Reduced expression of the adhesion protein tensin1 in cultured human dermal fibroblasts affects collagen gel contraction.
As revealed by immunohistochemistry and RT-QPCR, the focal adhesion protein tensin1 is expressed in cultured human dermal fibroblasts and reduced by 60% after transfection with tensin1 siRNA. Tensin1 silenced fibroblast exhibited a strongly reduced capacity to contract collagen gels. Aged fibroblasts, generated with the Hayflick replicative senescence model, exhibit as siRNA silences fibroblasts, a reduced tensin1 expression and an impaired gel contraction capacity. Based on these results, we speculate that in human dermal fibroblasts, tensin1 plays an important role in cell-matrix interaction and that a reduced expression might contribute to the dermal alterations observed during skin ageing.
Saintigny
Gaëlle
G
Chanel Parfum Beauté, 20 rue Victor Noir, Neuilly/Seine, France. gaelle.saintigny@chanel-corp.com
Bernard
François-Xavier
FX
Juchaux
Franck
F
Pedretti
Nathalie
N
Mahé
Christian
C
D002478:Cells, Cultured; D003094:Collagen / Q000502:physiology*; D005347:Fibroblasts / Q000378:metabolism*; D006801:Humans; D008840:Microfilament Proteins / Q000235:genetics / Q000378:metabolism*; D034741:RNA, Small Interfering / Q000235:genetics; D015595:Skin Aging; D000070876:Tensins
D008840:Microfilament Proteins; D034741:RNA, Small Interfering; C000603369:TNS1 protein, human; D000070876:Tensins; D003094:Collagen