Golgi apparatus enzymes

Warburton, M. J., and Wynn, C. H., The effect of intralysosomal sucrose storage on the turnover of hamster fibroblast lysosomal and Golgi-apparatus enzymes. Biochem. J. 158,401-407 (1976). 

The enzymes involved are located in various subcompartments of the Golgi apparatus. 

Man 6-P receptors, located in the Golgi apparatus, bind the Man 6-P residue of these enzymes and direct them to the lysosomes. Fibroblasts from patients with I-cell disease (see below) are severely deficient in the activity of the GIcNAc phosphotransferase. 

Like other cells, a neuron has a nucleus with genetic DNA, although nerve cells cannot divide (replicate) after maturity, and a prominent nucleolus for ribosome synthesis. There are also mitochondria for energy supply as well as a smooth and a rough endoplasmic reticulum for lipid and protein synthesis, and a Golgi apparatus. These are all in a fluid cytosol (cytoplasm), containing enzymes for cell metabolism and NT synthesis and which is surrounded by a phospholipid plasma membrane, impermeable to ions and water-soluble substances. In order to cross the membrane, substances either have to be very lipid soluble or transported by special carrier proteins. It is also the site for NT receptors and the various ion channels important in the control of neuronal excitability. 

The possibility that the initial degree of methyl-esterification might be controlled by the properties of the methyltransferase enzymes was examined partial characterisation of these enzymes in suspension-cultured cells of fiax. Pectin methyltransferases beii enzymes characteristic of the Golgi apparatus [22], microsomes were fiactionated daily for ten days from suspension-cultured flax cells and incubated in the presence of C-SAM, the universal donor of methyl groups. 

Fragments of the endoplasmic reticulum and the golgi apparatus produce enzymes and store calcium. 

Assay of Inosine-5-diphosphatase (IDPase) EC 3.6.1.6, Presumed Marker Enzyme for Golgi Apparatus Conclusions References... 

These cells are relatively undifferentiated and have a large nucleus, distinguishable nucleolus but few, if any, cytoplasmic granules. Myeloblasts arise from a precursor pool of stem cells, and both the rough endoplasmic reticulum and the Golgi apparatus stain for peroxidase, indicating that this enzyme is beginning to be synthesised. This cell type is capable of proliferation. 

Figure 1 The mode of action for bacterial AB-type exotoxins. AB-toxins are enzymes that modify specific substrate molecules in the cytosol of eukaryotic cells. Besides the enzyme domain (A-domain), AB-toxins have a binding/translocation domain (B-domain) that specifically interacts with a cell-surface receptor and facilitates internalization of the toxin into cellular transport vesicles, such as endosomes. In many cases, the B-domain mediates translocation of the A-domain into the cytosol by pore formation in cellular membranes. By following receptor-mediated endocytosis, AB-type toxins exploit normal vesicle traffic pathways into cells. One type of toxin escapes from early acidified endosomes (EE) into the cytosol, thus they are referred to as short-trip-toxins . In contrast, the long-trip-toxins take a retrograde route from early endosomes (EE) through late endosomes (LE), trans-Golgi network (TGN), and Golgi apparatus into the endoplasmic reticulum (ER) from where the A-domains translocate into the cytosol to modify specific substrates.

Lysosomal enzymes are glycosylated and modified in a characteristic way. Most importantly, when they arrive in the Golgi apparatus, specific mannose residues in their oligosaccharide chains are phosphorylated. This phosphorylation is the critical event that removes them Corn the secretion pathway and directs them to lysosomes. Genetic defects affecting this phosphorylation produce I-ceU disease in which lysosomal enzymes are released into the ejctracellular space, and inclusion bodies accumulate in the cell, compromising its function. 

It seems likely that the enzyme complexes for hemicelluloses, pectins and cellulose are constructed, at least in part, on the endoplasmic reticulum and then transferred to the Golgi apparatus, where they are modified and sorted so that they can be segregated within the compartments of the Golgi cisternae (30,31). The complex for cellulose synthesis is not normally active within the Golgi apparatus and it is transported to active sites at the plasma membrane (1). The hemicelluloses and pectins are formed within vesicles and cisternae of the Golgi apparatus and the vesicles are transported to the plasma membrane, where fusion occurs and the polysaccharides are packed into the wall (1). It is not known whether particular polysaccharides such as the xylans of the hemicellulose and the arabinogalactans of the pectins are transported in separate vesicles or together in one vesicle. Nor is it known if the complex for cellulose synthesis is transported by vesicles which carry hemicellulose and pectin polysaccharides. 

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