Interaction of rat hormone-sensitive lipase with adipocyte lipid-binding protein
Interaction of rat hormone-sensitive lipase with adipocyte lipid-binding protein
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DOI：
10.1073/pnas.96.10.5528
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发表时间：
1999-05-11
影响因子：
11.1
通讯作者：
Kraemer, FB
中科院分区：
文献类型：
--
作者：
Shen, WJ;Sridhar, K;Kraemer, FB
激素敏感脂肪酶（HSL）是一种细胞质中性脂肪酶，作为脂肪组织中游离脂肪酸动员的限速酶。通过使用酵母双杂交系统来检测HSL与其他细胞蛋白的潜在相互作用，提供了证据证明RSL与脂肪细胞脂质结合蛋白（ALBP）直接相互作用，ALBP是细胞内脂质结合蛋白家族的成员，可以结合脂肪酸、类维生素a和其他疏水配体。过表达HSL的中国仓鼠卵巢（CHO）细胞提取物和大鼠脂肪组织提取物中的HSL。最后，用抗hsl抗体免疫沉淀的大鼠脂肪组织免疫复合物中记录了ALBP的存在。HSL- albp相互作用映射到HSL的n端300-aa区域，该区域与c端催化区域不同。这些结果表明hsl衍生的脂肪酸与ALBP结合，促进疏水脂质的细胞内运输。
Hormone-sensitive lipase (HSL) is a cytosolic neutral lipase that functions as the rate-limiting enzyme for the mobilization of free fatty acids in adipose tissue. By using the yeast two-hybrid system to examine the potential interaction of HSL with other cellular proteins, evidence is provided to demonstrate a direct interaction of RSL with adipocyte lipid-binding protein (ALBP), a member of the family of intracellular lipid-binding proteins that binds fatty acids, retinoids, and other hydrophobic ligands, The interaction was demonstrated in vitro by the binding of ALBP to HSL translated in vitro, to HSL in extracts of HSL overexpressing Chinese hamster ovary (CHO) cells, and to HSL in extracts of rat adipose tissue. Finally, the presence of ALBP was documented in immune complexes from rat adipose tissue immunoprecipitated with anti-HSL antibodies. The HSL-ALBP interaction was mapped to an N-terminal 300-aa region of HSL that is distinct from the C-terminal catalytic domain. These results suggest that HSL-derived fatty acids are bound by ALBP to facilitate intracellular trafficking of hydrophobic lipids.