PHOSPHATIDYLINOSITOL IS INVOLVED IN THE MEMBRANE ATTACHMENT OF NCAM-120, THE SMALLEST COMPONENT OF THE NEURAL CELL-ADHESION MOLECULE
PHOSPHATIDYLINOSITOL IS INVOLVED IN THE MEMBRANE ATTACHMENT OF NCAM-120, THE SMALLEST COMPONENT OF THE NEURAL CELL-ADHESION MOLECULE
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DOI:
10.1002/j.1460-2075.1986.tb04526.x
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发表时间:
1986-10-01
期刊:
影响因子:
11.4
通讯作者:
GORIDIS, C
中科院分区:
文献类型:
--
作者:
HE, HT;BARBET, J;GORIDIS, C
The rodent neural cell adhesion molecule (NCAM) consists of three glycoproteins with Mr of 180,000, 140,000 and 120,000. The Mr 120,000 protein (NCAM-120) has been shown to exist in membrane-bound and soluble forms but the nature of its membrane association and release has remained obscure. We show here that phosphatidylinositol-specific phospholipase C (PI-PLC), but not a phospholipase C of different specificity, releases a substantial proportion of NCAM-120 from brain membranes and solubilizes almost quantitatively NCAM-120 present at the surface of C6 astroglial cells. The PI-PLC effect was highly selective since only one other protein species was detectably released from C6 cells. These results suggest that NCAM-120 is held in the membrane by covalently bound phosphatidylinositol or a closely related lipid in a way similar to several other surface proteins from eukaryotic cells. The presence of NCAM in a form which can be released from the cell surface by a highly selective mechanism raises additional possibilities for modulation and control of cell-cell adhesion.