OBJECTIVE: To determine the effects of a synthetic N-terminal peptide from link protein on the synthesis of proteoglycans by human articular cartilage. METHODS: Explants from adult knee cartilage were maintained for 4 days in serum-free Dulbecco's modified Eagle's medium. Peptides were added for the final 2 days of culture. Synthesis of proteoglycans and proteins was measured by the incorporation of 35S-sulfate and 3H-serine. The sizes, sulfation patterns, and serine: sulfate ratios of newly synthesized glycosaminoglycans were measured by gel chromatography, high performance liquid chromatography, and ion-exchange chromatography. RESULTS: The N-terminal peptide stimulated proteoglycan synthesis in cartilage from a wide age range of patients of both sexes. The newly synthesized glycosaminoglycans were identical in size and composition to those of control tissues, and their serine:sulfate ratios remained unchanged. CONCLUSION: This N-terminal peptide, which can be liberated from proteoglycan aggregates by proteolysis, potently stimulated the synthesis of proteoglycans with normal glycosaminoglycan chains. The results suggest that the N-terminal peptide may have a regulatory role in maintaining the integrity of human cartilage matrix.
OBJECTIVE: To determine the effects of a synthetic N-terminal peptide from link protein on the synthesis of proteoglycans by humanarticular cartilage. METHODS: Explants from adult knee cartilage were maintained for 4 days in serum-free Dulbecco's modified Eagle's medium. Peptides were added for the final 2 days of culture. Synthesis of proteoglycans and proteins was measured by the incorporation of 35S-sulfate and 3H-serine. The sizes, sulfation patterns, and serine: sulfate ratios of newly synthesized glycosaminoglycans were measured by gel chromatography, high performance liquid chromatography, and ion-exchange chromatography. RESULTS: The N-terminal peptide stimulated proteoglycan synthesis in cartilage from a wide age range of patients of both sexes. The newly synthesized glycosaminoglycans were identical in size and composition to those of control tissues, and their serine:sulfate ratios remained unchanged. CONCLUSION: This N-terminal peptide, which can be liberated from proteoglycan aggregates by proteolysis, potently stimulated the synthesis of proteoglycans with normal glycosaminoglycan chains. The results suggest that the N-terminal peptide may have a regulatory role in maintaining the integrity of humancartilage matrix.
Authors: Carol A Wise; Diane Sepich; Aki Ushiki; Anas M Khanshour; Yared H Kidane; Nadja Makki; Christina A Gurnett; Ryan S Gray; Jonathan J Rios; Nadav Ahituv; Lila Solnica-Krezel Journal: Bone Res Date: 2020-03-09 Impact factor: 13.567
Authors: Jillian E Mayer; James C Iatridis; Danny Chan; Sheeraz A Qureshi; Omri Gottesman; Andrew C Hecht Journal: Spine J Date: 2013-03 Impact factor: 4.166