Efficacy and Safety of Escherichia coli-derived recombinant human bone morphogenetic protein-2 in additional lumbar posterolateral fusion: minimum 1 year follow-up

Author(s):  
Hee-Jung Son ◽  
Sung Hoon Choi ◽  
Myoung Keun Lee ◽  
Chang-Nam Kang
2017 ◽  
Vol 30 (02) ◽  
pp. 153-159 ◽  
Author(s):  
Anna Massie ◽  
Mark Fuller ◽  
Frank Verstraete ◽  
Boaz Arzi ◽  
Amy Kapatkin

SummaryObjectives: To report the use of compression resistant matrix (CRM) infused with recombinant human bone morphogenetic protein (rhBMP-2) prospectively in the healing of non union long-bone fractures in dogs.Methods: A longitudinal cohort of dogs that were presented with nonunion fractures were classified and treated with CRM soaked with rhBMP-2 and fracture fixation. They were followed with serial radiographs and evaluated for healing times and complications according to the time frame and definitions previously established for orthopaedic clinical cases.Results: Eleven nonunion fractures in nine dogs were included. Median healing time was 10 weeks (range: 7–20 weeks). Major perioperative complications due to bandage morbidity were encountered in two of 11 limbs and resolved. All other complications were minor. They occurred perioperatively in eight of 11 limbs. Minor follow-up complications included short-term in one of two limbs, mid-term in one of three, and long-term in four of five limbs. Nine limbs returned to full function and two limbs returned to acceptable function at the last follow-up.Clinical significance: Nonunion fractures given a poor prognosis via standard-of-care treatment were successfully repaired using CRM with rhBMP-2 accompanying fixation. These dogs, previously at high risk of failure, returned to full or acceptable function.


2019 ◽  
Vol 32 (3) ◽  
pp. 153-157
Author(s):  
Wei Chen ◽  
Caiqian Zhang ◽  
Yeqing Wu ◽  
Xiuping Su

Abstract We developed a simple method of preparing recombinant human bone morphogenetic protein-2 (rhBMP-2) with high biological activity. This rhBMP-2 was overproduced in Escherichia coli as a fusion protein with thioredoxin 6xHis-tag at its amino terminus. The cDNA fragment of human bone morphogenetic protein-2 (hBMP-2) fused to the secretion signal of alkaline phosphatase (PhoA) was expressed under T7 promoter in E. coli. After DNA sequence confirmation, the recombinant vector pETpho-bmp2 was transformed into E. coli BL21 (DE3). rhBMP-2 was produced by the recombinant strain pETpho-bmp2/BL21 (DE3) in a soluble form with an yield of 6.2 mg/L culture. Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis (SDS-PAGE) results showed that the molecular weight of the product was approximately 28 kD. Moreover, rhBMP-2 was secreted as a dimer with a natural structure. rhBMP-2, purified by Ni Nitrilotriacetic acid Agarose (Ni-NTA) affinity chromatography, was used to examine osteosarcoma MG-63 cells and assay the alkaline phosphatase (ALP) activity. Results showed that rhBMP-2 induced MG-63 cell differentiation. When the final concentration was 500 ng/mL, the effect was more remarkable and ALP activity reached 525% compared with that of the control group.


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