Cell-specific constraints to the lateral diffusion of a membrane glycoprotein.

Journal Article (Journal Article)

We have previously shown that the lateral diffusion, D, of the class I Major Histocompatibility Complex (MHC) glycoprotein H-2Ld is constrained by its glycosylation, when expressed in mouse L-cells. Removal of one or more of the 3 N-linked oligosaccharides of H-2Ld glycoproteins results in an increase in D. In order to further examine the influence of glycosylation on D, we compared lateral diffusion of H-2Ld expressed in wild-type CHO cells with lateral diffusion of the same molecule expressed in mutant CHO cells with aberrant surface glycosylation. In addition, we compared lateral diffusion of wild-type and unglycosylated H-2Ld antigens in these cells. In contrast to the large effect of glycosylation state on lateral diffusion of H-2Ld in mouse L-cells, there was little effect of glycosylation on lateral diffusion of H-2Ld in any of the CHO cells. This, together with similar results on hamster class I antigens, indicates that the constraints to D of H-2Ld and other class I MHC molecules are different in CHO cells than in L-cells. Measurements of lateral diffusion after treatment of cells with cytochalasin D make it clear that interactions between MHC class I molecules and a cytoskeleton are important in reducing the mobile fraction of diffusing molecules, R, though they cannot be shown to directly affect the diffusion coefficient, D.

Full Text

Duke Authors

Cited Authors

  • Barbour, S; Edidin, M

Published Date

  • March 1992

Published In

Volume / Issue

  • 150 / 3

Start / End Page

  • 526 - 533

PubMed ID

  • 1537882

International Standard Serial Number (ISSN)

  • 0021-9541

Digital Object Identifier (DOI)

  • 10.1002/jcp.1041500313


  • eng

Conference Location

  • United States