| Project/Area Number |
04454376
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Orthopaedic surgery
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
YAMAMURO Takao Kyoto University, Medicine, Professor, 医学部, 教授 (00088527)
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| Co-Investigator(Kenkyū-buntansha) |
SHIMIZU Katsuji Kyoto University, Medicine Lecturer, 医学部, 講師 (90170969)
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| Project Period (FY) |
1992 – 1993
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| Project Status |
Completed (Fiscal Year 1993)
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| Budget Amount *help |
¥6,800,000 (Direct Cost: ¥6,800,000)
Fiscal Year 1993: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1992: ¥6,100,000 (Direct Cost: ¥6,100,000)
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| Keywords | calpain I / calpastatin / chemonucleolysis / Chemonucleolysis / 椎間板 / プロテオグリャン |
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| Research Abstract |
Calpain I is a clcium-dependent cystein proteinase that has been recently shown to degrade proteoglycan in vitro. The authors injected calpain I, which was purified from human red blood cells, into the intervertebral discs of rabbits. Roentgenograms showed disc space narrowing 1 week after the injection. Histologically, proteoglycan of the nucleus pulposus and anulus fibrosus decreased and notochordal cells in the nucleus pulposus almost disappeared. Biochemical data of the nucleus pulposus showed that the amounts of smaller proteoglycans increased 1 and 4 weeks after the injection. Eight weeks after the injection, histologic and boichemical data showed recovery compared with the data 1 week after injection. These findings show that calpain I is as potent as enzyme as chondroitinase ABC and has milder chemonucleolytic action than chymopapain. Regarding its possible clinical application, autogenous clapain I as purified from the patient's own red blood cells may have advantages over chymopapain and chondroitinase ABC in that it will prevent anaphylactic reaction.
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