Glycan bioengineering in immunogen design for tumor T antigen immunotargeting

Sendra, Víctor G.; Zlocowski, Natacha; Ditamo, Yanina; Copioli, Silvina; Tarp, Mads P.; Bennett, Eric; Clausen, Henrik; Roth, German A.; Nores, Gustavo A.; Irazoqui, Fernando J.

doi:10.1016/j.molimm.2009.08.007

Cited by 3 publications

(5 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The evolution and progression of tumors have a direct relation with the homeostasis of immune system where immunosupression facilitates the tumor cell growth. 23 However the in vivo immunosupression generated by ABL allowed an enhancement of CT26 tumor cell growth. These results show the significance of ABL inducing downregulation of macrophage and T lymphocyte protective functions with the consequence of faster tumor cell growth.…”

Section: Discussionmentioning

confidence: 99%

“…ABL has been described as an important inhibitor of epithelial tumor cell proliferation in in vitro assays of colon HT29, colon Caco-2, breast MCF7, 37 retinal pigment epithelium 14,38 and colon CT26 cells. 23 However the in vivo immunosupression generated by ABL allowed an enhancement of CT26 tumor cell growth. This result shows that downregulation by oral treatment of ABL was more relevant in immune system that in in vivo tumor cell proliferation.…”

Section: Discussionmentioning

confidence: 99%

“…23 Animals were sacrificed when tumor diameter exceeded 50 mm diameter, or when there were signs of distress. Animals received daily oral doses of ABL (10 µg per animal per day) or vehicle alone seven days before tumor implantation and through the end of the experiment.…”

Section: In Vivo Tumor Growthmentioning

confidence: 99%

“…CT26 tumor growth was monitored from 50 mm 3 (5 mm diameter) to 3.200 mm 3 (20 mm diameter). 23 Animals were sacrificed when tumor diameter exceeded 50 mm diameter, or when there were signs of distress.…”

Section: In Vivo Tumor Growthmentioning

confidence: 99%

See 3 more Smart Citations

In vivo immunomodulatory effect of the lectin from edible mushroom Agaricus bisporus

et al. 2016

Self Cite

View full text Add to dashboard Cite

Lectins are glycan-binding proteins that are resistant to digestion in the gastrointestinal tract and enter intact to blood circulation. The aim of this study was to evaluate the influence of edible mushroom Agaricus bisporus lectin (ABL) on innate and adaptive immune responses as well as its effect in two different experimental pathologies that involve the immune system. ABL inhibited in vitro nitric oxide (NO) production by mouse peritoneal macrophages in response to the pro-inflammatory stimuli lipopolysaccharides (LPS). However, it did not modify the activity of arginase, showing that while ABL downregulates M1 activation, it does not affect M2 activation. ABL also inhibited mononuclear cell proliferation in response to mitogen Con A, or in a mixed lymphocyte reaction. During the in vivo studies, oral administration of ABL to BALB/c mice induced a marked inhibition of NO production by peritoneal macrophages after LPS stimuli. The influence of ABL on tumor growth was studied in BALB/c mice receiving daily oral doses of ABL and implanted with CT26 tumor cells. ABL treatment induced significantly higher rate of tumor growth when compared with control mice. On the other hand, oral ABL administration in Wistar rats induced a marked diminution of the incidence of the disease and the severity of the clinical signs of experimental autoimmune encephalomyelitis. We can conclude that ABL has an in vivo immunomodulatory effect reducing the innate and adaptive responses. This food lectin shows potential therapeutic application on control of inflammatory autoimmune pathologies.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: In Vivo Tumor Growthmentioning

confidence: 99%

Section: In Vivo Tumor Growthmentioning

confidence: 99%

See 2 more Smart Citations

In vivo immunomodulatory effect of the lectin from edible mushroom Agaricus bisporus

et al. 2016

Self Cite

View full text Add to dashboard Cite

show abstract

“…Modification of glycosylation to effect deglycosylation of rhamnosylated drugs (Garnier et al, 2010) Gal-β-3GalNAc-α-Lys 5 TOF Immunogen design for tumor T antigen immuno-targeting (Sendra et al, 2009) Glycopolypeptide-based cholera toxin inhibitors MALDI Effect of peptide charge and glycan linker length on activity (Maheshwari et al, 2010) Glycopeptide carrying tetra-N-Ac-lactosamine containing core 2 decasaccharide TOF (DHB) Solid-phase synthesis (Ueki et al, 2010) Glycosaminoglycan-protein linkage tetraosyl peptide moieties of betaglycan TOF To investigate structures that best serve as a hexosamine acceptor for enzymatic glycosyl transfer (Tamura et al, 2010) Glycosulfopeptides from Nterminus of human endoglycan TOF/TOF (THAP)…”

Section: Tof (Dhb)mentioning

confidence: 99%

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2009–2010

Harvey

2014

Mass Spectrometry Reviews

View full text Add to dashboard Cite

This review is the sixth update of the original article published in 1999 on the application of MALDI mass spectrometry to the analysis of carbohydrates and glycoconjugates and brings coverage of the literature to the end of 2010. General aspects such as theory of the MALDI process, matrices, derivatization, MALDI imaging, arrays and fragmentation are covered in the first part of the review and applications to various structural typed constitutes the remainder. The main groups of compound that are discussed in this section are oligo and polysaccharides, glycoproteins, glycolipids, glycosides and biopharmaceuticals. Many of these applications are presented in tabular form. Also discussed are medical and industrial applications of the technique, studies of enzyme reactions and applications to chemical synthesis.

show abstract

Anti-Thomsen-Friedenreich-Ag anti-TF-Ag potential for cancer therapy

Rittenhouse-Olson¹

2012

Front Biosci

View full text Add to dashboard Cite

Thomsen-Friedenreich antigen (TF-Ag) is the disaccharide (Gal beta1-3 GalNAc alpha), which is also known as the core 1 structure. The presence of this disaccharide on the surface of approximately 90 percent of carcinomas is due to altered glycosylation in these tumors. TF-Ag plays a role in the adhesive properties of tumor cells involved in metastasis. Treatment of mice with JAA-F11, a monoclonal antibody to TF-Ag alpha inhibited lung metastasis and improved prognosis in a mouse breast cancer model. The presence of naturally occurring antibodies to TF-Ag in cancer patients is related to improved prognosis. The pancarcinoma expression of TF-Ag, combined with the evidence of a mechanistic role for TF-Ag in cancer spread, show that this target would have clinical utility. The presence of naturally occurring antibody to TF-Ag indicates that increasing the anti-TF-Ag antibody would be safe for the cancer patient and indicates that tolerance would not have to be broken to create this immune response. Finally, the prognostic improvements seen clinically and in animal models indicate that this is an important vaccine target.

show abstract

Glycan bioengineering in immunogen design for tumor T antigen immunotargeting

Cited by 3 publications

References 46 publications

In vivo immunomodulatory effect of the lectin from edible mushroom Agaricus bisporus

In vivo immunomodulatory effect of the lectin from edible mushroom Agaricus bisporus

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2009–2010

Anti-Thomsen-Friedenreich-Ag anti-TF-Ag potential for cancer therapy

Contact Info

Product

Resources

About