BIOSYNTHETIC ROUTE OF LOCUST APOLIPOPHORIN-III ISOFORMS

被引:13
作者
WEERS, PMM
VANBAAL, J
VANDOORN, JM
ZIEGLER, R
VANDERHORST, DJ
机构
[1] UNIV ARIZONA, DEPT BIOCHEM, TUCSON, AZ 85721 USA
[2] UNIV ARIZONA, CTR INSECT SCI, TUCSON, AZ 85721 USA
来源
BIOLOGICAL CHEMISTRY HOPPE-SEYLER | 1993年 / 374卷 / 09期
关键词
APOPROTEIN; LIPOPHORIN; LIPOPROTEIN; LOCUST FAT BODY; INSECT FLIGHT;
D O I
10.1515/bchm3.1993.374.7-12.863
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Insect apolipophorin III (apoLp-III) plays a key role in the enhanced diacylglycerol transport during insect flight. For apoLp-III of the migratory locust, two different isoforms have been described (apoLp-IIIa and -b), displaying different N-termini and isoelectric points; each of the isoforms is however equally well capable to perform its function in lipid transport. In the present report the biosynthetic route of the apoLp-III isoforms is elucidated. Immunoprecipitation of media from in vitro fat body incubations and analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis demonstrated that the locust fat body synthesized and secreted apoLp-III. ApoLp-III levels in the hemolymph showed that in young adults, apoLp-III concentrations were only very low (1-3 mg/ml). During adult maturation, however, the apoLp-III concentration increased rapidly to approximately 17 mg/ml. During apoLp-III elevation, the apoLp-IIIa:-b ratio remained equal or in the favour of the a-isoform, while in adults from approximately 12 days after adult ecdysis apoLp-IIIb was the most abundant isoform. Analysis of the protein by native polyacrylamide gel electrophoresis showed that only the apoLp-IIIa form was secreted. Injection of radiolabeled apoLp-IIIa into the hemolymph of adult locusts resulted in a slow conversion into apoLp-IIIb.
引用
收藏
页码:863 / 869
页数:7
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