Short-term effects of adhesion peptides on the responses of preosteoblasts to pBMP-9.
Adhesion peptides are currently used to enhance the interactions of osteoblasts with biomaterials. However, little is known about the effects of adhesion peptides on cell responses to growth factors, especially the bone morphogenetic proteins (BMPs). We used adhesion peptides Ac-CGGNGERPRGDTYRAY-NH(2) (pRGD), derived from bone sialoprotein, and Ac-CGGDGEA-NH(2) (pDGEA), derived from collagen, which interact with alpha(v)beta(3) and alpha(2)beta(1) integrins, respectively. We analyzed the effects of pRGD- and pDGEA-coated polystyrene (PS) on the responses of murine MC3T3-E1 preosteoblasts to a peptide derived from human BMP-9 (pBMP-9) in serum-free medium. After 1h, pRGD favoured interactions with alpha(v) while pDGEA bound beta(1) integrin subunits. Adding pBMP-9 (400 ng/mL) increased the amount of alpha(v) integrin subunits in cell membranes on pRGD-coated PS, but had no effect on beta(1) integrin subunits. Only on this substratum, collagen type I mRNA was enhanced and the addition of pBMP-9 promoted the early cell differentiation, increasing their alkaline phosphatase (ALP) activity within 24 h. These cells also organized beta(1) integrin subunits at their focal adhesion points. Inhibiting alpha(2)beta(1) integrins by pDGEA pre-treatment decreased this ALP activity. It is therefore important to understand the impact of adhesion peptides on the early cell responses to growth factors in order to improve biomimetic materials.
Marquis
Marie-Eve
ME
Laboratory of Cell-Biomaterial Biohybrid Systems, Chemical Engineering Department, Université de Sherbrooke, 2500, Université Blvd, Sherbrooke, Québec, Canada J1K 2R1.
Lord
Etienne
E
Bergeron
Eric
E
Bourgoin
Lee
L
Faucheux
Nathalie
N
D000469:Alkaline Phosphatase / Q000378:metabolism; D000818:Animals; D017209:Apoptosis / Q000187:drug effects; D019485:Bone Morphogenetic Proteins / Q000494:pharmacology*; D015815:Cell Adhesion Molecules / Q000737:chemistry*; D002454:Cell Differentiation / Q000187:drug effects; D049109:Cell Proliferation / Q000187:drug effects; D003094:Collagen / Q000737:chemistry; D024042:Collagen Type I / Q000235:genetics; D000090602:Collagen Type I, alpha 1 Chain; D016895:Culture Media, Serum-Free / Q000494:pharmacology; D022001:Focal Adhesions / Q000378:metabolism; D015870:Gene Expression / Q000187:drug effects; D055427:Growth Differentiation Factor 2; D055412:Growth Differentiation Factors; D006801:Humans; D038982:Integrin alpha2beta1 / Q000037:antagonists & inhibitors; D039564:Integrin alphaV / Q000378:metabolism; D019012:Integrin beta1 / Q000378:metabolism; D058574:Integrin-Binding Sialoprotein; D051379:Mice; D010006:Osteoblasts / Q000166:cytology / Q000187:drug effects* / Q000378:metabolism; D010455:Peptides / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D011137:Polystyrenes / Q000737:chemistry / Q000494:pharmacology; D012795:Sialoglycoproteins / Q000737:chemistry; D016596:Vinculin / Q000378:metabolism
D019485:Bone Morphogenetic Proteins; D015815:Cell Adhesion Molecules; D024042:Collagen Type I; D000090602:Collagen Type I, alpha 1 Chain; D016895:Culture Media, Serum-Free; C525887:GDF2 protein, human; C526108:Gdf2 protein, mouse; D055427:Growth Differentiation Factor 2; D055412:Growth Differentiation Factors; C546871:IBSP protein, human; C546872:Ibsp protein, mouse; D038982:Integrin alpha2beta1; D039564:Integrin alphaV; D019012:Integrin beta1; D058574:Integrin-Binding Sialoprotein; D010455:Peptides; D011137:Polystyrenes; D012795:Sialoglycoproteins; D016596:Vinculin; D003094:Collagen; D000469:Alkaline Phosphatase