Study finds genetically engineered muscle-derived stem cells improved cartilage repair in rats
Damage to articular cartilage (cartilage covering the ends of bones where they meet in a joint) frequently occurs due to injury or illness, and can lead to degenerative disease. Treatments and experimental approaches to repair this articular cartilage have achieved limited results, but currently there is no method to fully restore this type of injured cartilage. Tissue engineering involving the delivery of therapeutic proteins to the injured site is a promising new approach to repairing articular cartilage. Previous studies have suggested that muscles contain stem cells that can develop in various ways, including into cells that lead to the formation of bone. In a study published in the February 2006 issue of Arthritis & Rheumatism (http://www.interscience.wiley.com/journal/arthritis), researchers designed a study using muscle-derived stem cells (MDSCs) genetically engineered with a therapeutic protein in an effort to repair articular cartilage defects in rats.
Led by Johnny Huard, PhD, director of the Growth and Development Laboratory at Childrens Hospital of Pittsburgh and an associate professor in the departments of Orthopaedic Surgery and Molecular Genetics and Biochemistry and Bioengineering at the University of Pittsburgh School of Medicine, researchers induced damage to the knee joints in 36 12-week-old rats and divided them into three groups. Group 1 was treated with MDSCs embedded in fibrin glue. Group 2 was treated with MDSCs that had been cultured from 3-week-old rats and genetically engineered to express bone morphogenetic protein-4 (BMP-4). Group 3, the control group, was treated with fibrin glue.
Amy Molnar | EurekAlert!
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
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