Link Protein N-terminal Peptide Binds to Bone Morphogenetic Protein (BMP) Type II Receptor and Drives Matrix Protein Expression in Rabbit Intervertebral Disc Cells

• Authors: Zili Wang, Emory University; M. Neale Weitzmann, Emory University; Dr. Sreedhara Sangadala, Emory University; William C Hutton, Emory University; Sangwook Yoon, Emory University
• Journal Title: Journal of Biological Chemistry
• Volume: Volume 288, Number 39
• Publisher: American Society for Biochemistry and Molecular Biology | 2013-09-27, Pages 28243-28253
• Type of Work: Article | Final Publisher PDF
• Publisher DOI: http://doi.org/10.1074/jbc.M113.451948
• Subjects: Biology, Cell; Health Sciences, Medicine and Surgery
• Keywords: Science & Technology; Life Sciences & Biomedicine; Biochemistry & Molecular Biology; LOW-BACK-PAIN; CARTILAGE PROTEOGLYCANS; EXTRACELLULAR-MATRIX; ARTICULAR-CARTILAGE; NUCLEUS PULPOSUS; IN-VITRO; DEGENERATION; SOX9; GROWTH; BIOSYNTHESIS

Abstract

Background: LPP induces synthesis of aggrecan and collagen II; however, the mechanism is unknown. Results: LPP up-regulated expression of aggrecan, collagen II, and SOX9 through binding to BMP-RII, initiating a complex Smad/BMP feedforward circuit. Conclusion: LPP could promote disc matrix production directly or boost the activity of exogenous BMPs. Significance: LPP may have value in the treatment of degenerated discs.