Anti-T antibodies and peanut-agglutinin-binding glycoproteins in sera of patients with gastric cancer

Hwang, Inchan; Nahm, Dong Ho; Cho, S.-N.; Longenecker, B. M.; Koganty, R. Rao; Park, In Suh

doi:10.1007/s004320050320

Cited by 4 publications

(2 citation statements)

References 20 publications

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“…The decrease in anti-T antibodies in sera of patients with gastric cancer might be due to immune complex formation between circulating PNA-binding glycoproteins and anti-T antibodies (Hwang et al, 1999).…”

Section: Mode Of Action Of Plant Lectinsmentioning

confidence: 99%

Lectins as Bioactive Plant Proteins: A Potential in Cancer Treatment

Mejı́a

Prisecaru

2005

Critical Reviews in Food Science and Nutrition

297

159

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Plant lectins, a unique group of proteins and glycoproteins with potent biological activity, occur in foods like wheat, corn, tomato, peanut, kidney bean, banana, pea, lentil, soybean, mushroom, rice, and potato. Thus, dietary intakes by humans can be significant. Many lectins resist digestion, survive gut passage, and bind to gastrointestinal cells and/or enter the circulation intact, maintaining full biological activity. Several lectins have been found to possess anticancer properties in vitro, in vivo, and in human case studies; they are used as therapeutic agents, preferentially binding to cancer cell membranes or their receptors, causing cytotoxicity, apoptosis, and inhibition of tumor growth. These compounds can become internalized into cells, causing cancer cell agglutination and/or aggregation. Ingestion of lectins also sequesters the available body pool of polyamines, thereby thwarting cancer cell growth. They also affect the immune system by altering the production of various interleukins, or by activating certain protein kinases. Lectins can bind to ribosomes and inhibit protein synthesis. They also modify the cell cycle by inducing non-apoptotic G1-phase accumulation mechanisms, G2/M phase cell cycle arrest and apoptosis, and can activate the caspase cascade. Lectins can also downregulate telomerase activity and inhibit angiogenesis. Although lectins seem to have great potential as anticancer agents, further research is still needed and should include a genomic and proteomic approach.

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Section: Mode Of Action Of Plant Lectinsmentioning

confidence: 99%

Lectins as Bioactive Plant Proteins: A Potential in Cancer Treatment

Mejı́a

Prisecaru

2005

Critical Reviews in Food Science and Nutrition

297

159

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“…In addition to the truncated mucins that cover the plasma membrane of epithelial tumour cells, mucin molecules with altered O‐ glycan chains may be shed and appear in the bloodstream. Epithelial tumour progression and aggressiveness were found to be associated with a high serum concentration of glycans, which exposes the T antigen 24 , and which has an immunosuppressive function.…”

Section: Introductionmentioning

confidence: 99%

Immune response to Thomsen–Friedenreich disaccharide and glycan engineering

et al. 2005

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Summary Cancer-associated mucins show frequent alterations of their oligosaccharide chain profile, with a switch to unmask normally cryptic O-glycan backbone and core regions. Epithelial tumour cells typically show overexpression of the uncovered Gal β 1-3GalNAc α -O-Ser/Thr (Core 1) structure, known as the T antigen or the Thomsen-Friedenreich antigen, the oligosaccharide chain of which is called the Thomsen-Friedenreich disaccharide (TFD). T antigen expression has been associated with immunosuppression, metastasis dissemination, and the proliferation of cancer cells. Several different strategies have been used to trigger a specific immune response to TFD. Natural T antigen and synthetic TFD residues have low immunodominance. In the T antigen, flexibility of the glycosidic bond reduces the immunogenicity of the sugar residue. Enhanced rigidity should favour certain glycan conformations and thereby improve TFD immunotargeting. We propose the term 'glycan engineering' for this approach. Such engineering of TFD should reduce the flexibility of its glycan moiety and thereby enhance its stability, rigidity and immunogenicity.

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Brigati

Noonan

Albini

et al. 2002

Clinical and Experimental Metastasis

205

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The recognition of a role for inflammation in the natural history of a tumor has a long record, stretching from the mid-19th century. From the times of Virkow, who postulated that cancer originates from inflamed tissues, to Metchnikoff and many others, this field has continued to excite (and divide) the scientific community. The question as to whether the inflammatory infiltrate helps or hinders tumors is still open. In a sense, modern molecular biology has, if anything, worsened this dualism, and the literature on this issue shows a plethora of conflicting reports. We would like to provide another contribution to this topic, which was the subject of a recent brilliant review (Balkwill F and Mantovani A. Lancet 2001; 357: 539-45), by focussing more specifically to the relation between inflammation and tumor invasion and how this could drive rational therapeutic approaches.

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Anti-T antibodies and peanut-agglutinin-binding glycoproteins in sera of patients with gastric cancer

Cited by 4 publications

References 20 publications

Lectins as Bioactive Plant Proteins: A Potential in Cancer Treatment

Lectins as Bioactive Plant Proteins: A Potential in Cancer Treatment

Immune response to Thomsen–Friedenreich disaccharide and glycan engineering

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