Lateral diffusion of concanavalin a receptors in the plasma membrane of mouse fibroblasts

1976 ◽  
Vol 433 (1) ◽  
pp. 209-214 ◽  
Author(s):  
Yuli Zagyansky ◽  
Michael Edidin
Keyword(s):  
Plasma Membrane ◽  
Concanavalin A ◽  
Lateral Diffusion ◽  
Mouse Fibroblasts ◽  
Concanavalin A Receptors

Lateral Mobility of Integrin αIIbβ3 (Glycoprotein IIb/IIIa) in the Plasma Membrane of a Human Megakaryocyte

1997 ◽  
Vol 77 (01) ◽  
pp. 143-149 ◽  
Author(s):  
Annelies Schootemeijer ◽  
Gijsbert van Willigen ◽  
Hans van der Vuurst ◽  
Leon G J Tertoolen ◽  
Siegfried W De Laat ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Fluorescence Recovery After Photobleaching ◽  
Cell Activation ◽  
Lateral Diffusion ◽  
Cytochalasin D ◽  
Lag Phase ◽  
Integrin Αiibβ3 ◽  
Cell Matrix ◽  
Cytoplasmic Actin ◽  
Mobile Fraction

SummaryThe migration of integrins to sites of cell-cell and cell-matrix contact is thought to be important for adhesion strengthening. We studied the lateral diffusion of integrin αIIbβ3 (glycoprotein Ilb/IIIa) in the plasma membrane of a cultured human megakaryocyte by fluorescence recovery after photobleaching of FITC-labelled monovalent Fab fragments directed against the P3 subunit. The diffusion of P3 on the unstimulated megakaryocyte showed a lateral diffusion coefficient (D) of 0.37 X10'9 cm2/s and a mobile fraction of about 50%. Stimulation with ADP (20 μM) or α-thrombin (10 U/ml) at 22° C induced transient decreases in both parameters reducing D to 0.21 X 10‘9 cm2/s and the mobile fraction to about 25%. The fall in D was observed within 1 min after stimulation but the fall in mobile fraction showed a lag phase of 5 min. The lag phase was absent in the presence of Calpain I inhibitor, whereas cytochalasin D completely abolished the decrease in mobile fraction. The data are compatible with the concept that cell activation induces anchorage of 50% of the mobile αIIbβ3 (25% of the whole population of receptor) to the cytoplasmic actin filaments, although, as discussed, other rationals are not ruled out.

scholarly journals Lateral diffusion of wild-type and mutant Ld antigens in L cells.

1984 ◽  
Vol 99 (6) ◽  
pp. 2333-2335 ◽  
Author(s):  
M Edidin ◽  
M Zuniga
Keyword(s):  
Plasma Membrane ◽  
Diffusion Coefficients ◽  
Transmembrane Protein ◽  
Transmembrane Proteins ◽  
Lateral Diffusion ◽  
Cytoplasmic Domain ◽  
Histocompatibility Antigen ◽  
Wild Type ◽  
Major Histocompatibility Antigen ◽  
Cytoplasmic Side

We have compared the lateral diffusion of intact transmembrane proteins, wild-type H-2Ld antigens, with that of mutants truncated in the cytoplasmic domain. Diffusion coefficients and mobile fractions were similar for all molecules examined, from wild-type Ld antigens with 31 residues on the cytoplasmic side of the plasma membrane to mutants with only four residues in the cytoplasmic domain. This result limits ways in which the lateral diffusion of a major histocompatibility antigen, a transmembrane protein, can be constrained by interactions with other molecules.

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