Mechanism of concanavalin A-induced anchorage of the major cell surface glycoproteins to the submembrane cytoskeleton in 13762 ascites mammary adenocarcinoma cells.

Jung, Goeh; Helm, Ricki M.; Carraway, Coralie A. Carothers; Carraway, Kermit L.

doi:10.1083/jcb.98.1.179

Cited by 28 publications

(18 citation statements)

References 30 publications

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“…Treatment of 13762 MAT-B1 cells with Con A leads to capping of the sialomucin complex [6]. An early step in this process is Con A linkage of the sialomucin complex to a transmembrane complex associated with the microfilament core [19]. Thus, the ability of Con A to serve as a bridge between two different cell surface glycoproteins can explain induction of topographical redistributions of cell surface components by Con A.…”

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Topography and microfilament core association of a cell surface glycoprotein of ascites tumor cell microvilli

Sheng

Vanderpuye

Hull

et al. 1989

J of Cellular Biochemistry

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Membrane-microfilament interactions are being investigated in microvilli isolated from 13762 rat mammary ascites tumor cells. These microvilli are covered by a sialomucin complex, composed of the sialomucin ascites sialoglycoprotein-1 (ASGP-1) and the associated concanavalin A (Con A)-binding glycoprotein ASGP-2. Limited proteolysis of the microvilli releases large, highly glycosylated fragments of ASGP-1 from the microvilli and increases the association of ASGP-2 with the Triton-insoluble microvillar microfilament core (Vanderpuye OA, Carraway CAC, Carraway, KL: Exp Cell Res 178:211, 1988). To analyze the topography of ASGP-2 in the membrane and its association with the microfilament core, microvilli were treated with proteinase K for timed intervals and centrifuged. The pelleted microvilli were extracted with Triton X-100 for the preparation of microfilament cores and Triton-soluble proteins or with 0.1 M carbonate, pH 11, for the preparation of microvillar membranes depleted of peripheral membrane proteins. These microvilli fractions were analyzed by dodecyl sulfate gel electrophoresis, lectin blotting with Con A and L-phytohemagglutinin, and immunoblotting with anti-ASGP-2. The earliest major proteolysis product from this procedure was a 70 kDa membrane-bound fragment. At longer times a 60 kDa released fragment, 30-40 kDa Triton-soluble fragments, and 25-30 kDa membrane- and microfilament-associated fragments were observed. Phalloidin shift analysis of microfilament-associated proteins on velocity sedimentation gradients indicated that the 25-30 kDa fragments were strongly associated with the microfilament core. From these studies we propose that ASGP-2 has a site for indirect association with the microfilament core near the membrane on a 15-20 kDa segment.

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confidence: 99%

Topography and microfilament core association of a cell surface glycoprotein of ascites tumor cell microvilli

Sheng

Vanderpuye

Hull

et al. 1989

J of Cellular Biochemistry

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“…One recent report has provided evidence that a major glycoprotein present in microvilli isolated from mammary adenocarcinoma cells is directly associated with actin (5,18). However, the function of this glycoprotein is not yet known, so to relate these findings to receptor function is impossible at present.…”

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Isolation of a subpopulation of glycoprotein IIb-III from platelet membranes that is bound to membrane actin.

