Effect of praseodymium on drug metabolism in rat liver smooth and rough endoplasmic reticulum

1980 ◽  
Vol 36 (7) ◽  
pp. 860-861 ◽  
Author(s):  
P. Arvela ◽  
B. v. Lehmann ◽  
O. Grajewski ◽  
E. Oberdisse
Keyword(s):  
Endoplasmic Reticulum ◽  
Drug Metabolism ◽  
Rat Liver ◽  
Rough Endoplasmic Reticulum

The polypeptides of rat liver nuclear envelope. II. Comparison of rat liver nuclear membrane polypeptides with those of the rough endoplasmic reticulum

1980 ◽  
Vol 43 (1) ◽  
pp. 269-277
Author(s):  
J.C. Richardson ◽  
A.H. Maddy
Keyword(s):  
Endoplasmic Reticulum ◽  
Rat Liver ◽  
Rough Endoplasmic Reticulum ◽  
Nuclear Membrane ◽  
Relative Proportion ◽  
Membrane System ◽  
Membrane Systems ◽  
Nuclear Membranes ◽  
Cytoplasmic Surface ◽  
Triton X

Nuclear envelopes are separated into pore-lamina and membrane sub-fractions by extraction in 2.0% Triton X-100 followed by pelleting of the pore-laminae. The polypeptides of these subfractions are then compared with those from isolated rough endoplasmic reticulum. The dispositions of individual polypeptides in the cytoplasmic surface of nuclear envelopes and rought endoplasmic reticulum were studied by lactoperoxidase-catalysed iodination. These studies show that although the nuclear membranes exhibit several homologies with the Triton-soluble polypeptides of the rough endoplasmic reticulum the relative proportion of individual polypeptides within the two systems are very largely different. The cytoplasmic surfaces of the 2 membrane systems show only 2 obvious homologies at 105 000 and 15 000 mol. wt and the overall impression is that, at least in rat liver, the outer nuclear membrane is very substantially differentiated from rough endoplasmic reticulum. It is concluded that the nuclear membranes may not be regarded as a mere continuum of the endoplasmic reticulum, but should be seen as a highly specialized membrane system in their own right.

scholarly journals ULTRASTRUCTURAL VARIATIONS IN N,N'-BIS(4-AMINOPHENYL)-N,N'-DIMETHYLETHYLENEDIAMINE (BED) OXIDASE LOCALIZATION IN RAT LIVER AND PAROTID GLAND WITH VARIATION IN LENGTH OF FIXATION

1972 ◽  
Vol 20 (12) ◽  
pp. 1024-1030 ◽  
Author(s):  
W. ALLEN SHANNON ◽  
ARNOLD M. SELIGMAN
Keyword(s):  
Endoplasmic Reticulum ◽  
Parotid Gland ◽  
Rat Liver ◽  
Rough Endoplasmic Reticulum ◽  
Secretory Granules ◽  
Terminal Oxidase ◽  
Outer Compartment ◽  
Fixation Reaction

The localization and reactivity of a terminal oxidase which oxidizes N,N'-bis(4-amino-phenyl)-N,N'-dimethylethylenediamine (BED) were studied in rat liver and parotid gland after varying the concentration of formaldehyde fixative and the length of fixation. Reaction product was observed in mitochondrial outer compartments, smooth elements of rough endoplasmic reticulum, some Golgi lamellae, perinuclear membranes and cytoplasmic membranous structures often associated with mitochondria. A reaction also occurred in the limiting membrane and, to some degree, in the material comprising the secretory granules of the parotid. The reaction in the mitochondrial outer compartment was extremely formaldehyde-sensitive. Controls in which diaminobenzidine (DAB) was substituted for BED showed reaction only in mitochondrial cristae and outer compartments, whereas controls without either reagent showed no reactivity.

scholarly journals Detection of GTP-binding proteins in purified derivatives of rough endoplasmic reticulum

1989 ◽  
Vol 262 (2) ◽  
pp. 497-503 ◽  
Author(s):  
J Lanoix ◽  
L Roy ◽  
J Paiement
Keyword(s):  
Endoplasmic Reticulum ◽  
Rat Liver ◽  
Rough Endoplasmic Reticulum ◽  
Binding Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Cell Types ◽  
Electrophoretic Analysis ◽  
Gtp Binding Proteins ◽  
Gtp Binding ◽  
Dog Pancreas

As a first step in determining the molecular mechanism of membrane fusion stimulated by GTP in rough endoplasmic reticulum (RER), we have looked for GTP-binding proteins. Rough microsomes from rat liver were treated for the release of ribosomes, and the membrane proteins were separated by SDS/polyacrylamide-gel electrophoresis. The polypeptides were then blotted on to nitrocellulose sheets and incubated with [alpha-32P]GTP [Bhullar & Haslam (1987) Biochem. J. 245, 617-620]. A doublet of polypeptides (23 and 24 kDa) was detected in the presence of 2 microM-MgCl2. Binding of [alpha-32P]GTP was blocked by 1-5 mM-EDTA, 10-10,000 nM-GTP or 10 microM-GDP. Either guanosine 5′-[gamma-thio]triphosphate or guanosine 5′-[beta gamma-imido]triphosphate at 100 nM completely inhibited binding, but ATP, CTP or UTP at 10 mciroM did not. Pretreatment of microsomes by mild trypsin treatment (0.5-10 micrograms of trypsin/ml, concentrations known not to affect microsomal permeability) led to inhibition of [alpha-32P]GTP binding, suggesting a cytosolic membrane orientation for the GTP-binding proteins. Two-dimensional gel-electrophoretic analysis revealed the 23 and 24 kDa [alpha-32P]GTP-binding proteins to have similar acid isoelectric points. [alpha-32P]GTP binding occurred to similar proteins of rough microsomes from rat liver, rat prostate and dog pancreas, as well as to a 23 kDa protein of rough microsomes from frog liver, but occurred to distinctly different proteins in a rat liver plasma-membrane-enriched fraction. Thus [alpha-32P]GTP binding has been demonstrated to two low-molecular-mass (approx. 21 kDa) proteins in the rough endoplasmic reticulum of several varied cell types.

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