IDENTIFICATION OF SPECIES DIFFERENCES IN LIPOPROTEIN LIPASE AND MANIPULATION OF FAT DEPOSITION BY MONOCLONAL ANTIBODY FOR THE LIPASE IN CHICKENS
| Project/Area Number |
05454110
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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 |
Applied animal science
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| Research Institution | TOHOKU UNIVERSITY |
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Principal Investigator |
AKIBA Yukio FACULTY OF AGRICULTURE,TOHOKU UNIVERSITY,PROFESSOR, 農学部, 教授 (30005631)
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| Project Period (FY) |
1993 – 1995
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| Project Status |
Completed (Fiscal Year 1995)
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| Budget Amount *help |
¥6,800,000 (Direct Cost: ¥6,800,000)
Fiscal Year 1995: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1994: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1993: ¥4,800,000 (Direct Cost: ¥4,800,000)
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| Keywords | LIPOPROTEIN LIPASE / OBESITY / FAT DEPOSITION / SPECIES SPECIFICITY / MONOCLONAL ANTIBODY / CHICKEN / LIPOPROTEIN BREAKDOWN / 脂質代謝 |
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| Research Abstract |
Obesity (excessive fat deposition) is a metabolic disorder common in human and animals. Lipoprotein lipase (LPLase) in adipose tissues plays a major role in determining fat deposition in chickens. Present study was undertaken to identify species differences in LPLase in chickens and mammals and to explore the possible ways to manipulate the excess fat deposition by administration of the monoclonal antibodies of LPLase.
(1) Hydolysis of lipoproteins by LPLase was markedly inhibited by Triton WR-1339 in rats but inhibited to a small extent in chickens, suggesting existence of species differences in the LPLase.
(2) Glycerol was identified for an excellent reagent to stabilize LPLase activity, because LPLase was sensitive to the decomposition. LOLases of chickens and rats were purified with high specific activity by applying hydroxyapatite column.
(3) Purified LPLase of chickens differed from that of rats in terms of Km, Vm and kinetics on inhibition by Triton WR-1339.
(4) Ultrafiltration and Mono Q columns for apoproteins yielded a purified Apo C-II of chickens. Activation of LPLase by the Apo C-II was potent in chickens more than in rats.
(5) Purified LPLase was immunologically challenged to mice to produce the hybridomas and 24 clones characterized with high affinity to LPLase were identified. Three monoclonal antibodies out of 24 clones demonstrated marked inhibitory activity on the lipoprotein hydrolysis by LPLase.
(6) Intraperitoneal administration of the monoclonal antibody for LPLase resulted in an inhibition by 20% of adipose tissue LPLase activity and a marked increase in plasma triglyceride concentration in chickens, suggesting that the monoclonal antibody administration may be a possible procedure to retard excessive fat deposition in animals.
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Report
(4 results)
Research Products
(22 results)
