A novel function of glycosaminoglycans in degradation of collagen fibrils of bone

2020 Fiscal Year Final Research Report

• Project/Area Number: 18K06106
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Review Section: Basic Section 43030:Functional biochemistry-related
• Research Institution: Hirosaki University
• Principal Investigator: Tatara Yota 弘前大学, 医学研究科, 助教 (00443995)
• Project Period (FY): 2018-04-01 – 2021-03-31
• Keywords: グリコサミノグリカン / 骨分解 / コラーゲン線維

Outline of Final Research Achievements

Even though collagen and glycosaminoglycans (GAGs) are the major organic components of bone, little is known about their interaction so far. I have found that GAGs bind to collagen fibrils under acidic conditions to form acid-resistant collagen fibrils. In this year's study, I investigated the degradation of acid-resistant collagen fibrils by cathepsin K using a measurement system with a mass spectrometer that can comprehensively monitor the degradation products of collagen. As a result, the release of peptides from collagen fibrils by cathepsin K tended to be suppressed in the samples in which collagen fibrils bind to chondroitin 4-sulfate to form acid-resistant collagen fibrils.

Free Research Field

糖質生物学

Academic Significance and Societal Importance of the Research Achievements

グリコサミノグリカン（GAG）がコラーゲン線維に結合して、耐酸性コラーゲン線維を形成することに本研究による新発見であり、骨分解においてGAGが今まで知られていなかった新しい機能を持つ可能性が示された意義がある。このことは骨吸収においてコラーゲン線維が分解されるメカニズムの解明に寄与するものであり、骨のGAGをターゲットとした新しい骨粗鬆症治療薬の開発への貢献が期待される。