Download e-book for iPad: Biology of the Lysosome by John B. Lloyd (auth.), John B. Lloyd, Robert W. Mason (eds.)

By John B. Lloyd (auth.), John B. Lloyd, Robert W. Mason (eds.)

From a preview of a prior volume:
`The heterogeneity of topics...is very bold, and the result's, total, profitable as a result prime quality of the person contributions...highly recommended.'
Amercian Scientist.

`Well written and timely...of curiosity to all these all in favour of the research of this organelle and for these attracted to the clinical and genetic points of lysosomal disorders...recommended.'
Journal of clinical Genetics

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1994a). The removal of propeptides results in conversion to active single-chain forms of the enzymes that are further processed to two-chain forms. , 1993). However, in a recent report it was shown that mutation at the autocatalytic site in procathepsin D resulted in loss of autoactivation in vitro but did not interfere with the transport to Iysosomes and its normal processing to the mature form when the mutant cathepsin D was expressed in Ltk:- cells (Richo and Conner, 1994). The data suggest that the autocatalytic form of cathepsin D (pseudocathepsin D) found in vitro is not a normal proteolytic intermediate of cathepsin D in vivo.

1994). , Thomas Braulke 34 1994). , 1994). 2. Heterotrimeric G-Proteins The large G-proteins composed of a (39-52 kDa), ~ (35-36 kDa), and y (7-10 kDa) subunits are classically involved in transmembrane signaling of ligandactivated receptors resulting in either intracellular second messenger formation or regulation of ion channel function (Conklin and Bourne, 1993). In the absence of receptor ligands the a subunit is occupied by GOP while ligand binding stimulates the activation of trimeric G-proteins by catalyzing a GOP/GTP exchange and causes dissociation into a and ~y subunits.

Since various proteins with different subcellular localization are reported to be translocated to the plasma membrane in response to insulin or IGFs, it appears that these agents generally enhance the fusion between transport vesicles and increase their externalization rate. The underlying mechanisms regulating the distribution of MPRs are still unclear, but it is likely that common components and regulatory processes of vesicular transport are involved (see Section 5 for details). , 1994; Komer and Braulke, 1996).

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