Disease relevance of GLG1

• Isolation and characterization of chicken liver and hepatoma Mc-29 endoplasmic reticulum and Golgi apparatus membranes and biosynthesis of their glycoconjugates [1].
• Labelling of an intermediate saccule of the Golgi apparatus and of parts of the endoplasmic reticulum by a lectin (soybean agglutinin) in the chick ciliary ganglion [2].

High impact information on GLG1

• Apoprotein A1 from the Golgi apparatus, obtained by immunoprecipitation, contained sixfold more nascent lipids than did that from the endoplasmic reticulum [3].
• The swelling of the Golgi apparatus induced by X537A was reversible in the systems examined for reversibility: vascular smooth muscle and cultured chick heart [4].
• Myelin figures were common in the Golgi apparatus vacuolated by X537A [4].
• Possible role of the Golgi apparatus in the assembly of very low density lipoprotein [5].
• Expression of the cysteine-rich fibroblast growth factor (FGF) receptor (CFR) in COS-1 cells strongly inhibits the secretion of co-expressed FGF3 [6].

Biological context of GLG1

• These findings suggest that subunit assembly occurs in the Golgi apparatus and that phosphorylation/dephosphorylation mechanisms play a role in the control of AChR subunit assembly [7].
• While over 20 intrinsic proteins of the Golgi apparatus have been identified and sequenced, there is no information on their developmental history, i.e., whether all Golgi proteins are expressed simultaneously or whether there is a hierarchical or stage-specific order of their expression during embryonic development [8].
• The levels of CFR transcripts were high during the proliferation and the subsequent differentiation phases of retinal neurogenesis, reached a maximum around E11 during the onset of the major period of retinal cell death, and then declined progressively [9].
• In prolonged primary cell cultures of chicken embryo retina, CFR expression showed a similar down-regulation to that seen with increasing age in vivo [9].
• Intracellular immunoreactivity was present in the granular and agranular endoplasmic reticulum, Golgi apparatus and in lysosomes, representing the sites of synthesis, glycosylation and degradation of the protein [10].

Anatomical context of GLG1

• Significantly less time was required for transport through the Golgi apparatus and insertion in the plasma membrane [11].
• Cysteine-rich fibroblast growth factor receptor alters secretion and intracellular routing of fibroblast growth factor 3 [6].
• The released CFR is associated with the extracellular matrix through its affinity for glycosaminoglycans [6].
• Based on these results, we discuss the hypothesis that a selective CV-mediated pathway exists in developing skeletal muscle cells for the transport of CSQ from the early/intermediate Golgi apparatus to the SR [12].
• Further, the results of subcellular fractionation of oviduct membranes suggest that N-acetylgalactosaminyl:polypeptide transferase is localized primarily in membranes derived from the smooth endoplasmic reticulum and Golgi apparatus [13].

Associations of GLG1 with chemical compounds

• The cysteine-rich FGF receptor (CFR) is a 150-kD membrane-associated glycoprotein that specifically binds FGFs [14].
• The rate of AChR assembly is decreased by metabolic inhibitors and by monensin, an ionophore that impairs the Golgi apparatus [7].
• In regard to a progressive increase in the expression of their ligands during retinal development, we suggest that CFR may have a role distinct from that of the tyrosine kinase FGF receptors during retinogenesis [9].
• Golgi apparatus fractions were prepared by flotation of microsomes, obtained from the same homogenate as the low-speed pellet, in a discontinuous sucrose gradient [15].
• At the ultrastructural level, GABA treatment also led to an increased density of neurotubules, rough endoplasmic reticulum (RER), Golgi apparatus, coated vesicles, and other vesicles [16].

Physical interactions of GLG1

• GH binding to its receptor leads to internalization of the GH-GHR complex to the Golgi apparatus [17].

Regulatory relationships of GLG1

• During the last week of incubation, which is the final third of the incubation period, the digestion seemed to progress rapidly in the yolk drops, which came to resemble lipolysosomes; lipoprotein production became active as expressed by an enlarged Golgi apparatus [18].
• Monensin, which is known to cause dilatation of the Golgi apparatus and to inhibit sulfation of proteoglycan, was found to affect the release of the sulfotransferases [19].

Other interactions of GLG1

• Intracellular IGF-I was observed in the endosomes, Golgi apparatus, and lysosomes of epithelial cells, in addition, it was shown for the first time that IGF-I was translocated to the nucleus of epithelial cells [20].
• Immuno-electron microscopy reveals that somatostatin-like immunoreactivity is localized to Golgi apparatus and large dense core vesicles [21].
• At the electron microscopic level, acetylcholinesterase activity was found in the nuclear envelope, granular endoplasmic reticulum and the Golgi apparatus of the neurons [22].

Analytical, diagnostic and therapeutic context of GLG1

• By using a column retention assay and affinity chromatography, we demonstrate that at physiological salt concentrations FGF3 binds with strong affinity to CFR in vivo and in vitro [6].
• Tethers are nanocylinders of lipid bilayer membrane, arising in situations ranging from micromanipulation experiments on synthetic vesicles to the formation of dynamic tubular networks in the Golgi apparatus [23].
• The expression of the chicken cysteine-rich fibroblast growth factor receptor (CFR) during organogenesis and specifically during retina formation was studied by Northern blotting and a sensitive in situ hybridization [9].
• A quantitative evaluation of the positional changes of the Golgi apparatus during the invagination of the lens placode and the presumptive neural retina of the chick embryo was carried out by silver impregnation [24].
• Electron microscopy following incubation of tissue sections with the antibody and the protein A-gold complex revealed specific immunolabeling over the rER and Golgi apparatus of osteoblasts and over those areas of bone matrix containing Ca and P as determined by electron probe x-ray microanalysis [25].

References