2006
DOI: 10.1111/j.1432-0436.2005.00059.x
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Integrin α3 subunit participates in myoblast adhesion and fusion in vitro

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Cited by 49 publications
(47 citation statements)
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References 62 publications
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“…We performed experiments using an antibody specific for the extracellular domains of M-cadherin and showed that it inhibited the fusion of cultured myoblasts. Our observations suggest significant role of M-cadherin in the differentiation of satellite cells and in myoblast fusion in primary cultures Moreover, we showed (Brzoska et al, 2006a), that the integrin α3 subunit was expressed in quiescent and activated satellite cells and was localized at cell-cell and cell-extracellular matrix contacts during myoblasts differentiation (Fig. 3D).…”
Section: D B Asupporting
confidence: 62%
“…We performed experiments using an antibody specific for the extracellular domains of M-cadherin and showed that it inhibited the fusion of cultured myoblasts. Our observations suggest significant role of M-cadherin in the differentiation of satellite cells and in myoblast fusion in primary cultures Moreover, we showed (Brzoska et al, 2006a), that the integrin α3 subunit was expressed in quiescent and activated satellite cells and was localized at cell-cell and cell-extracellular matrix contacts during myoblasts differentiation (Fig. 3D).…”
Section: D B Asupporting
confidence: 62%
“…Knockdown of a3 or b1 integrin, or inhibition of a9b1 integrin function inhibits myoblast fusion both in vitro and in vivo. 15,16,17 In parallel with studies in Drosophila, knockdown of BRAG2 in cultured mammalian myoblasts also impairs fusion, apparently by disrupting the organization of focal adhesions. 13 Studies from our laboratory have shown that BRAG2 modulates the level of cell surface b1-integrin, at least in part by regulating its rate of endocytosis.…”
Section: Integrin Traffickingmentioning
confidence: 81%
“…For example, molecules such as musclecadherin (M-cadherin), integrins and a disintegrin and metalloprotease 12 (Adam12) are commonly found localized at the contact sites in both contacting muscle cells (Cifuentes-Diaz et al, 1995;Schwander et al, 2003;Lafuste et al, 2005;Brzoska et al, 2006). M-cadherin function is required for myotube formation in vitro (Zeschnigk et al, 1995;Charrasse et al, 2006) but not in vivo (Hollnagel et al, 2002), suggesting that other cadherins or cell adhesion molecules may functionally compensate for the lack of Mcadherin.…”
Section: Myoblast Migration Recognition and Adhesion In Micementioning
confidence: 99%
“…M-cadherin function is required for myotube formation in vitro (Zeschnigk et al, 1995;Charrasse et al, 2006) but not in vivo (Hollnagel et al, 2002), suggesting that other cadherins or cell adhesion molecules may functionally compensate for the lack of Mcadherin. Eliminating the function of 1 integrin, 3 integrin and 9 integrin decreases myoblast fusion in vitro (Schwander et al, 2003;Lafuste et al, 2005;Brzoska et al, 2006) and in vivo (Schwander et al, 2003). Adam12 is a transmembrane protein that contains an integrin-binding site and can bind 91 integrin in muscle cells (Lafuste et al, 2005).…”
Section: Myoblast Migration Recognition and Adhesion In Micementioning
confidence: 99%