Effects of succinyl-con A on the growth of normal and transformed cells

Trowbridge, Ian S.; Hilborn, David A.

doi:10.1038/250304a0

Cited by 19 publications

(4 citation statements)

References 23 publications

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“…Gunther etal. (1973) and Trowbridge and Hilborn (1974)]. However, the present study shows that Man7-Man9 oligomannose-type glycopeptides have approximately 4-and 10-fold reduced affinities, respectively, for dimeric Con A and its acetyl-and succinyl-derivatives relative to tetrameric Con A.…”

Section: Resultscontrasting

confidence: 49%

“…0006-2960/93/0432-5116$04.00/0 Succinyl-and acetyl-Con A are pH-independent dimeric derivatives of the lectin which have been widely used to determine the effects of Con A valency on its biological activities (Gunther et al, 1973;Wang et al, 1976). Such studies include a comparison of thymidine-induced incorporation and mitogenic effects of succinyl-Con A and native tetrameric Con A in normal and transformed cells (Trowbridge & Hilborn, 1974), investigations of the "capping" behavior of cell receptors for dimeric and tetrameric Con A (Gunther et al, 1973), and the cell agglutination properties of dimeric versus tetrameric Con A (Gunther et al, 1973). In view of the similar affinities of acetyl-and succinyl-Con A and the native lectin for monosaccharides such as methyl a-Dglucopyranoside, differences in their biological activities have been attributed to differences in their valencies (Gunther et al, 1973).…”

mentioning

confidence: 99%

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Differences in the binding affinities of dimeric concanavalin A (including acetyl and succinyl derivatives) and tetrameric concanavalin A with large oligomannose-type glycopeptides

Mandal¹,

Brewer²

1993

Biochemistry

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Dimeric derivatives of concanavalin A (Con A) such as acetyl- and succinyl-Con A have been used for years as probes of cellular membranes. The altered binding and biological activities of these derivatives relative to native tetrameric Con A have generally been attributed to their reduced valence. However, the present study shows that acetyl- and succinyl-Con A possess lower affinities than tetrameric Con A toward certain oligomannose-type glycopeptides which are found on the surface of cells. It has previously been shown that native tetrameric Con A possesses 5-30-fold enhanced affinities toward Man7-Man9 oligomannose-type glycopeptides, respectively, relative to Man5 and Man6 oligomannose-type glycopeptides [Bhattacharyya, L., & Brewer, C. F. (1989) Eur. J. Biochem. 178, 721-726]. Using titration microcalorimetry and hemagglutination inhibition measurements, methyl alpha-D-mannopyranoside, methyl 3,6-di-O-(alpha-D-mannopyranosyl)-alpha-D-mannopyranoside (which binds with about 60-fold higher affinity than methyl alpha-D-mannopyranoside and is the major Con A binding epitope on oligomannose-type carbohydrates), and a Man5 oligomannose-type oligosaccharide are shown to bind to underivatized dimeric Con A at pH 5.2 and acetyl- and succinyl-Con A at pH 7.2 with affinities equal to those of native tetrameric Con A. However, a mixture of Man7 and Man8 glycopeptides and a Man9 oligomannose-type glycopeptide were shown to bind to underivatized dimeric Con A and acetyl- and succinyl-Con A with affinities only about 2-fold higher than the Man5 oligosaccharide, in contrast to the higher affinities of native tetrameric Con A for these carbohydrates.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Resultscontrasting

confidence: 49%

mentioning

confidence: 99%

Differences in the binding affinities of dimeric concanavalin A (including acetyl and succinyl derivatives) and tetrameric concanavalin A with large oligomannose-type glycopeptides

Mandal¹,

Brewer²

1993

Biochemistry

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“…The dimer, however, is still capable of binding low molecular weight sugar deriva tives and yeast mannan (92) or binding to the surface of transformed cells (105). The dimer in the fo rm of succinyl-Con A is also equally effective as a mitogen as native Con A (219) and, in contrast to an earlier report (269), is capable of inhibiting the growth of normal and transformed cells by an effect manifested during the early G1 phase of the cell cycle (159). Agglutination or precipitation may therefore represent a two-step process: the first step involving a simple monovalent or possibly divalent binding process which is apparently sufficient to trigger mitogenesis or to inhibit cell growth, and a second step involving a multivalent process in which the cross-linking of macromolecules, or of cell surface receptor sites, results in the precipitation of macromolecules or in the agglutination of cells respectively.…”

Section: Assays For Biological Activitycontrasting

confidence: 49%

Phytohemagglutinins (Phytolectins)

Liener¹

1976

Annu. Rev. Plant. Physiol.

234

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“…Succinyl-Con A was found not to alter significantly the growth rates of SV3T3, Py3T3 or 3T3 itself (Trowbridge and Hilborn, 1974).…”

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confidence: 70%

Studies on the relationship between concanavalin A and SV40-transformed human fibroblasts

Webb¹

1976

Br J Cancer

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Summary.-The extent of binding of 1251-Con A to the surface of SV40-transformed human fibroblasts and the degree of agglutination of the cells by the native lectin have been measured. In addition, trypsinized and succinylated Con A have been used to study the effects of the lectin upon certain cell growth parameters. Trypsinized Con A was found to alter the growth rate, the saturation density and the contact inhibition of the transformed cells, an effect not neutralized by oz-methyl-D-mannoside.

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Effects of succinyl-con A on the growth of normal and transformed cells

Cited by 19 publications

References 23 publications

Differences in the binding affinities of dimeric concanavalin A (including acetyl and succinyl derivatives) and tetrameric concanavalin A with large oligomannose-type glycopeptides

Differences in the binding affinities of dimeric concanavalin A (including acetyl and succinyl derivatives) and tetrameric concanavalin A with large oligomannose-type glycopeptides

Phytohemagglutinins (Phytolectins)

Studies on the relationship between concanavalin A and SV40-transformed human fibroblasts

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