 1) to one-half (π = 0.5), but also in muscles that are returned to π = 1 after equilibration in π = 2 medium. The equilibration in π = 2 medium does not affect pump density. Ouabain-binding increments cannot be ascribed to a rise in the Na⁺–K⁺ exchange rate of a fixed number of pumps: they also occurred in the continued presence of a saturating concentration of ouabain (50 μM). Under those conditions, the π = 1 → π = 0.5 transfer produced a 43 % increase in pump sites, while the π = 2 → π = 1 transfer induced a rise of 46 %. Actinomycin D did not alter the stimulation of Na⁺ extrusion elicited by hypotonicity, suggesting that <i>de novo</i> synthesis of pumps was not involved in the increase of the apparent number of pump sites. Disruption of microtubules by colchicine (100 μM) and intermediate filaments by acrylamide (4 mM) did not alter the hypotonic effect. Likewise, genistein (100 μM), a specific inhibitor of tyrosine kinase, did not affect significantly the hypotonic response. Microfilament-disrupting agents like cytochalasin B (5 μM) and latrunculin B (10 μM) reduced the increase in Na⁺ efflux induced by π = 1 → π = 0.5 transfer by about 35 % and 72 %, respectively. Latrunculin B reduced the increases in pump density generated by π = 1 → π = 0.5 and π = 2 → π = 1 transfers by about 79 % and 91 %, respectively. The results suggest that the membrane stretch due to hypotonic fibre volume increase would promote a microfilament-mediated insertion of submembranous spare Na⁺ pumps in the sarcolemma and, consequently, the rise in active Na⁺ transport. |
publishDate |
2003 |
dc.date.none.fl_str_mv |
2003-04 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Articulo http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://sedici.unlp.edu.ar/handle/10915/127112 |
url |
http://sedici.unlp.edu.ar/handle/10915/127112 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://physoc.onlinelibrary.wiley.com/doi/10.1111/j.1469-7793.2003.00451.x info:eu-repo/semantics/altIdentifier/issn/0022-3751 info:eu-repo/semantics/altIdentifier/issn/1469-7793 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) |
dc.format.none.fl_str_mv |
application/pdf 451-459 |
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