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Microfilament association of ASGP-2, the concanavalin A-binding glycoprotein of the cell-surface sialomucin complex of 13,762 rat mammary ascites tumor cells.

Abstract：

:Microfilament-associated proteins and membrane-microfilament interactions are being investigated in microvilli isolated from 13,762 rat mammary ascites tumor cells. "Phalloidin shift" analyses on velocity sedimentation gradients of Triton X-100 extracts of [3H]-glucosamine-labeled microvilli identified a 120-kDa cell-surface glycoprotein associated with the microvillar microfilament core. The identification was verified by concanavalin A (Con A) blots of one- and two-dimensional (2D) electrophoresis gels of sedimented microfilament cores. By 2D-electrophoresis and lectin analyses the 120-kDa protein appeared to be a fraction of ASGP-2, the major Con A-binding glycoprotein of the sialomucin complex of the 13,762 cells. This identity was confirmed by immunoblot analyses using immunoblot-purified anti-ASGP-2 from anti-membrane serum prepared against microvillar membranes. Proteolysis of the microvilli with subtilisin or trypsin resulted in an increase in the amount of ASGP-2 associated with the microfilament cores. An increase was also observed with sialidase treatment of the microvilli, suggesting that negative charges, probably present on the highly sialated sialomucin ASGP-1 of the ASGP-1/ASGP-2 sialomucin complex, reduce ASGP-2 association with the microfilament core. Proteolysis of isolated microvillar membranes, which contain actin but not microfilaments, also increased the association of ASGP-2 with a Triton-insoluble, actin-containing membrane fraction. Purified ASGP-2 does not bind to microfilaments in sedimentation assays. Since the Triton-insoluble membrane residue is enriched in an actin-containing transmembrane complex, which contains a different glycoprotein, we suggest that the ASGP-2 is binding indirectly via this complex to the microfilament core in the intact microvilli.

journal_name

Exp Cell Res

journal_title

Experimental cell research

authors

Vanderpuye OA,Carraway CA,Carraway KL

doi

10.1016/0014-4827(88)90392-8

subject

Has Abstract

pub_date

1988-10-01 00:00:00

pages

211-23

issue

eissn

0014-4827

issn

1090-2422

journal_volume

178

pub_type

杂志文章

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Microfilament association of ASGP-2, the concanavalin A-binding glycoprotein of the cell-surface sialomucin complex of 13,762 rat mammary ascites tumor cells.