Characterization of lipoprotein lipase storage vesicles in 3T3-L1 adipocytes.

Lipoprotein lipase (LPL) is a secreted triglyceride lipase involved in the clearance of very-low-density lipoproteins and chylomicrons from circulation. LPL is expressed primarily in adipose and muscle tissues and transported to the capillary lumen. LPL secretion is regulated by insulin in adipose tissue; however, few studies have examined the regulatory and trafficking steps involved in secretion. Here, we describe the intracellular localization and insulin-dependent trafficking of LPL in 3T3-L1 adipocytes. We compared LPL trafficking to the better characterized trafficking pathways taken by leptin and GLUT4 (also known as SLC2A4). We show that the LPL trafficking pathway shares some characteristics of these other pathways, but that LPL subcellular localization and trafficking are distinct from those of GLUT4 and leptin. LPL secretion occurs slowly in response to insulin and rapidly in response to the Ca2+ ionophore ionomycin. This regulated trafficking is dependent on Golgi protein kinase D and the ADP-ribosylation factor GTPase ARF1. Together, these data give support to a new trafficking pathway for soluble cargo that is active in adipocytes.