Studies on Cell Deformability

Weiss, Leonard

doi:10.1083/jcb.26.3.735

Cited by 167 publications

(19 citation statements)

References 8 publications

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“…Treatment with neuraminidase causes a desialation of the surface glycoprotein, loss of surface negaive charge and the related changes in cell shape (56). From the viewpoint of tumor immunity, removal of sialic acid from the cell surface causes a reduced growth of tumors in susceptible hosts (48) and increases tumor immunogenicity (4,42).…”

Section: Discussionmentioning

confidence: 99%

Ultrastructural Demonstration of the Negative Surface Charge on Human Trophoblast

Kawagoe

Kawana

Sakamoto

1980

Acta Histochem. Cytochem

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Section: Discussionmentioning

confidence: 99%

Ultrastructural Demonstration of the Negative Surface Charge on Human Trophoblast

Kawagoe

Kawana

Sakamoto

1980

Acta Histochem. Cytochem

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“…Untreated control cells were resuspended in 5 to 7 ml of half-strength Hanks' in 5 % sucrose (pH 7.6 =t= 0.2) and incubated at 25°C. In the "neuraminidase" series, the control cells were resuspended in 2 ml calcium-saline (0.145M NaCl; 0.005g CaCI~; 3 X 10-~M NaHCO3; pH 7.2 4-0.2), and the enzyme-treated cells were resuspended in 1 ml calcium-saline plus 1 ml 100 units/ml neuraminidase in calciumsaline (I volume Behringwerke stock neuraminidase, free of protease, aldolase, phospholipase, and lipase activity (31), 500 units/ml diluted with 4 volumes calciumsaline). This concentration of neuraminidase was calculated to be in excess of the amount needed to liberate all of the neuraminic acid present in 10 X 106 cells.…”

Section: Preparation For Electrophor Esismentioning

confidence: 99%

Cellular Electrophoretic Mobility and the Mitotic Cycle

Mayhew

1966

The Journal of General Physiology

118

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The electrophoretic mobility of RPMI No. 41 cells grown in suspension, parasynchronized by double thymidine blocking and cold shock, is reported. No. 41 cells have a higher electrophoretic mobility during the mitotic peak phase than at other times in the mitotic cycle. Treatment of parasynchronous cells by neuraminidase reduces the mobility to the same value irrespective of the stage of the cells in the mitotic cycle. The higher electrophoretic mobility of cells in mitotic peak phase is probably due to a higher surface charge density at this time, possibly caused by a higher concentration of ionized neuraminic acid carboxyl groups at the hydrodynamic shear layer. The mobility of nonsynchronous rapidly and slowly growing cells differs; neuraminidase reduces their mobility by proportionately similar amounts. The results suggest that the differences in mobility between rapidly and slowly growing cells cannot be accounted for exclusively by differences in the amount of neuraminic acid groups at the shear layer.Eisenberg et al. (8) noted greater variability in the electrophoretic mobilities of rapidly growing liver cells compared with those growing more slowly. This observation could suggest that at different stages during the mitotic cycle ceils m a y have different electrophoretic mobilities. In a preliminary communication (13) some change was reported in the mobility of cultured cells parasynchronized by double thymidine blocking. In this communication further studies are reported in which another synchronization technique was used, and the effect of neuraminidase on the mobility of synchronous cells was studied. M A T E R I A L S AND M E T H O D SStock Cell Culture RPMI No. 41 cells derived from a human osteogenic sarcoma (16) cultured in suspension at 37°C in RPMI medium 906 (16), supplemented by 5 % caff serum, were used throughout. The density of the cell suspension was maintained at 200 to 250 X 103 eells/ml; the glucose level at 1200 mg/liter

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“…Moreover, there is evidence that this high degree of sialation contributes to the negative surface charge, rigidity, and lack of adhesiveness of these cells (7,8), for as myeloid precursor cells mature, they become less negatively charged, more deformable and more adhesive, coincident with a progressive loss of cell surface sialic acid (6).…”

Section: Introductionmentioning

confidence: 99%

Mobilization of sialidase from intracellular stores to the surface of human neutrophils and its role in stimulated adhesion responses of these cells.

Cross¹,

Wright²

1991

J. Clin. Invest.

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Desialation of cell surfaces has been associated with the initiation or modification of diverse cellular functions. In these studies we have examined the subcellular distribution of sialidase (SE) in human neutrophils as well as the mobilization of this enzyme following neutrophil activation. Separation of subcellular fractions by density gradient centrifugation showed that SE is present not only in neutrophil primary and secondary granule populations, like lysozyme, but also in plasma membrane fractions. Neutrophil activation was associated with a redistribution of SE from secondary granule-enriched fractions to the plasma membrane. Furthermore, SE activity detected on the surface of intact neutrophils with a fluorescent SE substrate increased rapidly after activation with kinetics that matched both the loss of total cell-associated sialic acid and release of free sialic acid from the cells. These activation-dependent events were in each case blocked by incubation of neutrophils with the SE inhibitor, 2-deoxy-N-acetyl-neuraminic acid. Aggregation responses of neutrophils as well as adhesion responses to nylon and plastic surfaces were also inhibited by 2-deoxyNANA. Our findings indicate that the activation-dependent desialation of the neutrophil surface is associated with mobilization of an endogenous SE to the plasma membrane and has a role in stimulated adhesion responses of these cells. (J.

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Studies on Cell Deformability

Cited by 167 publications

References 8 publications

Ultrastructural Demonstration of the Negative Surface Charge on Human Trophoblast

Ultrastructural Demonstration of the Negative Surface Charge on Human Trophoblast

Cellular Electrophoretic Mobility and the Mitotic Cycle

Mobilization of sialidase from intracellular stores to the surface of human neutrophils and its role in stimulated adhesion responses of these cells.

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