Recent studies on human platelets-galectin-1 interactions

Animal lectins are proteins that have the ability to bind monosaccharide or oligosaccharide carbohydrates. They were classified into five families according to their primary structure. Galectins, one of the members of this group, were previously known as S-type lectins or S-Lac. The galectin family...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: González, Mariana Marta, Fink, Nilda Esther
Formato: Articulo
Lenguaje:Inglés
Publicado: 2009
Materias:
Química
galectin-1
human platelets
trombin
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/177405
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-177405
record_format dspace
spelling I19-R120-10915-1774052025-03-14T20:12:40Z http://sedici.unlp.edu.ar/handle/10915/177405 Recent studies on human platelets-galectin-1 interactions González, Mariana Marta Fink, Nilda Esther 2009 2025-03-14T17:08:41Z en Química galectin-1 human platelets trombin Animal lectins are proteins that have the ability to bind monosaccharide or oligosaccharide carbohydrates. They were classified into five families according to their primary structure. Galectins, one of the members of this group, were previously known as S-type lectins or S-Lac. The galectin family is a phylogenetically conserved lectin family which shared amino acid sequences and a carbohydrate recognition domain. All galectins bind lactose and other β-galactosidic oligosaccharides. Fifteen mammalian galectins have been identified, being designated as Gal-1 to Gal-15. We have previously demonstrated that porcine spleen Gal-1 interacts with resting human platelets and after activation with thrombin (Tr) demonstrating the presence of receptors, a necessary condition in order to exert functional roles. The discovery of endogenous Gal-1 and their potential ligands/receptors, suggest an autocrine mechanism acting in HPlt (human platelets) to produce different functional roles. The information available is very poor which demonstrates the need to deep other aspects, some of which have already been addressed (localization and ultrastructural changes, protein associations and platelet receptors) and other are pending, as its relevance in platelet physiopathology, in particular its association with thrombotic and inflammatory processes. Las lectinas animales son proteínas que tienen la capacidad de unir carbohidratos, monosacáridos u oligosacáridos simples. Fueron clasificadas en cinco familias de acuerdo a su estructura primaria. Las galectinas, uno de los miembros de este grupo, fueron previamente conocidas como lectinas de tipo S o S-Lac. Las galectinas son una familia filogenéticamente conservada de lectinas que contienen secuencias de aminoácidos características compartidas y dominios de reconocimiento de carbohidratos. Todas las galectinas unen lactosa y otros oligosacáridos β-galactosídicos. Se han identificado 15 galectinas de mamíferos, siendo designadas como Gal-1 a Gal-15. En nuestro trabajo, demostramos que la Gal-1 esplénica porcina interacciona con plaquetas humanas (PltH) en reposo y luego de la activación con trombina (Tr) lo cual demuestra la presencia de receptores, condición necesaria para que pueda ejercer algún rol funcional. El hallazgo de Gal-1 endógena y de posibles receptores, permite suponer que un mecanismo autócrino actúe en la Plth para ejercer diferentes roles funcionales. La información disponible es muy escasa lo que demuestra la necesidad de profundizar otros aspectos, algunos de los cuales ya han sido abordados (localización y cambios ultraestructurales, asociaciones proteicas y receptores plaquetarios) y otros están pendientes de encarar, como su relevancia en la fisiopatología plaquetaria, en particular su vinculación a procesos trombóticos y a la inflamación. Facultad de Ciencias Exactas Articulo Articulo http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) application/pdf 234-241
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Química
galectin-1
human platelets
trombin
spellingShingle Química
galectin-1
human platelets
trombin
González, Mariana Marta
Fink, Nilda Esther
Recent studies on human platelets-galectin-1 interactions
topic_facet Química
galectin-1
human platelets
trombin
description Animal lectins are proteins that have the ability to bind monosaccharide or oligosaccharide carbohydrates. They were classified into five families according to their primary structure. Galectins, one of the members of this group, were previously known as S-type lectins or S-Lac. The galectin family is a phylogenetically conserved lectin family which shared amino acid sequences and a carbohydrate recognition domain. All galectins bind lactose and other β-galactosidic oligosaccharides. Fifteen mammalian galectins have been identified, being designated as Gal-1 to Gal-15. We have previously demonstrated that porcine spleen Gal-1 interacts with resting human platelets and after activation with thrombin (Tr) demonstrating the presence of receptors, a necessary condition in order to exert functional roles. The discovery of endogenous Gal-1 and their potential ligands/receptors, suggest an autocrine mechanism acting in HPlt (human platelets) to produce different functional roles. The information available is very poor which demonstrates the need to deep other aspects, some of which have already been addressed (localization and ultrastructural changes, protein associations and platelet receptors) and other are pending, as its relevance in platelet physiopathology, in particular its association with thrombotic and inflammatory processes.
format Articulo
Articulo
author González, Mariana Marta
Fink, Nilda Esther
author_facet González, Mariana Marta
Fink, Nilda Esther
author_sort González, Mariana Marta
title Recent studies on human platelets-galectin-1 interactions
title_short Recent studies on human platelets-galectin-1 interactions
title_full Recent studies on human platelets-galectin-1 interactions
title_fullStr Recent studies on human platelets-galectin-1 interactions
title_full_unstemmed Recent studies on human platelets-galectin-1 interactions
title_sort recent studies on human platelets-galectin-1 interactions
publishDate 2009
url http://sedici.unlp.edu.ar/handle/10915/177405
work_keys_str_mv AT gonzalezmarianamarta recentstudiesonhumanplateletsgalectin1interactions
AT finknildaesther recentstudiesonhumanplateletsgalectin1interactions
_version_ 1849827798039920640

Ejemplares similares