Role of transforming growth factor β1 as modulator of endothelial L-Arginine/ nitric oxide signalling pathway

Autores
Vásquez, Rodrigo; Sobrevia, Luis
Año de publicación
2006
Idioma
inglés
Tipo de recurso
reseña artículo
Estado
versión publicada
Descripción
TGF-β is one of the members of the TGF-β superfamily of growth factors, including activins/inhibins and bone morphogenic proteins (BMP). At least three TGF-β isoforms have been reported in mammals: TGF-β1, TGF-β2 and TGF-β3. Virtually all human cells produce TGF-β and express its plasma membrane receptors. Each isoform is coded by a different gene, in a tissue-specific and developmental-regulated manner. TGF-β1 mRNA is expressed in endothelial, haematopoietic and connective-tissue cells, TGF-β2 mRNA is expressed in epithelial and neuronal cells, and TGF-β3 mRNA in mesenchymal cells (1,3,25). The sequence homology is 70-80% between TGF-β isoforms and 30-40% with activins/inhibins and BMP. TGF-β1, 2 and 3 are highly conserved in mammals suggesting a critical biological function for each of these isoforms, acting as strong mediators of tissue repair through chemotaxis and angiogenesis stimulation and extracellular matrix generation (1,3,25). TGF-β1 is a 112 amino acid polypeptide which forms a homodimer with both subunits linked with a disulfide bond. TGF-β1 is synthesized as a precursor of 391 amino acids whose amino acid sequence includes TGF-β1 and the propeptide latencyassociated peptide (LAP) in the amino terminal. TGF-β1 is cleaved from LAP before the precursor is secreted from the cells, but it continues non-covalently bond to this propeptide. After being secreted, TGF-β1 is stored at the extracellular matrix as a complex formed between TGF-β1, LAP and the latent TGF-b binding protein (LTBP). The relation between TGF-β1 and LTBP through disulfide bond prevents the binding of TGF-β1 to its receptors. In vivo, TGF-β1 is released from the complex by the matrix glycoprotein thrombospondin 1 (TSP-1), which changes the conformation of LTBP (1,25).
Sociedad Argentina de Fisiología
Materia
Ciencias Médicas
Fisiología
TGF-β
Growth factors
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/146981

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spelling Role of transforming growth factor β1 as modulator of endothelial L-Arginine/ nitric oxide signalling pathwayVásquez, RodrigoSobrevia, LuisCiencias MédicasFisiologíaTGF-βGrowth factorsTGF-β is one of the members of the TGF-β superfamily of growth factors, including activins/inhibins and bone morphogenic proteins (BMP). At least three TGF-β isoforms have been reported in mammals: TGF-β1, TGF-β2 and TGF-β3. Virtually all human cells produce TGF-β and express its plasma membrane receptors. Each isoform is coded by a different gene, in a tissue-specific and developmental-regulated manner. TGF-β1 mRNA is expressed in endothelial, haematopoietic and connective-tissue cells, TGF-β2 mRNA is expressed in epithelial and neuronal cells, and TGF-β3 mRNA in mesenchymal cells (1,3,25). The sequence homology is 70-80% between TGF-β isoforms and 30-40% with activins/inhibins and BMP. TGF-β1, 2 and 3 are highly conserved in mammals suggesting a critical biological function for each of these isoforms, acting as strong mediators of tissue repair through chemotaxis and angiogenesis stimulation and extracellular matrix generation (1,3,25). TGF-β1 is a 112 amino acid polypeptide which forms a homodimer with both subunits linked with a disulfide bond. TGF-β1 is synthesized as a precursor of 391 amino acids whose amino acid sequence includes TGF-β1 and the propeptide latencyassociated peptide (LAP) in the amino terminal. TGF-β1 is cleaved from LAP before the precursor is secreted from the cells, but it continues non-covalently bond to this propeptide. After being secreted, TGF-β1 is stored at the extracellular matrix as a complex formed between TGF-β1, LAP and the latent TGF-b binding protein (LTBP). The relation between TGF-β1 and LTBP through disulfide bond prevents the binding of TGF-β1 to its receptors. In vivo, TGF-β1 is released from the complex by the matrix glycoprotein thrombospondin 1 (TSP-1), which changes the conformation of LTBP (1,25).Sociedad Argentina de Fisiología2006-06info:eu-repo/semantics/reviewinfo:eu-repo/semantics/publishedVersionRevisionhttp://purl.org/coar/resource_type/c_dcae04bcinfo:ar-repo/semantics/resenaArticuloapplication/pdfhttp://sedici.unlp.edu.ar/handle/10915/146981enginfo:eu-repo/semantics/altIdentifier/url/https://pmr.safisiol.org.ar/wp-content/uploads/2022/09/vol1_n11_june.pdfinfo:eu-repo/semantics/altIdentifier/issn/1669-5410info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:37:32Zoai:sedici.unlp.edu.ar:10915/146981Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:37:32.661SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Role of transforming growth factor β1 as modulator of endothelial L-Arginine/ nitric oxide signalling pathway
