Cartilage proteoglycan core protein gene expression during limb cartilage differentiation |
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| Authors: | R A Kosher S W Gay J R Kamanitz W M Kulyk B J Rodgers S Sai T Tanaka M L Tanzer |
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| Affiliation: | 1. Department of Anatomy, University of Connecticut Health Center, Farmington, Connecticut 06032 USA;2. Department of Biochemistry, University of Connecticut Health Center, Farmington, Connecticut 06032 USA;1. Department of Anesthesiology, The Affiliated Huai’an Hospital of Xuzhou Medical University and the Second People’s Hospital of Huai’an, Huaian, 223001, Jiangsu, China;2. Department of Pain Management, The Central Hospital of Wuhan, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, 430014, Hubei, China;3. Department of Radiology, The Affiliated Huai’an Hospital of Xuzhou Medical University and the Second People’s Hospital of Huai’an, Huaian, 223001, Jiangsu, China;4. Department of Ultrasonography, The Affiliated Huai’an Hospital of Xuzhou Medical University and the Second People’s Hospital of Huai’an, Huaian, 223001, Jiangsu, China;5. Department of Neurosurgery, The Affiliated Huai’an Hospital of Xuzhou Medical University and the Second People’s Hospital of Huai’an, Huai’an, 223002, China;6. Department of Pain Management, The Affiliated Huai’an Hospital of Xuzhou Medical University and the Second People’s Hospital of Huai’an, Huaian, 223001, Jiangsu, China;1. State Key Laboratory of Oral Diseases & National Clinical Research Center for Oral Diseases, West China Hospital of Stomatology, Sichuan University, Chengdu, China;2. Translational Research Program of Pediatric Orthopedics, Department of Surgery, Children’s Hospital of Philadelphia, Philadelphia, PA, USA;3. Courant Institute of Mathematical Sciences, New York University, New York, NY, USA;4. Orthopedic Institute, Medical College, Soochow University, Suzhou, China;5. West China Hospital of Stomatology, Sichuan University, Chengdu, China;6. Department of Orthopedics, The Second Xiangya Hospital, Central South University, Changsha, China;7. Department of Orthopedic Surgery, University of Pennsylvania, Philadelphia, PA, USA;3. From the Medical Research Council Centre for Drug Safety Science, Department of Molecular and Clinical Pharmacology, Institute of Translational Medicine, University of Liverpool, Liverpool L69 3GE, United Kingdom;4. Department of Biomedical Engineering, Lerner Research Institute, Cleveland Clinic, Cleveland, Ohio 44195;5. Research Division, Shriners Hospital for Children, Portland, Oregon 97239;6. Department of Biochemistry, Faculty of Medicine, Oita University, Oita 879-5593, Japan;1. Center for Regenerative Medicine and Skeletal Development, School of Dental Medicine, University of Connecticut Health Center, United States;2. Biomedical Engineering Program, College of Engineering and Applied Science, University of Cincinnati, United States;3. Department of Orthopaedic Surgery, Washington University in St. Louis, United States;4. Division of Developmental Biology, Cincinnati Children’s Hospital Medical Center, United States;5. Department of Orthopaedic Surgery, Nippon Medical School Hospital, Tokyo, Japan;1. Department of Anatomy and Cell Biology, University of Iowa Carver College of Medicine, Iowa City, IA, USA;2. College of Engineering, University of Iowa Carver College of Medicine, Iowa City, IA, USA;3. Center for Gene Therapy, University of Iowa Carver College of Medicine, Iowa City, IA, USA;4. Institute for Vision Research, University of Iowa Carver College of Medicine, Iowa City, IA, USA |
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| Abstract: | Changes in the steady-state cytoplasmic levels of mRNA for the core protein of the major sulfated proteoglycan of cartilage were examined during the course of limb chondrogenesis in vitro using cloned cDNA probes. Cytoplasmic core protein mRNA begins to accumulate at the onset of overt chondrogenesis in micromass culture coincident with the crucial condensation phase of the process, in which prechondrogenic mesenchymal cells become closely juxtaposed prior to depositing a cartilage matrix. The initiation of core protein mRNA accumulation coincides with a dramatic increase in the accumulation of mRNA for type II collagen, the other major constituent of hyaline cartilage matrix. Following condensation, there is a concomitant progressive increase in cytoplasmic core protein and type II collagen mRNA accumulation which parallels the progressive accumulation of cartilage matrix by the cells. The relative rate of accumulation of cytoplasmic type II collagen mRNA is greater than twice that of core protein mRNA during chondrogenesis in micromass culture. Cyclic AMP, an agent implicated in the regulation of chondrogenesis elicits a concomitant two- to fourfold increase in both cartilage core protein and type II collagen mRNA levels by limb mesenchymal cells. Core protein gene expression is more sensitive to cAMP than type II collagen gene expression. These results suggest that the cartilage proteoglycan core protein and type II collagen genes are coordinately regulated during the course of limb cartilage differentiation, although there are quantitative differences in the extent of expression of the two genes. |
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