scholarly journals Immunological Cross-reactivity between Plasma Membrane and Endoplasmic Reticulum of Ehrlich Ascites Carcinoma

Nature ◽  
1967 ◽  
Vol 216 (5111) ◽  
pp. 182-182 ◽  
Author(s):  
DONALD F. HOELZL WALLACE ◽  
VLASTA VLAHOVIC
1966 ◽  
Vol 30 (3) ◽  
pp. 601-621 ◽  
Author(s):  
Donald F. Hoelzl Wallach ◽  
Virendra B. Kamat ◽  
Mitchell H. Gail

Specific turbidities, densities, and refractive indices of fragments of plasma membrane (PM) and endoplasmic reticulum (ER) from Ehrlich ascites carcinoma have been measured. A spherical shell model of specified dimensions and refractive index was established for PM fragments. The ionic composition of the dispersion medium was varied systematically. Increases in Γ/2 caused increases in the turbidity of both PM and ER suspensions, the greatest effects being observed with Ca2+ and Mg2+. In the case of PM this effect is attributable mainly to aggregation, whereas "structural" changes account for most of the turbidity increase with ER. The pH was also varied systematically to obtain pH- density and turbidity profiles and to establish the isoelectric pH of the two membrane types (PM—3.6; ER—4.35). Turbidity was maximum at "isoelectric" pH, which corresponds in each case to the region of minimum charge on the particle surfaces. Both PM and ER show large increases of density at the "isoelectric" pH, but only ER shows substantial structurally based turbidity increase under these conditions. Both PM and ER show operation of electrostatic attractions near "isoelectric" pH. PM has been shown to have ionically distinctive inner and outer surfaces while ER shows no such dissymmetry. The necessary theoretical background for interpretation of turbidity and density measurements is included, as well as a discussion of the limitations of our conclusions and the biological importance of our results.


1991 ◽  
Vol 147 (1) ◽  
pp. 182-190 ◽  
Author(s):  
Alexei A. Bogdanov ◽  
Larisa V. Gordeeva ◽  
Boris A. Baibakov ◽  
Leonid B. Margolis ◽  
Vladimir P. Torchilin

Author(s):  
M. A. Hayat

Potassium permanganate has been successfully employed to study membranous structures such as endoplasmic reticulum, Golgi, plastids, plasma membrane and myelin sheath. Since KMnO4 is a strong oxidizing agent, deposition of manganese or its oxides account for some of the observed contrast in the lipoprotein membranes, but a good deal of it is due to the removal of background proteins either by dehydration agents or by volatalization under the electron beam. Tissues fixed with KMnO4 exhibit somewhat granular structure because of the deposition of large clusters of stain molecules. The gross arrangement of membranes can also be modified. Since the aim of a good fixation technique is to preserve satisfactorily the cell as a whole and not the best preservation of only a small part of it, a combination of a mixture of glutaraldehyde and acrolein to obtain general preservation and KMnO4 to enhance contrast was employed to fix plant embryos, green algae and fungi.


Author(s):  
Shaikh Shohidul Islam ◽  
Md. Rezaul Karim ◽  
A. K. M. Asaduzzaman ◽  
A. H. M. Khurshid Alam ◽  
Zahid Hayat Mahmud ◽  
...  

2021 ◽  
Author(s):  
Noemi Ruiz-Lopez ◽  
Jessica Pérez-Sancho ◽  
Alicia Esteban del Valle ◽  
Richard P Haslam ◽  
Steffen Vanneste ◽  
...  

Abstract Endoplasmic reticulum-plasma membrane contact sites (ER-PM CS) play fundamental roles in all eukaryotic cells. Arabidopsis thaliana mutants lacking the ER-PM protein tether synaptotagmin1 (SYT1) exhibit decreased plasma membrane (PM) integrity under multiple abiotic stresses such as freezing, high salt, osmotic stress and mechanical damage. Here, we show that, together with SYT1, the stress-induced SYT3 is an ER-PM tether that also functions in maintaining PM integrity. The ER-PM CS localization of SYT1 and SYT3 is dependent on PM phosphatidylinositol-4-phosphate and is regulated by abiotic stress. Lipidomic analysis revealed that cold stress increased the accumulation of diacylglycerol at the PM in a syt1/3 double mutant relative to wild type while the levels of most glycerolipid species remain unchanged. Additionally, the SYT1-green fluorescent protein (GFP) fusion preferentially binds diacylglycerol in vivo with little affinity for polar glycerolipids. Our work uncovers a SYT-dependent mechanism of stress adaptation counteracting the detrimental accumulation of diacylglycerol at the PM produced during episodes of abiotic stress.


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