title Role of transforming growth factor β1 as modulator of endothelial L-Arginine/ nitric oxide signalling pathway
spellingShingle Role of transforming growth factor β1 as modulator of endothelial L-Arginine/ nitric oxide signalling pathway
Vásquez, Rodrigo
Ciencias Médicas
Fisiología
TGF-β
Growth factors
title_short Role of transforming growth factor β1 as modulator of endothelial L-Arginine/ nitric oxide signalling pathway
title_full Role of transforming growth factor β1 as modulator of endothelial L-Arginine/ nitric oxide signalling pathway
title_fullStr Role of transforming growth factor β1 as modulator of endothelial L-Arginine/ nitric oxide signalling pathway
title_full_unstemmed Role of transforming growth factor β1 as modulator of endothelial L-Arginine/ nitric oxide signalling pathway
title_sort Role of transforming growth factor β1 as modulator of endothelial L-Arginine/ nitric oxide signalling pathway
dc.creator.none.fl_str_mv Vásquez, Rodrigo
Sobrevia, Luis
author Vásquez, Rodrigo
author_facet Vásquez, Rodrigo
Sobrevia, Luis
author_role author
author2 Sobrevia, Luis
author2_role author
dc.subject.none.fl_str_mv Ciencias Médicas
Fisiología
TGF-β
Growth factors
topic Ciencias Médicas
Fisiología
TGF-β
Growth factors
dc.description.none.fl_txt_mv TGF-β is one of the members of the TGF-β superfamily of growth factors, including activins/inhibins and bone morphogenic proteins (BMP). At least three TGF-β isoforms have been reported in mammals: TGF-β1, TGF-β2 and TGF-β3. Virtually all human cells produce TGF-β and express its plasma membrane receptors. Each isoform is coded by a different gene, in a tissue-specific and developmental-regulated manner. TGF-β1 mRNA is expressed in endothelial, haematopoietic and connective-tissue cells, TGF-β2 mRNA is expressed in epithelial and neuronal cells, and TGF-β3 mRNA in mesenchymal cells (1,3,25). The sequence homology is 70-80% between TGF-β isoforms and 30-40% with activins/inhibins and BMP. TGF-β1, 2 and 3 are highly conserved in mammals suggesting a critical biological function for each of these isoforms, acting as strong mediators of tissue repair through chemotaxis and angiogenesis stimulation and extracellular matrix generation (1,3,25). TGF-β1 is a 112 amino acid polypeptide which forms a homodimer with both subunits linked with a disulfide bond. TGF-β1 is synthesized as a precursor of 391 amino acids whose amino acid sequence includes TGF-β1 and the propeptide latencyassociated peptide (LAP) in the amino terminal. TGF-β1 is cleaved from LAP before the precursor is secreted from the cells, but it continues non-covalently bond to this propeptide. After being secreted, TGF-β1 is stored at the extracellular matrix as a complex formed between TGF-β1, LAP and the latent TGF-b binding protein (LTBP). The relation between TGF-β1 and LTBP through disulfide bond prevents the binding of TGF-β1 to its receptors. In vivo, TGF-β1 is released from the complex by the matrix glycoprotein thrombospondin 1 (TSP-1), which changes the conformation of LTBP (1,25).
Sociedad Argentina de Fisiología
description TGF-β is one of the members of the TGF-β superfamily of growth factors, including activins/inhibins and bone morphogenic proteins (BMP). At least three TGF-β isoforms have been reported in mammals: TGF-β1, TGF-β2 and TGF-β3. Virtually all human cells produce TGF-β and express its plasma membrane receptors. Each isoform is coded by a different gene, in a tissue-specific and developmental-regulated manner. TGF-β1 mRNA is expressed in endothelial, haematopoietic and connective-tissue cells, TGF-β2 mRNA is expressed in epithelial and neuronal cells, and TGF-β3 mRNA in mesenchymal cells (1,3,25). The sequence homology is 70-80% between TGF-β isoforms and 30-40% with activins/inhibins and BMP. TGF-β1, 2 and 3 are highly conserved in mammals suggesting a critical biological function for each of these isoforms, acting as strong mediators of tissue repair through chemotaxis and angiogenesis stimulation and extracellular matrix generation (1,3,25). TGF-β1 is a 112 amino acid polypeptide which forms a homodimer with both subunits linked with a disulfide bond. TGF-β1 is synthesized as a precursor of 391 amino acids whose amino acid sequence includes TGF-β1 and the propeptide latencyassociated peptide (LAP) in the amino terminal. TGF-β1 is cleaved from LAP before the precursor is secreted from the cells, but it continues non-covalently bond to this propeptide. After being secreted, TGF-β1 is stored at the extracellular matrix as a complex formed between TGF-β1, LAP and the latent TGF-b binding protein (LTBP). The relation between TGF-β1 and LTBP through disulfide bond prevents the binding of TGF-β1 to its receptors. In vivo, TGF-β1 is released from the complex by the matrix glycoprotein thrombospondin 1 (TSP-1), which changes the conformation of LTBP (1,25).
publishDate 2006
dc.date.none.fl_str_mv 2006-06
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