Comparison of satellite cell-derived myoblasts and C2C12 differentiation in two- and three-dimensional cultures: changes in adhesion protein expression.
Changes in the expression of adhesion proteins involved in myoblast differentiation were investigated in monolayer (two-dimensional) and 3D (three-dimensional) cell cultures. The expression of integrin alpha3 subunit, integrin beta1 subunit, ADAM12 (a disintegrin and metalloproteinase 12), tetraspanins CD9 and CD81 and M-cadherin were examined in the murine myoblast cell line C2C12 and in a primary culture of rat satellite cells. Myoblasts in monolayer and 3D cultures showed significant differences in their morphology and cytoskeletal organization. All of the studied proteins participated in myoblast fusion in each culture examined, but differences in their levels of expression were observed. Satellite cell-derived myoblasts exhibited higher expression of adhesion protein mRNAs than C2C12 cells. Also, C2C12 cells from a 3D culture showed slightly higher expression of adhesion protein transcripts than the same cells cultured as a monolayer. Significantly, the levels of adhesion protein mRNAs were found to change in parallel in all cell culture types. Despite this finding, it is important that differences between satellite cell-derived myoblasts and cell line C2C12 grown in monolayer and 3D cultures are taken into account when studying processes of myoblast differentiation in vitro.
Grabowska
Iwona
I
Department of Cytology, Institute of Zoology, Faculty of Biology, University of Warsaw, 1 Miecznikowa St., 02096 Warsaw, Poland.
Szeliga
Anna
A
Moraczewski
Jerzy
J
Czaplicka
Iwona
I
Brzóska
Edyta
E
D051722:ADAM Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism; D000818:Animals; D015703:Antigens, CD / Q000032:analysis / Q000235:genetics / Q000378:metabolism; D015820:Cadherins / Q000032:analysis / Q000235:genetics / Q000378:metabolism; D002448:Cell Adhesion; D018929:Cell Culture Techniques; D002454:Cell Differentiation; D002478:Cells, Cultured; D039422:Integrin alpha3 / Q000032:analysis / Q000235:genetics / Q000378:metabolism; D019012:Integrin beta1 / Q000032:analysis / Q000235:genetics / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism*; D051379:Mice; D032446:Myoblasts / Q000166:cytology / Q000378:metabolism*; D012333:RNA, Messenger / Q000378:metabolism; D051381:Rats; D032496:Satellite Cells, Skeletal Muscle / Q000166:cytology / Q000378:metabolism*; D060225:Tetraspanin 28; D060245:Tetraspanin 29
D015703:Antigens, CD; D015820:Cadherins; C554799:Cd81 protein, mouse; C554797:Cd81 protein, rat; C554870:Cd9 protein, mouse; D039422:Integrin alpha3; D019012:Integrin beta1; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D012333:RNA, Messenger; D060225:Tetraspanin 28; D060245:Tetraspanin 29; C070896:M-cadherin; D051722:ADAM Proteins