Publications by authors named "Michelle Korda"

Introduction: Achilles tendinopathy (AT) is a cause of pain and disability affecting both athletes and sedentary individuals. More than 150 000 people in the UK every year suffer from AT.While there is much preclinical work on the use of stem cells in tendon pathology, there is a scarcity of clinical data looking at the use of mesenchymal stem cells to treat tendon disease and there does not appear to be any studies of the use of autologous cultured mesenchymal stem cells (MSCs) for AT.

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Introduction: Impaction allograft with cement is a common technique used in revision hip surgeries for the last 20 years. However, its clinical results are inconsistent. Recent studies have shown that mesenchymal stem cells (MSCs) seeded onto allograft can enhance bone formation.

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Revision total hip replacement has a failure rate of up to 25%. Part of the reason for this high failure is the lack of bone stock. In this study, we investigated whether mesenchymal stromal cells (MSCs) or osteoprogenitors (OPs) contribute to bone formation in impacted allograft or an allograft and hydroxyapatite (HA) combination.

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Tissue engineering approaches to regenerate bone stock in revision total hip replacements could enhance the longevity of the implant and benefit the quality of the patient's life. This study investigated the impaction of allograft with mesenchymal stem cells in an ovine hip hemiarthroplasty model. In total, 10 sheep were divided into two groups with 5 sheep in each group.

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Impaction allograft as a scaffold for bone-forming cells is a tissue-engineering approach for filling bone defects that are commonly encountered during revision total joint replacement (THR). The purpose of this in vitro study is to assess the viability of mesenchymal stem cells (MSC) grown on allograft following impaction using forces similar to those measured during revision total hip replacements. Impaction forces of 0, 3, 6, and 9 kN were used representing normal and high impact.

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Integrin alpha2beta1 is the major receptor for collagens in human tissues, being involved in cell adhesion and the control of collagen and collagenase gene expression. The collagen binding site of alpha2beta1 has been localized to the alpha2 von Willebrand Factor type A (VWFA) domain (A-domain or I-domain) and the residues responsible for the interaction with collagen have been mapped. We report a study of alpha2 VWFA domain in which residue E318, which lies outside the collagen binding site, is mutated to tryptophan, showing that this is a gain-of-function mutation.

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