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At least 19 recordsLinked to original sources
PubMed1993

On the role of the platelet membrane skeleton in mediating signal transduction. Association of GP IIb-IIIa, pp60c-src, pp62c-yes, and the p21ras GTPase-activating protein with the membrane skeleton.

The platelet plasma membrane is lined with a membrane skeleton composed of short actin filaments, actin-binding protein, spectrin, vinculin, and other unidentified proteins. It is connected to the outside of the cell through association with the cytoplasmic domains of transmembrane receptors. In detergent-lysed platelets, cytoplasmic actin filaments are sedimented by centrifugation at 15,600 x g, but the sedimentation of membrane skeleton fragments requires higher g-forces (100,000 x g). In the present study, we show that the major platelet integrin, glycoprotein (GP) IIb-IIIa, sediments from detergent-lysed platelets at 100,000 x g together with fragments of the membrane skeleton that contain the cytoskeletal proteins spectrin, vinculin, and talin. In addition, this cell fraction contained the tyrosine kinases pp60c-src and pp62c-yes and the p21ras GTPase-activating protein (GAP). After thrombin-induced platelet aggregation mediated by fibrinogen binding to GP IIb-IIIa on adjacent platelets, we detected a redistribution of spectrin, talin, vinculin, pp60c-src, and pp62c-yes to the fraction that sediments at 15,600 x g. The redistribution of these proteins from the high-speed detergent-insoluble fraction to the low-speed fraction correlated with the extent of aggregation and was not detected in aggregation-defective thrombasthenic platelets (which lack the GP IIb-IIIa complex). In addition, many of the proteins phosphorylated on tyrosine in activated platelets were present in detergent-insoluble fractions. These results are consistent with the possibilities that 1) GP IIb-IIIa, pp60c-src, pp62c-yes, and GAP associate with a membrane skeleton fraction that contains spectrin, vinculin, and talin, 2) the association of GP IIb-IIIa with adhesive ligand in a platelet aggregate causes components of the membrane skeleton to undergo altered association with cytoplasmic actin filaments, and 3) many of the proteins phosphorylated on tyrosine residues in activated platelets are components of the cytoskeleton. The results imply that the membrane skeleton may play an important role in binding signaling molecules at sites of integrin-cytoskeleton interactions and in mediating signal transduction events in platelets. Further, GP IIb-IIIa-induced redistribution of components of the membrane skeleton and associated signaling molecules may represent an important step in regulating integrin-induced motile events in platelets.

Actins↗
PubMed1987

Concanavalin A-agglutinability of membrane-skeleton-free vesicles and aged cellular remnants derived from human erythrocytes. Is the membrane skeleton required for agglutination?

Vesicles and cell remnants have been obtained by aging of erythrocytes in vitro. The vesicles lacking the membrane skeletal proteins and the remnants known to possess a rigid skeleton have been used to assess the role of membrane skeletal proteins in the process of Con A (concanavalin A)-mediated agglutination of erythrocytes. Both the vesicles and the remnants were found to bind Con A at the same density as did intact cells. The vesicles, isolated from normal as well as from the Con A-agglutinable trypsin- and Pronase-treated cells, failed to agglutinate with Con A. They were, however, well agglutinated by WGA (wheat-germ agglutinin) and RCA [Ricinus communis (castor bean) agglutinin], indicating that the vesicles are not defective in agglutination. Large, cytoskeleton-free, vesicles prepared by another procedure also gave the same results. The aged remnants from trypsin- and Pronase-treated erythrocytes showed significantly decreased agglutination with Con A, but were agglutinated as well as the fresh cells by WGA and RCA. The agglutination with Con A is thus abolished when the membrane skeleton is absent, and reduced when it is rigid, suggesting that the skeleton may play an important role in the agglutination of erythrocytes by Con A.

Concanavalin A↗
PubMedDate not supplied

Relationship between spatial pattern of basal bodies and membrane skeleton (epiplasm) during the cell cycle of Tetrahymena: cdaA mutant and anti-membrane skeleton immunostaining.

Microtubular basal bodies and epiplasm (membrane skeleton) are the main components of the cortical skeleton of Tetrahymena. The aim of this report was to study functional interactions of basal bodies and epiplasm during the cell cycle. The cortex of Tetrahymena cells was stained with anti-epiplasm antibody. This staining produced a bright epiplasmic layer with a dark pattern of unstained microtubular structures. The fluorescence of the anti-epiplasm antibody disappeared at sites of newly formed microtubular structures, so the new basal body domains and epiplasmic layer could be followed throughout the cell cycle. Different patterns of deployment of new basal bodies were observed in early and advanced dividers. In advanced dividers the fluorescence of the epiplasmic layer diminished locally within the forming fission line where the polymerization of new basal bodies largely extincted. In wild type Tetrahymena, the completion of the micronuclear metaphase/anaphase transition was associated with a transition from the pattern of new basal body deployment and epiplasm staining of the early divider to the pattern of the advanced dividers. The signal for the fission line formation in Tetrahymena (absent in cdaA1 Tetrahymena mutationally arrested in cytokinesis) brings about 1) transition of patterns of deployment of basal bodies and epiplasmic layer on both sides of the fission line; and 2) coordination of cortical divisional morphogenesis with the micronuclear mitotic cycle.

Animals↗
PubMed1983

Phase I study of iv mycobacterial cell wall skeleton and cell wall skeleton combined with trehalose dimycolate.

A phase I study to determine the toxicity and immunologic effects of iv administered aqueous suspensions of mycobacterial cell wall skeleton (CWS) and CWS combined with trehalose dimycolate (TDM) was performed. A total of 26 patients received suspensions of either CWS or CWS/TDM given iv every 1 or 2 weeks in set doses of either 100, 250, 500, or 1000 micrograms/m2. The major dose-limiting side effects for both preparations were fever and chills at a dose of 1 mg/m2. This was more severe with the combined CWS/TDM. There was no renal or pulmonary toxicity. There was evidence of hepatic toxicity, with increases in the alkaline phosphatase and gamma glutamyl transferase, especially with high doses of CWS/TDM. Both the CWS and CWS/TDM groups had an increase in their wbc count. In the patients receiving CWS alone, there was a decrease in the peripheral blood monocytes. In the CWS/TDM group, there was an increase in the serum lysozyme, suggesting macrophage activation. No antitumor effect was seen in this phase I study. Aqueous suspensions of CWS and CWS/TDM can be administered safely iv over a period of time, with evidence of an effect on hematologic parameters.

Animals↗
PubMed1978

The craniofacial skeleton in anencephalic human fetuses. III. Facial skeleton.

A sample of 12 anencephalic fetuses with gestational ages ranging from 26 to 40 weeks and exhibiting varying degrees of severity of the dorsal cranial defect was compared to three normal fetuses of comparable gestational ages with regard to the morphology and positional relationships of the maxillofacial skeletal complex. Gross dissection, alizarin red S staining, radiographs, cephalometric tracings, and histologic techniques were utilized. It was found that some facial bones were severely affected in morphology, size, spatial and angular relationships. The manner in which these were altered suggests that their morphogenesis is an adaptation to the primary defect of the neurocranium.

Anencephaly↗