The relationship of the cell surface to metabolism. VI. The chemical nature of uranium-complexing groups of the cell surface

A macrophage cell-surface antigen associated with pyran and Corynebacterium parvum-activated macrophages and P388D1 cells but not detectable on normal or glycogen and thioglycollate-elicited murine macrophages has been described. The antigen was demonstrated both by complement-mediated cytotoxicity and immunofluorescence, using an appropriately absorbed rabbit antiserum to P388D1. This antiserum should enable the characterization of activated macrophage cell populations on an individual cell basis and should be a useful probe to study the interactions of macrophages with tumor cells and the relationship of activation to cell-surface changes.

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THE RELATIONSHIP OF CONCANAVALIN A BINDING TO LECTIN-INITIATED CELL AGGLUTINATION

The Journal of Cell Biology ◽

10.1083/jcb.59.1.134 ◽

1973 ◽

Vol 59 (1) ◽

pp. 134-142 ◽

Cited By ~ 82

Author(s):

Kenneth D. Noonan ◽

Max M. Burger

Keyword(s):

Cell Surface ◽

Concanavalin A ◽

Room Temperature ◽

Transformed Cells ◽

Glutaraldehyde Fixation ◽

Cell Agglutination ◽

Normal Cells ◽

Receptor Sites ◽

Relationship Of ◽

The Relationship

We have investigated the relationship of concanavalin. A binding to the cell surface of normal and transformed cells and the subsequent agglutination of the transformed cells. At room temperature almost no differences could be detected in agglutinin binding between transformed and untransformed cells. At 0°C, however, where endocytosis was negligible, the transformed cells bound three times more agglutinin. However, transformed cells and trypsin-treated normal cells do not agglutinate at 0°C although the amounts of agglutinin bound at 0°C are sufficient to permit agglutination when such cells are shifted up to room temperature. Both transformed and trypsin-treated normal cells show a marked increase in agglutination at 15°C as compared to agglutination at 0°C. From this, as well as the observation that mild glutaraldehyde fixation of the cell surface inhibited agglutination but not agglutinin binding, it was concluded that concanavalin A-mediated cell agglutination requires free movement of the agglutinin receptor sites within the plane of the cell surface.

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Freeze-Etch Studies on Fish Skeletal Muscle

Journal of Cell Science ◽

10.1242/jcs.6.2.537 ◽

1970 ◽

Vol 6 (2) ◽

pp. 537-557

Author(s):

W. S. BERTAUD ◽

D. G. RAYNS ◽

F. O. SIMPSON

Keyword(s):

Skeletal Muscle ◽

Cell Surface ◽

Extracellular Space ◽

Muscle Cells ◽

Luminal Surface ◽

Thick Filaments ◽

T Tubules ◽

Relationship Of ◽

Transverse Fractures ◽

The Relationship

The results of a freeze-etch study of skeletal muscle cells of a fish, the Black Mollie (Mollienesia sp), correlated well with published descriptions of sectioned material. The arrays of apertures of the T-tubules at the cell surface were clearly demonstrated. Numerous vesicles, communicating with the extracellular space, were also seen at the cell surface. The relationship of the T-tubules with the adjoining sarcotubular cisternae was studied; in transverse fractures at Z-levels there was a tendency for pieces of T-tubule to adhere to the cisternae No scalloping of the sarcotubular membrane was noted where it apposed the T-tubule, but some ridges on its luminal surface were demonstrated at these regions; elsewhere the luminal surface of the sarcotubular membrane was densely covered with particles. In the myofibrils, a reversal of polarity of the structure of the thick filaments was suggested at the M-line.

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