Efficient Isolation and Quantitative Proteomic Analysis of Cancer Cell Plasma Membrane Proteins for Identification of Metastasis-Associated Cell Surface Markers

2009 ◽  
Vol 8 (6) ◽  
pp. 3078-3090 ◽  
Author(s):  
Rikke Lund ◽  
Rikke Leth-Larsen ◽  
Ole N. Jensen ◽  
Henrik J. Ditzel
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Cell Surface ◽  
Cancer Cell ◽  
Proteomic Analysis ◽  
Surface Markers ◽  
Cell Surface Markers ◽  
Cell Plasma Membrane ◽  
Quantitative Proteomic Analysis ◽  
Cell Plasma

scholarly journals Cell surface heparan sulfate proteoglycans are involved in the binding of Hsp90α and Hsp90β to the cell plasma membrane

2015 ◽  
Vol 9 (6) ◽  
pp. 460-468 ◽  
Author(s):  
Anastasiya V Snigireva ◽  
Veronika V Vrublevskaya ◽  
Vladimir N Afanasyev ◽  
Oleg S Morenkov
Keyword(s):  
Plasma Membrane ◽  
Cell Surface ◽  
Heparan Sulfate ◽  
Heparan Sulfate Proteoglycans ◽  
Cell Plasma Membrane ◽  
Cell Plasma

scholarly journals Specific interaction of Penetratin with cell surface partners measured with biomembrane force probe

2020 ◽  
Author(s):  
P Soule ◽  
F Illien ◽  
S Kulifaj ◽  
A Joliot ◽  
C Gourier ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Cell Surface ◽  
Specific Interaction ◽  
Cell Plasma Membrane ◽  
Biomembrane Force Probe ◽  
Cell Plasma ◽  
A Cell ◽  
Heparan Sulfates ◽  
Chemical Groups ◽  
Molecular Description

ABSTRACTPenetratin is a Cell Penetrating Peptide able to cross the cell plasma membrane possibly bound to a cargo molecule to be delivered into the cell. The mechanism of its entry is poorly known. A key to a molecular description of this mechanism is to identify the partners of Penetratin at the cell surface during its adhesion and internalization. We used the Biomembrane Force Probe to identify the partners during the first second of adhesion of Penetratin on the cell plasma membrane. We evidenced that heparan sulfates are the first partners after contact as well as unknown partners hidden by sialic acids. Experiments of binding of Penetratin on vesicles bearing charged or sulfated lipids showed no adhesion pointing that a negatively charged partner is not enough and there is a specificity for certain chemical groups bearing the charges. A model of the measured forces of interaction enabled to determine the adhesion energy of a Penetratin with heparan sulfates on a cell to be in the range 18 to 22 kBT.

scholarly journals Membrane proteins synthesized by rabbit reticulocytes.

1975 ◽  
Vol 65 (1) ◽  
pp. 51-64 ◽  
Author(s):  
H F Lodish ◽  
B Small
Keyword(s):  
Amino Acids ◽  
Plasma Membrane ◽  
Membrane Proteins ◽  
Cell Plasma Membrane ◽  
Whole Cells ◽  
Predominant Species ◽  
Cytoplasmic Surface ◽  
Cell Plasma ◽  
Intact Rabbit ◽  
Rabbit Reticulocytes

Intact rabbit reticulocyte cells synthesize two predominant species of polypeptides which are components of the cell plasma membrane. Previous work (Lodish, H. F. 1973. Proc. Natl. Acad. Sci. U. S. A. 70:1526-1530.) showed that these proteins were synthesized by polyribosomes not attached to membranes. We show here that both polypeptides are confined to the cytoplasmic surface of the cell membrane. These studies utilized iodination of whole cells and of membranes with lactoperoxidase, and digestion of whole cells and membranes with chymotrypsin, One of these proteins is synthesized as a precursor, and about 20-40 amino acids are removed after it is incorporated into the membrane, We discuss the probable sites of synthesis of these and other classes of membrane proteins.

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