Regulation of Immunoglobulin Synthesis by Dextran

Battisto, Jack R.; Pappas, F

doi:10.1084/jem.138.1.176

Cited by 25 publications

(8 citation statements)

References 30 publications

(13 reference statements)

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“…Recently, it was reported that unsubstituted dextrans show in vivo adjuvanticity (6). This can also be explained in terms of B-cell mitogenicity of these molecules, since other B-cell mitogens and Gram-negative bacteria (which contain B-cell mitogens) are known to be strong adjuvants.…”

Section: Discussionmentioning

confidence: 99%

Molecular Basis of B‐Cell Activation

1974

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The present experiments were performed in an attempt to investigate the nature of the surface receptor on B lymphocytes responsible for triggering of these cells. B‐cell mitogenicity of unsubstituted dextrans, quantitated by activation of DNA and antibody synthesis was detected only if the ligand had a MVC higher than 7 × 104. Above this threshold mitogenicity increased linearly with the log of the MW Substitution of the polymeric structure with lipid residues did not result in increased mitogenicity of the conjugate. However, sulphate substitution of the sugar units greatly enhanced the ability of the conjugates to activate DNA synthesis and. to a much smaller extent, antibody synthesis. Mitogenicity of sulphate derivatives was independent of their MW. Another polyanionic derivative (carboxymethyl) did not show increased mitogenicity. whereas a low‐MW compound very similar to dextran sulphate (pentosan sulphate) was highly active. The activation induced by dextrans was immunologically nonspecific and caused induction of polyclonal antibody synthesis. The activated cells presumably belong to a subset of B cells at a rather premature stage of differentiation. These findings suggest that the mitogenic signal is delivered to the cells by single sites at the membrane. These sites appear to have the capacity to interact with polysaccharide structures or releated conformations The polymeric structure of the active ligands is not a necessary requirement for mitogenicity and seems to have the accessory function of providing multipoint binding to low‐affinity receptors.

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Section: Discussionmentioning

confidence: 99%

Molecular Basis of B‐Cell Activation

1974

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“…May generate an immunoglobulin-M response (Azzopardi, Ferguson, and Thomas, 2011b) Degraded slowly (Azzopardi et al, 2011b;Battisto and Pappas, 1973) Tend to form nondegradable products during chemical modification (Battisto and Pappas, 1973) HES HES fractions may cause hypersensitivity and interfere with coagulation processes causing haemorrhage (Vercauteren, Bruneel, Schacht, et al, 1990;Zarychanski et al, 2013)…”

Section: Dextransmentioning

confidence: 99%

Polymer therapeutics in surgery: the next frontier

Azzopardi

Conlan

Whitaker

2016

Journal of Interdisciplinary Nanomedicine

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Polymer therapeutics is a successful branch of nanomedicine, which is now established in several facets of everyday practice. However, to our knowledge, no literature regarding the application of the underpinning principles, general safety, and potential of this versatile class to the perioperative patient has been published. This study provides an overview of polymer therapeutics applied to clinical surgery, including the evolution of this demand‐oriented scientific field, cutting‐edge concepts, its implications, and limitations, illustrated by products already in clinical use and promising ones in development. In particular, the effect of design of polymer therapeutics on biophysical and biochemical properties, the potential for targeted delivery, smart release, and safety are addressed. Emphasis is made on principles, giving examples in salient areas of demand in current surgical practice. Exposure of the practising surgeon to this versatile class is crucial to evaluate and maximise the benefits that this established field presents and to attract a new generation of clinician–scientists with the necessary knowledge mix to drive highly successful innovation.

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“…Dextran is unable to cause in vitro blastogenesis of mouse B and T cells, but it alters in vivo antibody synthesis of B cells to an unrelated antigenic stimulation [2]. In particular, administering it to mice before antigenic stimulation causes marked alteration in their abilities to synthesize IgM and IgG antibodies [2].…”

Section: Discussionmentioning

confidence: 99%

“…In particular, administering it to mice before antigenic stimulation causes marked alteration in their abilities to synthesize IgM and IgG antibodies [2]. Dextran was presumed to act primarily upon B cells but not on T cells [2].…”

Section: Discussionmentioning

confidence: 99%

Modulation of Mouse Anti-Trinitrophenyl Plaque-Forming Cell Affinity by Adjuvants or Lectins

Saito

Nakano

Kumazawa

1976

Japanese Journal of Microbiology

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The effects of several kinds of adjuvants or lectins, such as Corynebacterium parvum, dextran, poly AU, poly IC, dibutyryl cAMP, concanavalin A (Con A), phytohemagglutinin (PHA) and pokeweed mitogen (PWM) on anti-trinitrophenyl (TNP) direct plaque-forming cells (PFC) in the spleen of mice and the affinity of antibodies produced by these PFC were examined. The numbers of anti-TNP PFC in the spleens of mice which had been injected with C. parvum 7 days in advance were greater than those in controls after immunization with TNP-coupled heterologous erythrocytes, while the affinity of antibodies released by these PFC was not affected. On the contrary, simultaneous injection of dextran with TNP-erythrocytes did not increase the numbers of splenic anti-TNP PFC, but heightened the affinity of antibodies released by these PFC. Copolymers of nucleotides, poly AU and poly IC, were capable of enhancing splenic anti-TNP PFC responses, but showed almost no altering of PFC affinity. Dibutyryl cAMP did not have any effect on this system. Con A had potencies to both augment the number of anti-TNP PFC and heighten the PFC affinity, while PHA seemed to lack these potencies. Injection of PWM in the presence of antigen increased the number of anti-TNP PFC and heightened slightly the PFC affinity. These results indicate that the heightening of the affinity at the cellular level is regulated in ways different from the augmenting effects on the number of anti-TNP PFC by adjuvants or lectins. These results are discussed in the light of the mode of action of the substances used.The anti-hapten antibodies secreted by antibody-producing cells (B cells) after antigenic stimulation are heterogeneous with respect to their affinity for hapten, and the antibodies with higher affinity increase with time after the stimulation [17,26,29]. The affinity of the antibody reflects the properties of B cells rather than those of T helper cells [16], but the helper cells still seem to have some influence on the alteration of the affinity of anti-hapten antibodies [9,18,30,31]. Injection of complete Freund's adjuvant or bacterial lipopolysaccharide (LPS) concomitantly with antigen results in a heightening of the affinity of serum antibody [20]. LPS is known not only to be a powerful adjuvant [21] but also to have a potency as a polyclonal activator [22].Our previous studies [27] indicated that LPS in the presence of antigenic stimulation has some effect on hapten-specific B precursors in heightening the affinity or in selecting high affinity antibody-producing progeny cells, but the alteration of antibody affinity and the increase in number of antibody-producing cells induced by LPS are regulated by different mechanisms. There are many other adjuvants and mitogens such as Corynebacterium parvum, dextran, polynucleotides and lectins, which can stimulate T or B cells specifically and result in augmentation of immune responses. To examine whether these substances affect the affinity of antibodies secreted from antigenstimulated anti-hapten antibody-pr...

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Regulation of Immunoglobulin Synthesis by Dextran

Cited by 25 publications

References 30 publications

Molecular Basis of B‐Cell Activation

Molecular Basis of B‐Cell Activation

Polymer therapeutics in surgery: the next frontier

Modulation of Mouse Anti-Trinitrophenyl Plaque-Forming Cell Affinity by Adjuvants or Lectins

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