1999 Fiscal Year Final Research Report Summary
Purification of a new bone metabolic marker from human cortical and cancellous bone.
| Project/Area Number |
10671386
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Orthopaedic surgery
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| Research Institution | JIKEI UNIVERSITY |
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Principal Investigator |
MARUNO Keishi Jikei University,School of Medicine,Department of Orthopaedic Surgery, Lecturer, 医学部, 講師 (70199925)
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| Co-Investigator(Kenkyū-buntansha) |
SAITO Mitsuru Jikei University,School of Medicine,Department of Orthopaedic Surgery,Research Assistant, 医学部, 助手 (50301528)
KOYANO Yasuhiko Jikei University,School of Medicine,Department of Orthopaedic Surgery,Research Assistant, 医学部, 助手 (10234907)
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| Project Period (FY) |
1998 – 1999
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| Keywords | Chondroadherin / Human bone / bone metabolic marker |
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| Research Abstract |
In this study, we isolated 36 and 37 kDa proteins from human bone. The primary structure of these proteins were identical with that of previously reported CHAD cloned from human chondrocyte. However, the phosphorylation existed only in bone CHAD and the glycosylation pattern was distinctly different from that described for bovine cartilage and bone. This differences could be ascribed to species variation, or more likely the existence of tissue specific isoforms that differ in their phospholylation and glycosylation pateern. It is postulated that the specific functions of CHAD in cartilage and bone are dependent on the unique structure of the protein, and the posttransitional modifications have especially been assigned a significant importance. Human bone CHAD has specific affinity to type I collagen among several kinds of matrix protein and has high affinity to type I collagen similar to that of BSP, with a dissociation constant of 0.5mM. It is suggested that CHAD may mediate the attachment of bone cells to collagen and modulation of fibrogenesis of collagen. Among the CNBr peptides of type I collagen, α1CB8 which is corresponding to helix region of collagen provided the binding site for CHAD. However, the binding capacity of the denatured collagen, such as Hd and CNBr peptides, was apparently less than the native collagen for CHAD. The fact indicates that helical structure of native collagen as well as primary structure of α1CB8 is important for interaction between CHAD and collagen.
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