scholarly journals The fluidity of normal and virus-transformed cell plasma membrane

1976 ◽  
Vol 154 (3) ◽  
pp. 561-566 ◽  
Author(s):  
K J. Micklem ◽  
R M. Abra ◽  
S Knutton ◽  
J M Graham ◽  
C A Pasternak
Keyword(s):  
Plasma Membrane ◽  
Phospholipid Composition ◽  
British Library ◽  
Oncogenic Viruses ◽  
Cell Plasma Membrane ◽  
Bhk Cells ◽  
Receptor Sites ◽  
Cell Plasma ◽  
Significant Difference ◽  
Phospholipid Ratio

1. The phospholipid composition and cholesterol/phospholipid ratio of plasma membrane is the same in normal as in transformed BHK (baby-hamster kidney) cells; no significant difference in length or degree of unsaturation of the contributing acyl chains is apparent. 2. The turnover of acetate-labelled phosphatidylcholine species in the plasma membrane of normal and transformed BHK cells is the same. 3. Intramembranous particles of normal and transformed 3T3-cell plasma membrane are randomly distributed, whether at 4degreesC or at 37degreesC, in sparse or in dense cultures. There is no correlation between distribution of particles and the movement of concanavalin A receptor sites. 4. It is concluded that transformation of fibroblastic cells by oncogenic viruses does not lead to major changes in the lipid fluidity of the plasma membrane. 5. Details of the phospholipid composition of nuclei, mitochondria and endoplasmic reticulum in normal and transformed BHK cells have been deposited as Supplementary Publication SUP 50061 (5 pages) at the British Library Lending Division, Boston, Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1976) 153, 5.

Stimulation of Tumor-Specific Immunity Using Tumor Cell Plasma Membrane Antigen

Methods ◽  
1997 ◽  
Vol 12 (2) ◽  
pp. 155-164 ◽  
Author(s):  
Matthew F Mescher ◽  
Elena Savelieva
Keyword(s):  
Plasma Membrane ◽  
Tumor Cell ◽  
Cell Plasma Membrane ◽  
Specific Immunity ◽  
Cell Plasma ◽  
Stimulation Of

PROTEIN KINASE ACTIVITY ASSOCIATED WITH THE FAT CELL PLASMA MEMBRANE

1981 ◽  
Vol 9 (2) ◽  
pp. 232P-232P
Author(s):  
G. J. Belsham ◽  
R. W. Brownsey ◽  
R. M. Denton
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
Kinase Activity ◽  
Protein Kinase Activity ◽  
Fat Cell ◽  
Cell Plasma Membrane ◽  
Cell Plasma

Gastrointestinal Cell Plasma Membrane Wounding and Resealing In Vivo

1989 ◽  
Vol 96 (5) ◽  
pp. 1238-1248 ◽  
Author(s):  
Paul L. McNeil ◽  
Susumu Ito
Keyword(s):  
Plasma Membrane ◽  
Cell Plasma Membrane ◽  
Cell Plasma

scholarly journals A murine model of Charcot-Marie-Tooth disease 4F reveals a role for the C-terminus of periaxin in the formation and stabilization of Cajal bands

2018 ◽  
Vol 3 ◽  
pp. 20 ◽  
Author(s):  
Diane L. Sherman ◽  
Peter J. Brophy
Keyword(s):  
Plasma Membrane ◽  
Schwann Cell ◽  
Laminin Receptor ◽  
Cell Plasma Membrane ◽  
Charcot Marie Tooth ◽  
Charcot Marie Tooth Disease ◽  
C Terminus ◽  
Cell Plasma ◽  
Inherited Neuropathies ◽  
Tooth Disease

Charcot-Marie-Tooth (CMT) disease comprises up to 80 monogenic inherited neuropathies of the peripheral nervous system (PNS) that collectively result in demyelination and axon degeneration. The majority of CMT disease is primarily either dysmyelinating or demyelinating in which mutations affect the ability of Schwann cells to either assemble or stabilize peripheral nerve myelin. CMT4F is a recessive demyelinating form of the disease caused by mutations in the Periaxin (PRX) gene. Periaxin (Prx) interacts with Dystrophin Related Protein 2 (Drp2) in an adhesion complex with the laminin receptor Dystroglycan (Dag). In mice the Prx/Drp2/Dag complex assembles adhesive domains at the interface between the abaxonal surface of the myelin sheath and the cytoplasmic surface of the Schwann cell plasma membrane. Assembly of these appositions causes the formation of cytoplasmic channels called Cajal bands beneath the surface of the Schwann cell plasma membrane. Loss of either Periaxin or Drp2 disrupts the appositions and causes CMT in both mouse and man. In a mouse model of CMT4F, complete loss of Periaxin first prevents normal Schwann cell elongation resulting in abnormally short internodal distances which can reduce nerve conduction velocity, and subsequently precipitates demyelination. Distinct functional domains responsible for Periaxin homodimerization and interaction with Drp2 to form the Prx/Drp2/Dag complex have been identified at the N-terminus of Periaxin. However, CMT4F can also be caused by a mutation that results in the truncation of Periaxin at the extreme C-terminus with the loss of 391 amino acids. By modelling this in mice, we show that loss of the C-terminus of Periaxin results in a surprising reduction in Drp2. This would be predicted to cause the observed instability of both appositions and myelin, and contribute significantly to the clinical phenotype in CMT4F.

Plant cell plasma membrane structure and properties under clinostatting

1989 ◽  
Vol 9 (11) ◽  
pp. 71-74 ◽  
Author(s):  
Yu.A. Polulakh ◽  
S.I. Zhadko ◽  
D.A. Klimchuk ◽  
V.A. Baraboy ◽  
A.N. Alpatov ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Plant Cell ◽  
Membrane Structure ◽  
Structure And Properties ◽  
Cell Plasma Membrane ◽  
Cell Plasma
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