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By Margaret A. Shupnik

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Additional info for Gene Engineering in Endocrinology (Contemporary Endocrinology)

Example text

The insulin-responsive glucose transporter GLUT4 is expressed at high levels almost exclusively in classical insulin targets such as muscle and adipose tissue (for a review see ref. 59). Insulin stimulates increased glucose transport in these tissues by causing the redistribution of GLUT4 from an intracellular pool to the cell surface, where it acts as a facilitative transporter to enhance entry of glucose into the cell (60–62). This redistribution of GLUT4 is due largely to insulin increasing the rate of exocytosis of GLUT4 (insulin may also have a minor effect in decreasing endocytosis of GLUT4) (63–65).

Insulin stimulates increased glucose transport in these tissues by causing the redistribution of GLUT4 from an intracellular pool to the cell surface, where it acts as a facilitative transporter to enhance entry of glucose into the cell (60–62). This redistribution of GLUT4 is due largely to insulin increasing the rate of exocytosis of GLUT4 (insulin may also have a minor effect in decreasing endocytosis of GLUT4) (63–65). Although the tissue-specific distribution of GLUT4 and the effects of insulin on the subcellular localization of GLUT4 have been known for some time, elucidation of metabolic insulin signaling pathways has lagged behind other areas of insulin signal transduction for several reasons.

24. Sun XJ, Wang LM, Zhang Y, Yenush L, Myers MG Jr, Glasheen E, Lane WS, Pierce JH, White MF. Role of IRS-2 in insulin and cytokine signalling. Nature 1995; 377:173–177. 25. Lavan BE, Lane WS, Lienhard GE. The 60-kDa phosphotyrosine protein in insulin-treated adipocytes is a new member of the insulin receptor substrate family. J Biol Chem 1997; 272:11,439–11,443. 26. Holgado-Madruga M, Emlet DR, Moscatello DK, Godwin AK, Wong AJ. A Grb2-associated docking protein in EGF- and insulin-receptor signalling.

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