Importance of Glomus Cell Plasma Membrane and Mitochondrial Membrane Potentials During Acute Hypoxia Signaling in the Rat Carotid Body

2003 ◽  
pp. 305-311
Author(s):  
Arijit Roy ◽  
Abu B. Al-mehdi ◽  
Anil Mokashi ◽  
Sukhamay Lahiri
Keyword(s):  
Plasma Membrane ◽  
Carotid Body ◽  
Mitochondrial Membrane ◽  
Acute Hypoxia ◽  
Membrane Potentials ◽  
Glomus Cell ◽  
Cell Plasma Membrane ◽  
Cell Plasma ◽  
Hypoxia Signaling

Effect of Ca2+ ions on liver cell plasma membrane polypeptides

1983 ◽  
Vol 61 (5) ◽  
pp. 293-300 ◽  
Author(s):  
Ibrahim M. Yousef
Keyword(s):  
Plasma Membrane ◽  
Liver Cell ◽  
Mitochondrial Membrane ◽  
Low Molecular Weight ◽  
Cell Plasma Membrane ◽  
Polypeptide Patterns ◽  
Cell Plasma ◽  
Membrane Components ◽  
Low Ionic Strength ◽  
Liver Cell Plasma Membrane

Plasma membrane fractions, microsomes, and mitochondrial membrane were prepared from rat liver. The effects of incubation of these membranes in various ionic strengths (1–12 mM) of NaHCO3 (pH 7.4) on the polypeptide patterns were studied in the absence or the presence of various concentrations of CaCl2 (1–12 mM). Many polypeptides were extracted from each of the membranes in the low ionic strength buffers (1 mM); these polypeptides were essentially similar to those remaining in the membrane after incubation. The extraction of these polypeptides continued when concentration of NaHCO3 increased. However, the presence of CaCl2 at a concentration of 4 mM or higher stabilized the membrane proteins and reduced the continuous loss of the polypeptides, and only low molecular weight polypeptides were affected. These data suggest that the organization of proteins in liver cell membranes may depend on the nature of their interaction with other membrane components (i.e., phospholipids), which could be affected by Ca2+ ions.

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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