Glycolipids as markers of murine T and B lymphoblastoid tumour cell lines

Rosenfelder, Günter; Herbst, Hermann; Braun, Dietmar

doi:10.1016/0014-5793(80)81117-3

Cited by 16 publications

(6 citation statements)

References 20 publications

(2 reference statements)

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“…In humans, PNA receptors act as a differentiation antigen on monoblasts and monocytes (313). Glycolipid patterns also change as a function of lymphoid cell differentiation (314)(315)(316)(317)(318)(319)(320).…”

Section: Carbohydrate Differentiation Antigens In the Immune Systemmentioning

confidence: 99%

Carbohydrate structure in tumor immunity

Reading

Hutchins

1985

Cancer Metast Rev

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Researchers have endeavored to define surface alterations associated with neoplasia for at least 25 years. In comparisons of normal tissues with animal and human tumors, cultured cells before and after transformation with oncogenic agents, tumorigenic and nontumorigenic transformed cells, metastatic and nonmetastatic tumor cells, high- and low-metastatic variants, and tumor cells before and after induction of differentiation to a less malignant phenotype, a consistent finding has been some form of alteration in surface carbohydrate structures. These changes in glycolipids, glycoproteins and glycosaminoglycans are reviewed, and their structures are illustrated. Both nucleotide sugar biosynthesis and glycosyltransferase changes have been associated with these alterations. In some cases, alterations in transformed cells were related to growth, rather than transformation. In others, the altered glycoconjugates are truly tumor-associated. There is evidence that cell surface glycoconjugates may function in growth control. Altered carbohydrate structures could also serve as receptors for growth promoting factors and be directly responsible for altered growth control. Recent studies with monoclonal antibodies indicate that the vast majority of antibodies recognizing tumor-associated antigens are detecting altered carbohydrate structures. Mechanisms by which the immune system can recognize these carbohydrate structures are considered, and immune recognition of tumor-associated carbohydrate structural alterations is explored. A number of these hypotheses relating to alterations in glycosylation, growth control, and tumor immunity deserve further investigation.

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Section: Carbohydrate Differentiation Antigens In the Immune Systemmentioning

confidence: 99%

Carbohydrate structure in tumor immunity

Reading

Hutchins

1985

Cancer Metast Rev

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“…Studies from several laboratories have revealed the ganglioside differences among human leukocytes, leukemia cells, and leukemia cell lines (Tuboyama et Rosenfelder et al, 1980;Saito et al, 1980;Xia et al, 1989). We have shown that the ganglioside patterns can be useful for distinguishing different types of human leukemia cells (Tsuboyama et al, 1980).…”

Section: Discussionmentioning

confidence: 59%

“…The classification of myelogenous leukemia cells is primarily based on morphologic and cytochemical features. The extensive studies by Rosenfelder et al (1980Rosenfelder et al ( ,1982, Saito et al (1980), andRokukawa et al (1988) have indicated that glycolipids are excellent markers for diagnosis of leukemic cells and appear to be suitable for classification purposes. Most leukemic cells used in these studies are obtained by in vitro passage.…”

Section: Discussionmentioning

confidence: 99%

“…We previously reported that the ganglioside composition in human leukemic leukocytes undergoes dramatic changes during differentiation (Tsuboyama et al, 1980). Thereafter, several reports have also shown that alterations in glycolipid patterns occur in leukocytes undergoing differentiation (Rosenfelder et al, 1980(Rosenfelder et al, , 1982Saito et al, 1980; Lee et al, 1982; Kannagi & Hakomori, 1983; Kniep et al, 1983;Buehler et al, 1985;Nojiri et al, 1985;Taki et al, 1988;Rokukawa et tThis work was supported in part by a grant-in-aid for scientific research from the Ministry of Education, Science, and Culture of Japan (to T.A. and K.Y.)…”

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confidence: 96%

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Glycolipid changes in murine myelogenous leukemias: neutral glycolipids as markers for specific populations of leukemias

Ariga

Yoshida²,

Nemoto³

et al. 1991

Biochemistry

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We have studied the glycolipid composition of six different murine myelogenous leukemias as well as that of T-cell leukemias and normal spleen cells. Neutral and acidic lipid fractions were isolated by column chromatography on DEAE-Sephadex and analyzed by high-performance thin-layer chromatography (HPTLC) and an HPTLC overlay method. Murine myelogenous leukemias were found to contain globo- and ganglio-series neutral glycolipids, e.g., glucosylceramide (Glc-cer), lactosylceramide (Lac-cer), globotriaosylceramide (Gb3), globoside (Gb4), Forssman glycolipid (Gb5), and asialo-GM1 (GA1). Monoblastic leukemia cells contained increased proportions of Gb3, Gb4, Gb5, and GA1. Monocytic and myelomonocytic leukemia cells contained increased proportions of Glc-cer and Lac-cer. Especially, Glc-cer accounted for approximately 60% of the total neutral glycolipids in monocytic leukemia cells. Gb3 was the major neutral glycolipid in reticulum cell neoplasm type A, and it accounted for approximately 75% of the neutral glycolipids. GA1 was the major neutral glycolipid in myeloblastic and granulocytic leukemia cells as well as T-cell leukemias. Especially, granulocytic leukemia cells contained predominantly GA1, and it accounted for approximately 80% of the total neutral glycolipids. The pattern of gangliosides in myelogenous leukemias was more complex when compared with that of the neutral glycolipids; murine myelogenous leukemias contained at least 13 gangliosides, including such major gangliosides as GM1, GM1b containing N-acetyl neuraminic acid and N-glycolyl neuraminic acid, and Ga1NAc-GM1b. Alterations of glycolipid composition in murine myeloid leukemias may be associated with cellular differentiation and maturation, and therefore these characteristic glycolipid species may be regarded as markers for specific populations of leukemia cells.

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“…no animals or cell lines were available that lacked expression of GM1) [108][109][110]. Thus, it has been difficult to design experiments to directly evaluate the correlation between CT or LT-I and GM1 binding, adjuvanticity, and immunomodulation.…”

Section: Mutant Type I Hlts With Altered Ganglioside Binding Activitiesmentioning

confidence: 99%

Cholera toxin, LT-I, LT-IIa and LT-IIb: the critical role of ganglioside binding in immunomodulation by Type I and Type II heat-labile enterotoxins

Connell

2007

Expert Review of Vaccines

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The heat-labile enterotoxins (HLT) expressed by Vibrio cholerae (cholera toxin) and Escherichia coli (LT-I, LT-IIa, and LT-IIb) are potent systemic and mucosal adjuvants. Co-administration of the enterotoxins with a foreign antigen (Ag) produces an augmented immune response to that antigen. Although each enterotoxin has potent adjuvant properties, the means by which the enterotoxins induce various immune responses are distinctive for each adjuvant. Various mutants have been engineered to dissect the functions of the enterotoxins required for their adjuvanticity. The capacity to strongly bind to one or more specific ganglioside receptors appears to drive the distinctive immunomodulatory properties associated with each enterotoxin. Mutant enterotoxins with ablated or altered ganglioside binding affinities have been employed to investigate the role of gangliosides in enterotoxin-dependent immunomodulation.

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Glycolipids as markers of murine T and B lymphoblastoid tumour cell lines

Cited by 16 publications

References 20 publications

Carbohydrate structure in tumor immunity

Carbohydrate structure in tumor immunity

Glycolipid changes in murine myelogenous leukemias: neutral glycolipids as markers for specific populations of leukemias

Cholera toxin, LT-I, LT-IIa and LT-IIb: the critical role of ganglioside binding in immunomodulation by Type I and Type II heat-labile enterotoxins

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