Painter¹,

Prodouz²,

Gaarde³

1985

The Journal of Cell Biology

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Triton X-100-insoluble residues, or skeletons, of plasma membrane-rich vesicles obtained from unstimulated human platelets were isolated by high speed centrifugation. About 10-15% of the total surface iodinatable glycoproteins lib and III (GPIIb and GPIII, respectively) co-isolated with the insoluble fraction. After sonication and centrifugation the solubilized material was further purified by affinity chromatography on Lens culinaris lectin-Sepharose. SDS PAGE analysis of this material revealed the presence of at least three major proteins, which were shown to be GPIIb, GPIII, and membrane actin, as judged by their electrophoretic properties and on the basis of immunological criteria. Antibodies directed against platelet surface glycoproteins and antibodies directed against rabbit actin were able to immunoprecipitate all three proteins, which indicates that they were noncovalently associated with one another. Gel filtration of the Lens lectin-purified Triton-insoluble complex on Ultrogel AcA 22 showed that >85% of the total surface GPIIb and III was associated with an actin-rich peak that eluted in the void volume. In contrast, the form of GPIIb-III present in the Triton-soluble membrane fraction behaved as monomeric species when chromatographed under identical conditions. Finally, the GPIIb-III membrane actin complex bound with high efficiency to rabbit f-actin in vitro in a Ca++-independent manner, whereas the monomeric forms found in the Triton-soluble fraction did not bind to actin. These results indicate that two forms of GPllb and III exist: one that binds directly to endogenous membrane actin and one that does not.Numerous studies have provided largely indirect evidence for transmembrane interactions among surface proteins and receptors of cells and an internal membrane matrix composed of actin and other cytoskeletal proteins (3,5,7,10,14,16,17,19,23,25,27,31,35,40,45). Indeed, a number of studies have shown that the surface topography and lateral mobility of receptors can be modulated by the underlying cytoskeleton and its associated contractile and motile elements (20,28,30,31,36,37,39).In the erythrocyte membrane, the major membrane glycoprotein, band III, interacts directly with ankyrin (2), which links this surface protein to the spectrin-actin submembranous matrix of this cell type (9, 27), The molecular basis for these interactions is poorly understood in nonerythroid cell types, however. One recent report has provided evidence that a major glycoprotein present in microvilli isolated from mammary adenocarcinoma cells is directly associated with actin (5, 18). However, the function of this glycoprotein is not yet known, so to relate these findings to receptor function is impossible at present. We have previously shown that a molecular complex exists in membranes derived from unstimulated platelets that consists of actin, glycoproteins lib and III (GPIIb and GPIII, respectively), ~ and polypeptides of 180, 000-200,000 (29). We further demonstrated that these proteins can be crosslinked to o...

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“…It has been observed in many cell types such as platelets (Wheeler et al, 1985), pheochromocytoma cells (Vale and Shooter, 1983), granulocytes (Jesaitis et aL, 1984), rat mammary adenocarcinoma cells (Jung et al, 1984), RBL cells (Robertson et al, 1986;Apgar, 1990;Seagrave and Oliver, 1990), and B lymphocytes (Braun et aL, 1982;Woda and McFadden, 1983;Woda and Woodin, 1984) that binding of ligand and crosslinking of cell surface proteins induces detergent insolubility of those receptors. Often this immobility of crosslinked receptors is a prelude to patching, capping, and internalization of the receptors, which in turn may be important in the down-regulation of responses.…”

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confidence: 99%

Association of the crosslinked IgE receptor with the membrane skeleton is independent of the known signaling mechanisms in rat basophilic leukemia cells.

Apgar¹

1991

Cell Regul

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Crosslinking of the IgE receptor on the surface of rat basophilic leukemia (RBL) cells by multivalent antigen induces an association of these receptors with the detergent-insoluble membrane skeleton. Detergent insolubility of the receptor can also be induced on purified plasma membranes isolated from RBL cells by the use of either IgE oligomers or IgE monomers plus multivalent antigen. The critical event in initiating this interaction between the receptor and the membrane skeleton is crosslinking of the receptor. This association is rapid, and, when triggered by multivalent antigen, it is quickly reversed by the addition of excess monovalent antigen. The fact that this association occurs with the use of purified plasma membranes indicates that all of the components necessary for this interaction are present in the plasma membrane and that intracellular components are not required.Although crosslinking of the receptor activates phospholipase C and phospholipase A2 leading to the generation of several second messengers, none of these signaling mechanisms appears to be involved in IgE receptor interaction with the membrane skeleton. This interaction cannot be induced by phorbol 12-myristate 13-acetate (PMA), ionomycin, or a combination of these two reagents, although this will result in degranulation. Furthermore, receptor detergent insolubility is temperature independent when triggered by multivalent antigen, thus indicating that enzyme-catalyzed reactions are not important. This was verified by the fact that a variety of inhibitors that block phosphatidylinositol metabolism, arachidonic acid metabolism, Ca2l influx, and protein kinase C (PKC) activation had no effect on antigen-induced association of the receptor with the membrane skeleton. These results indicate that the signaling mechanisms leading to the degranulation response are not involved in the association of the crosslinked receptor with the membrane skeleton.

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Mechanism of concanavalin A-induced anchorage of the major cell surface glycoproteins to the submembrane cytoskeleton in 13762 ascites mammary adenocarcinoma cells.

Cited by 28 publications

References 30 publications

Topography and microfilament core association of a cell surface glycoprotein of ascites tumor cell microvilli

Topography and microfilament core association of a cell surface glycoprotein of ascites tumor cell microvilli

Isolation of a subpopulation of glycoprotein IIb-III from platelet membranes that is bound to membrane actin.

Association of the crosslinked IgE receptor with the membrane skeleton is independent of the known signaling mechanisms in rat basophilic leukemia cells.

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