Cellular determinants of the lateral mobility of neural cell adhesion molecules

被引:27
作者
Jacobson, KA
Moore, SE
Yang, B
Doherty, P
Gordon, GW
Walsh, FS
机构
[1] UNIV N CAROLINA, LINEBERGER COMPREHENS CANC CTR, CHAPEL HILL, NC 27599 USA
[2] UMDS, GUYS HOSP, DEPT EXPT PATHOL, LONDON SE1 9RT, ENGLAND
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 1997年 / 1330卷 / 02期
基金
英国惠康基金;
关键词
cell adhesion protein; neuron; membrane mobility; diffusion coefficient; cell-cell interaction; splicing;
D O I
10.1016/S0005-2736(97)00128-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The lateral mobility of the neural cell adhesion molecule (NCAM) was examined using fluorescence recovery after photobleaching (FRAP). Various isoforms of human NCAM, differing in their ectodomain, their membrane anchorage mode or in the size of their cytoplasmic domain, were expressed in NIH 3T3 cells and C2C12 muscle cells. When the various isoforms were compared in 3T3 cells, FRAP studies showed both GPI-anchored and transmembrane isoforms diffused rapidly and only small differences in either the diffusion coefficients (D) or the mobile fractions (mf) were measured, suggesting the importance of the ectodomain in regulating lateral diffusion. However, the mobility of all NCAM isoforms was greatly reduced in regions of cell-cell contact, presumably due to homophilic trans interactions between NCAMs on adjacent cells. NCAM isoforms transfected into C2C12 cells which express NCAM naturally usually displayed a significantly lower D compared to the same isoforms transfected into 3T3 cells. Thus, NCAM lateral mobility is modulated in regions where cells interact and by the structure of the host cell membrane. (C) 1997 Elsevier Science B.V.
引用
收藏
页码:138 / 144
页数:7
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