2005
DOI: 10.1016/j.jinorgbio.2005.01.011
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Adsorption of recombinant human bone morphogenetic protein rhBMP-2m onto hydroxyapatite

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Cited by 91 publications
(94 citation statements)
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References 33 publications
(35 reference statements)
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“…The amount of active rhBMP-2 detected in the cell culture medium supernatant is reduced to a corresponding amount. We attribute this effect to the high affinity of BMP-2 to hydroxyapatite-based materials [37] as well as to the high surface area (79.7 m 2 /g) of DBBM due to its micro-and nano-structure [38]. Moreover, instead of the expected release after immersion of to hydroxyapatite is higher than the affinity of bovine serum albumin to hydroxyapatite [37].…”
Section: Biological Activity Of Rhbmp-2 -Impact Of Bone Substitute Mamentioning
confidence: 93%
See 1 more Smart Citation
“…The amount of active rhBMP-2 detected in the cell culture medium supernatant is reduced to a corresponding amount. We attribute this effect to the high affinity of BMP-2 to hydroxyapatite-based materials [37] as well as to the high surface area (79.7 m 2 /g) of DBBM due to its micro-and nano-structure [38]. Moreover, instead of the expected release after immersion of to hydroxyapatite is higher than the affinity of bovine serum albumin to hydroxyapatite [37].…”
Section: Biological Activity Of Rhbmp-2 -Impact Of Bone Substitute Mamentioning
confidence: 93%
“…We attribute this effect to the high affinity of BMP-2 to hydroxyapatite-based materials [37] as well as to the high surface area (79.7 m 2 /g) of DBBM due to its micro-and nano-structure [38]. Moreover, instead of the expected release after immersion of to hydroxyapatite is higher than the affinity of bovine serum albumin to hydroxyapatite [37]. The reduced activity of the supernatant, however, does not necessarily imply a reduced activity in vivo, as indicated by successful studies on the combination of DBBM and rhBMP-2 [9,32,39].…”
Section: Biological Activity Of Rhbmp-2 -Impact Of Bone Substitute Mamentioning
confidence: 99%
“…They can only be displaced by mineral ions and/or soluble proteins with a stronger affinity for apatite surfaces but in a predicable manner, or by cell activity (Errassif et al, 2010). This characteristic has been observed for various growth factors like bone morphogenetic protein (BMP-2) or vascular endothelial growth factor (VEGF) (Midy et al, 2001;Boix et al, 2005), antiosteoporisis agents (Yoshinari et al, 2001;McLeod et al, 2006) and anticancer drugs as methotraxate and cisplatin (Barroug et al, 2004;Lebugle et al, 2002). It has been reported that slow release of MTX from calcium phosphate is not only due to the porosity like in most of the cases, but mainly due to the adsorption of MTX (Lebugle et al, 2002).…”
Section: Drug Deliverymentioning
confidence: 99%
“…Some studies have investigated the bone forming capacities of growth factors loaded synthetic bone substitutes. In terms of growth factors, most research has focused on the use of the bone morphogenic proteins (BMPs) (Mont et al 2004;Termaat et al, 2005 (Boix et al, 2005). Current examination of alternatives to grafting techniques suggests three possible new approaches to inducing new bone formation: implantation of certain cytokines such as BMPs in combination with appropriate delivery systems at the target site (Liu et al, 2007;Niu et al, 2009); transduction of genes encoding cytokines with osteogenic capacity into cells at repair sites; and transplantation of cultured osteogenic cells derived from host bone marrow (Chu et al, 2007).…”
Section: Introductionmentioning
confidence: 99%