Lipid transfer particle mediates the delivery of diacylglycerol from lipophorin to fat body in larval Manduca sexta
| Autor: | Michael A. Wells, Hwa Kyung Yun, Lilian E. Canavoso, Zeina E. Jouni |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
Lipoproteins
Suramin Fat Body lipoprotein lipase developmental stages QD415-436 Tritium Endocytosis Biochemistry Diglycerides chemistry.chemical_compound Endocrinology Manduca medicine Animals endocytosis Lipase Incubation Diacylglycerol kinase Lipoprotein lipase biology urogenital system Biological Transport Cell Biology biology.organism_classification chemistry Manduca sexta Larva biology.protein lipids (amino acids peptides and proteins) Ammonium chloride triacylglycerol medicine.drug |
| Zdroj: | Journal of Lipid Research, Vol 45, Iss 3, Pp 456-465 (2004) |
| ISSN: | 0022-2275 |
| Popis: | This work analyzed the process of lipid storage in fat body of larval Manduca sexta, focusing on the role of lipid transfer particle (LTP). Incubation of fat bodies with [(3)H]diacylglycerol-labeled lipophorin resulted in a significant accumulation of diacylglycerol (DAG) and triacylglycerol (TAG) in the tissue. Transfer of DAG to fat body and its storage as TAG was significantly inhibited (60%) by preincubating the tissue with anti-LTP antibody. Lipid transfer was restored to control values by adding LTP to fat body. Incubation of fat body with dual-labeled DAG lipophorin or its treatment with ammonium chloride showed that neither a membrane-bound lipoprotein lipase nor lipophorin endocytosis is a relevant pathway to transfer or to storage lipids into fat body, respectively. Treatment of fat body with suramin caused a 50% inhibition in [(3)H]DAG transfer from lipophorin. Treatment of [(3)H]DAG-labeled fat body with lipase significantly reduced the amount of [(3)H]DAG associated with the tissue, suggesting that the lipid is still on the external surface of the membrane. Whether this lipid represents irreversibly adsorbed lipophorin or a DAG lipase-sensitive pool is unknown. Nevertheless, these results indicate that the main pathway for DAG transfer from lipophorin to fat body is via LTP and receptor-mediated processes. |
| Databáze: | OpenAIRE |
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