Factors Affecting the Redistribution of Surface-Bound Concanavalin a on Human Polymorphonuclear Leukocytes

Ryan, Graeme B.; Borysenko, Joan Z.; Karnovsky, Morris J.

doi:10.1083/jcb.62.2.351

Cited by 122 publications

(36 citation statements)

References 25 publications

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“…Ryan et al (1974) did observe a gradient of fluorescence labeling on polymorphonuclear leucocytes. Braun et al (1978) reported that some membrane proteins were concentrated in one end of pre-fixed polarized lymphocytes.…”

Section: Discussionmentioning

confidence: 97%

Analysis of lateral redistribution of a plasma membrane glycoprotein- monoclonal antibody complex [corrected] [published erratum appears in J Cell Biol 1988 Apr;106(4):following 1403]

Ishihara

Holifield

Jacobson

1988

The Journal of Cell Biology

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Abstract. The lateral redistribution of a major murine glycoprotein, GP80, was studied on locomoting fibroblasts, using rhodamine-conjugated mAbs and ultralow light level digitized fluorescence microscopy. Confirming an earlier study (Jacobson, K., D. O'Dell, B. Holifield, T. L. Murphy, and J. T. August. 1984. J. Cell Biol. 99:1613-1623, the distribution of GP80 was coupled with cell locomotion; motile cells exhibited a gradated distribution of the GP80-mAb complex over the cell surface, increasing from the front to the rear, whereas stationary cells exhibited a nearly uniform GP80 distribution. By monitoring locomoting single cells, we found the gradated fluorescence distribution to be maintained as an approximate steady state. Newly extended leading edges were almost devoid of the fluorescence labeling. This was strikingly demonstrated in prechilled cells in which the extension of fluorescence-free leading edges caused a pronounced boundary between fluorescent and nonfluorescent zones. Subsequently this boundary eroded gradually in a manner consistent with diffusional relaxation. Evidence indicated that the GP80 redistribution was primarily caused by the lateral motion of GP80 in the plasma membrane and not via intracellular membrane traffic. Two cell locomotion models which, in principle, could account for the GP80 redistribution were tested: the retrograde lipid flow (RLF) model (Bretscher, M. S., 1984. Science (Wash. DC).224:681-686) and an alternative hypothesis, the retraction-induced spreading (RIS) model. The predictions of these models were simulated by computer and compared with experiment to assess which model was more appropriate. Whereas both models predicted steady-state gradients similar to the experimental result, only the RIS model predicted the lack of retrograde movement of the fluorescent boundary.

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Section: Discussionmentioning

confidence: 97%

Analysis of lateral redistribution of a plasma membrane glycoprotein- monoclonal antibody complex [corrected] [published erratum appears in J Cell Biol 1988 Apr;106(4):following 1403]

Ishihara

Holifield

Jacobson

1988

The Journal of Cell Biology

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“…This network could then either transfer the message to other parts of the cell or itself direct the rearrangement, de Petris (14) has suggested that such a network could be provided by microfilaments because of the effects of cytochalasin B on label-induced rearrangement. He and others (44,56) have found a cooperative inhibitory effect of cytochalasin B and colchicine on capping, indicating that a microtubule system may be involved as well. Networks of microfilamerits (49) and microtubules (40) are present below the cell surface, but there is no absolutely conclusive evidence for the direct involvement of such networks in the arrangement of surface molecules.…”

Section: Discussionmentioning

confidence: 99%

Reversibility of cell surface label rearrangement.

