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- W1602553462 endingPage "150" @default.
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- W1602553462 abstract "Insulin, like most secreted proteins, enters the secretory pathway at the level of the endoplasmic reticulum (ER), being directed there by the hydrophobic leader (signal) sequence corresponding to the first 16 amino acids of the preproinsulin structure. Once in the lumen of the ER, the three disulphide bonds are formed and the leader sequence is removed by signal peptidases to form proinsulin. Some of the fundamentals of the regulation of the expression of these proteins have been elucidated, both in the case of proinsulin conversion and for other prohormones that may undergo more complex differential processing. Nascent secretory granules are characteristically membrane-bounded spherical organelles enveloping an electron dense core. Proteins travel between compartments via vesicular intermediates that bud from the donor compartment and fuse with the acceptor compartment. Formation of vesicles is controlled by a complex molecular machinery, many aspects of which are common to numerous intracellular transport steps. Major advances in identifying and characterizing the components involved have come from two complementary approaches; the development of cell-free transport assays, on the one hand, and yeast genetics, on the other. The finding that a number of genes defining secretory (sec) mutants in yeast represent proteins involved in constitutive and regulated secretion in mammalian cells illustrates the high degree of conservation of many underlying principles of vesicular transport." @default.
- W1602553462 created "2016-06-24" @default.
- W1602553462 creator A5016247863 @default.
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- W1602553462 creator A5061340857 @default.
- W1602553462 creator A5089667935 @default.
- W1602553462 date "1999-01-01" @default.
- W1602553462 modified "2023-09-24" @default.
- W1602553462 title "Proinsulin Processing and Insulin Storage" @default.
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