Adhesion proteins--an impact on skeletal myoblast differentiation.

Formation of mammalian skeletal muscle myofibers, that takes place during embryogenesis, muscle growth or regeneration, requires precise regulation of myoblast adhesion and fusion. There are few evidences showing that adhesion proteins play important role in both processes. To follow the function of...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Marta Przewoźniak, Iwona Czaplicka, Areta M Czerwińska, Agnieszka Markowska-Zagrajek, Jerzy Moraczewski, Władysława Stremińska, Katarzyna Jańczyk-Ilach, Maria A Ciemerych, Edyta Brzoska
Formato: article
Lenguaje:EN
Publicado: Public Library of Science (PLoS) 2013
Materias:
R
Q
Acceso en línea:https://doaj.org/article/e68f0ccaa7fc4344b724f36bf72119da
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:e68f0ccaa7fc4344b724f36bf72119da
record_format dspace
spelling oai:doaj.org-article:e68f0ccaa7fc4344b724f36bf72119da2021-11-18T07:46:50ZAdhesion proteins--an impact on skeletal myoblast differentiation.1932-620310.1371/journal.pone.0061760https://doaj.org/article/e68f0ccaa7fc4344b724f36bf72119da2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23671573/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Formation of mammalian skeletal muscle myofibers, that takes place during embryogenesis, muscle growth or regeneration, requires precise regulation of myoblast adhesion and fusion. There are few evidences showing that adhesion proteins play important role in both processes. To follow the function of these molecules in myoblast differentiation we analysed integrin alpha3, integrin beta1, ADAM12, CD9, CD81, M-cadherin, and VCAM-1 during muscle regeneration. We showed that increase in the expression of these proteins accompanies myoblast fusion and myotube formation in vivo. We also showed that during myoblast fusion in vitro integrin alpha3 associates with integrin beta1 and ADAM12, and also CD9 and CD81, but not with M-cadherin or VCAM-1. Moreover, we documented that experimental modification in the expression of integrin alpha3 lead to the modification of myoblast fusion in vitro. Underexpression of integrin alpha3 decreased myoblasts' ability to fuse. This phenomenon was not related to the modifications in the expression of other adhesion proteins, i.e. integrin beta1, CD9, CD81, ADAM12, M-cadherin, or VCAM-1. Apparently, aberrant expression only of one partner of multiprotein adhesion complexes necessary for myoblast fusion, in this case integrin alpha3, prevents its proper function. Summarizing, we demonstrated the importance of analysed adhesion proteins in myoblast fusion both in vivo and in vitro.Marta PrzewoźniakIwona CzaplickaAreta M CzerwińskaAgnieszka Markowska-ZagrajekJerzy MoraczewskiWładysława StremińskaKatarzyna Jańczyk-IlachMaria A CiemerychMaria A CiemerychEdyta BrzoskaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 5, p e61760 (2013)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Marta Przewoźniak
Iwona Czaplicka
Areta M Czerwińska
Agnieszka Markowska-Zagrajek
Jerzy Moraczewski
Władysława Stremińska
Katarzyna Jańczyk-Ilach
Maria A Ciemerych
Maria A Ciemerych
Edyta Brzoska
Adhesion proteins--an impact on skeletal myoblast differentiation.
description Formation of mammalian skeletal muscle myofibers, that takes place during embryogenesis, muscle growth or regeneration, requires precise regulation of myoblast adhesion and fusion. There are few evidences showing that adhesion proteins play important role in both processes. To follow the function of these molecules in myoblast differentiation we analysed integrin alpha3, integrin beta1, ADAM12, CD9, CD81, M-cadherin, and VCAM-1 during muscle regeneration. We showed that increase in the expression of these proteins accompanies myoblast fusion and myotube formation in vivo. We also showed that during myoblast fusion in vitro integrin alpha3 associates with integrin beta1 and ADAM12, and also CD9 and CD81, but not with M-cadherin or VCAM-1. Moreover, we documented that experimental modification in the expression of integrin alpha3 lead to the modification of myoblast fusion in vitro. Underexpression of integrin alpha3 decreased myoblasts' ability to fuse. This phenomenon was not related to the modifications in the expression of other adhesion proteins, i.e. integrin beta1, CD9, CD81, ADAM12, M-cadherin, or VCAM-1. Apparently, aberrant expression only of one partner of multiprotein adhesion complexes necessary for myoblast fusion, in this case integrin alpha3, prevents its proper function. Summarizing, we demonstrated the importance of analysed adhesion proteins in myoblast fusion both in vivo and in vitro.
format article
author Marta Przewoźniak
Iwona Czaplicka
Areta M Czerwińska
Agnieszka Markowska-Zagrajek
Jerzy Moraczewski
Władysława Stremińska
Katarzyna Jańczyk-Ilach
Maria A Ciemerych
Maria A Ciemerych
Edyta Brzoska
author_facet Marta Przewoźniak
Iwona Czaplicka
Areta M Czerwińska
Agnieszka Markowska-Zagrajek
Jerzy Moraczewski
Władysława Stremińska
Katarzyna Jańczyk-Ilach
Maria A Ciemerych
Maria A Ciemerych
Edyta Brzoska
author_sort Marta Przewoźniak
title Adhesion proteins--an impact on skeletal myoblast differentiation.
title_short Adhesion proteins--an impact on skeletal myoblast differentiation.
title_full Adhesion proteins--an impact on skeletal myoblast differentiation.
title_fullStr Adhesion proteins--an impact on skeletal myoblast differentiation.
title_full_unstemmed Adhesion proteins--an impact on skeletal myoblast differentiation.
title_sort adhesion proteins--an impact on skeletal myoblast differentiation.
publisher Public Library of Science (PLoS)
publishDate 2013
url https://doaj.org/article/e68f0ccaa7fc4344b724f36bf72119da
work_keys_str_mv AT martaprzewozniak adhesionproteinsanimpactonskeletalmyoblastdifferentiation
AT iwonaczaplicka adhesionproteinsanimpactonskeletalmyoblastdifferentiation
AT aretamczerwinska adhesionproteinsanimpactonskeletalmyoblastdifferentiation
AT agnieszkamarkowskazagrajek adhesionproteinsanimpactonskeletalmyoblastdifferentiation
AT jerzymoraczewski adhesionproteinsanimpactonskeletalmyoblastdifferentiation
AT władysławastreminska adhesionproteinsanimpactonskeletalmyoblastdifferentiation
AT katarzynajanczykilach adhesionproteinsanimpactonskeletalmyoblastdifferentiation
AT mariaaciemerych adhesionproteinsanimpactonskeletalmyoblastdifferentiation
AT mariaaciemerych adhesionproteinsanimpactonskeletalmyoblastdifferentiation
AT edytabrzoska adhesionproteinsanimpactonskeletalmyoblastdifferentiation
_version_ 1718423007094898688