Brown¹,

Revel²

1976

The Journal of Cell Biology

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Cell surface labeling can cause rearrangements of randomly distributed membrane components. Removal of the label bound to the cell surface allows the membrane components to return to their original random distribution, demonstrating that label is necessary to maintain as well as to induce rearrangements. With scanning electron microscopy, the rearrangement of concanavalin A (con A) and ricin binding sites on LA-9 cells has been followed by means of hemocyanin, a visual label. The removal of con A from its binding sites at the cell surface with alpha-methyl mannoside, and the return of these sites to their original distribution are also followed in this manner.There are labeling differences with con A and ricin. Under some conditions, however, the same rearrangements are seen with both lectins. The disappearance of labeled sites from areas of ruffling activity is a major feature of the rearrangements seen. Both this ruffling activity and the rearrangement of label are sensitive to cytochalasin B, and ruffling activity, perhaps along with other cytochalasin-sensitire structure, may play a role in the rearrangements of labeled sites.Evidence from a number of laboratories indicates that the application of label to cell surfaces causes a rearrangement of randomly distributed membrane molecules (12,15,20,30,35,43,51,53). Rearrangement is not a general membrane phenomenon, but involves only the labeled sites; surface molecules which do not interact with the label remain in a random, homogeneous distribution (29). It is not known how the interaction between label and receptor causes rearrangement.Two components can be recognized during label-induced rearrangement (12,35,53,55): the formation of clusters of label; and the preferential relocation of label to certain areas on the cell and away from others, e.g., capping. It has been proposed that the first component, clustering, results from crosslinking of surface sites by multivalent label molecules, since univalent antibody fragments appear uniformly distributed on the cell surface (16,35,53). Stackpole et al. (50), however, have demonstrated that clustering can occur even with strictly univalent reagents. They suggest that interaction of label with its binding sites may cause an alteration which thermodynamically favors aggregation. The second component of rearrangement must involve more than crosslinking or aggregation of labeled molecules in the plane of the membrane; it requires energy (12,15,20,35,53,57) and must therefore be directed by some activity of the cell.In this communication we follow the rearrangements at the cell surface obtained with two different lectins and show that the label-receptor interaction is necessary for the maintenance as well as the induction of rearrangements. Mechanisms consistent with our findings whereby label-receptor THE JOURNAL OF CELL BIOLOGY 9 VOLUME 68, 1976 9 pages 629-641 629

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“…(b) The serine proteases might be associated with the movement of the macromolecules in the surface membrane; as it has been suggested that the triggering of the metabolic activation of phagocytic cells is provided by a surface redistribution of the ligand-receptor complexes, which may perturb the surface membrane to activate the NAD(P)H oxidase (30). If this is the case, it may be possible that impaired movement of the macromolecules in the surface membrane may also contribute to the inhibition of chemiiotaxis and phagocytosis in addition to°2 production by serine protease inhibitors, inasmuch as chemotaxis and phagocytosis also accompany the movement of the macromolecules in the surface membrane (35)(36)(37).…”

Section: Discussionmentioning

confidence: 99%

Evidence that proteases are involved in superoxide production by human polymorphonuclear leukocytes and monocytes.

Kitagawa¹,

Takaku²,

Sakamoto³

1980

J. Clin. Invest.

134

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A B S T R A C T The possible participation of proteases in superoxide (O°) production by human polymorphonuclear leukocytes (PMN) and monocytes was explored using various protease inhibitors and substrates. Protease inhibitors used included naturally occurring inhibitors of serine proteases and synthetic inhibitors that modify the active site of serine proteases. Substrates used were synthetic substrates of the chymotrypsin type as well as trypsin type ofprotease. All these inhibitors and substrates inhibited O2 production by human PMN and monocytes induced by cytochalasin E and concanavalin A, though PMN were more sensitive to these inhibitors and substrates than monocytes. Inhibition appeared rapidly even when the inhibitors were added at the same time as the stimulants, during the "induction time of O2 production" or at the time of maximum O2 production, whereas much greater inhibition was observed when the cells were preincubated with the inhibitors. These observations suggest that enzymatically active serine proteases are essential for these phagocytic cells to initiate and maintain the O2 production in response to the stimuli. The inhibitory effect of the inhibitor and substrate for chymotrypsin type protease was greater than that of those substances for trypsin-type protease. Macromolecular inhibitors also inhibited the O2 production.These findings suggest that the serine proteases involved in the O2 production by human PMN and monocytes are similar to chymotrypsin rather than trypsin, and are possibly located at the cell surface membrane.

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Factors Affecting the Redistribution of Surface-Bound Concanavalin a on Human Polymorphonuclear Leukocytes

Cited by 122 publications

References 25 publications

Analysis of lateral redistribution of a plasma membrane glycoprotein- monoclonal antibody complex [corrected] [published erratum appears in J Cell Biol 1988 Apr;106(4):following 1403]

Analysis of lateral redistribution of a plasma membrane glycoprotein- monoclonal antibody complex [corrected] [published erratum appears in J Cell Biol 1988 Apr;106(4):following 1403]

Reversibility of cell surface label rearrangement.

Evidence that proteases are involved in superoxide production by human polymorphonuclear leukocytes and monocytes.

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