Tn, a carcinoma-associated antigen, reacts with anti-Tn of normal human sera

Springer, Georg F.; Taylor, Clive R.; Howard, Donald; Tegtmeyer, H.; Desai, Pankaja; Murthy, Satya; Felder, Barbara; Scanlon, Edward F.

doi:10.1002/1097-0142(19850201)55:3<561::aid-cncr2820550315>3.0.co;2-1

Cited by 75 publications

(25 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A similar inhibition may also be achieved by anti-A antibodies toward incompatible A antigens expressed in cancers occurring in group B and O individuals and also by anti-T nouvelle antibodies toward the cryptic T-nouvelle (CD175) antigen (GalNAca1-Ser/Thr), observed frequently in a variety of cancers, including hematological malignancies. 62,63 Crossreactions may also occur as a result of the overlapping structural homology among those antigens. Furthermore, immune cells may also be involved in addition to antibodies.…”

Section: Discussionmentioning

confidence: 99%

ABO blood group A transferases catalyze the biosynthesis of FORS blood group FORS1 antigen upon deletion of exon 3 or 4

2017

View full text Add to dashboard Cite

Key Points• ABO blood group A transferases possess intrinsic FS activity upon deletion of exon 3 or 4 of A transferase messenger RNAs.• Cointroduction of exon 3 or 4 deletion and GlyGlyAla substitution synergistically confers human A transferases with strong FS activity. (B3GALNT1) cells, and cell-surface expression of FORS1 was immunologically monitored. To our surprise, the deletion of exon 3 or 4, but not of exon 2 or 5, of human AT transcripts bestowed moderate FS activity, indicating that the A allele is inherently capable of producing a protein with FS activity. Because RNA splicing is frequently altered in cancer, this mechanism may explain, at least partially, the appearance of FORS1 in human cancer. Furthermore, strong FS activity was attained, in addition to AT and BT activities, by cointroducing 1 of those deletions and the GlyGlyAla substitution, possibly by the synergistic effects of altered intraGolgi localization/conformation by the former and modified enzyme specificity by the latter.

show abstract

Section: Discussionmentioning

confidence: 99%

ABO blood group A transferases catalyze the biosynthesis of FORS blood group FORS1 antigen upon deletion of exon 3 or 4

2017

View full text Add to dashboard Cite

show abstract

“…The normal breast epithelial cell line HBL100 did not express T or Tn antigen, both of which seldom appear in normal breast epithelium or other tissues 10,11) except in the healthy colon, and uterine cervix.…”

Section: Discussionmentioning

confidence: 99%

Specific Role of T and Tn Tumor‐associated Antigens in Adhesion between a Human Breast Carcinoma Cell Line and a Normal Human Breast Epithelial Cell Line

Kishikawa

Ghazizadeh

Sasaki

et al. 1999

Japanese Journal of Cancer Research

Self Cite

View full text Add to dashboard Cite

The possibility that tumor-associated antigens T and Tn act as adhesion molecules between normal and malignant breast epithelial cells at the early stages of recognition in the metastatic pathway was examined in vitro. The adhesive specificity of the antigens was assessed by means of in vitro adhesion tests between a carcinomatous breast cancer cell line (ZR75-30) and a normal epithelial breast cell line (HLB100) using both monoclonal antibodies and lectins specific as well as nonspecific for each antigen. Adhesion assay was performed using monolayers of the normal cell line prepared on plastic culture plates and the tumor cell line labeled with a fluorescent dye as a probe. The adhesion between the two cell types occurred with significant specificity via T and Tn antigens (P < < < <0.001), and was temperature-dependent. The results suggest that at the early stages of recognition by tumor cells in the metastatic process, T and Tn antigens play a role as adhesion molecules between the tumor cells and adjacent normal cells. Key words: Breast carcinoma -Cell line -Adhesion -T and Tn antigensCell-cell interactions are of obvious importance not only in normal physiological processes, but also in the processes of proliferation and invasion of carcinoma (CA) cells, [1][2][3] and metastasis. 4) Several steps in cancer invasion have been investigated. The first step is considered to be the release of cancer cells from the primary cancer lesion due to the regulatory effects of E-cadherin-related systems. 5,6) In the second step, the released cancer cells make contact with nearby normal epithelial cells before reaching the extra-cellular matrix or vascular endothelial cells. This step may be one of the most important in the very early stage of the metastatic processes, such as in the intraductal invasion of breast cancer cells. Little attention, however, has been paid to this event, i.e., the interaction or the binding of malignant cells to healthy (normal) cells immediately after release from the original cancer lesion.Among the tumor-associated antigenic glycoproteins, T [Gal(β1-3)GalNAc(α1-3)Ser/Thr] and Tn [GalNAc(α1-3)-Ser/Thr] antigens were first described as cryptic determinants on human erythrocytes 7) that were exposed by neuraminidase treatment. These pan-CA auto-antigens [8][9][10] play a profound role in cancer pathogenesis. 11) Specific adhesion between invasive, metastatic murine Esb T-lymphoma cells and syngeneic hepatocytes has been demonstrated 12, 13) ; direct molecular binding of the Esb cells, which were later confirmed to strongly express T and Tn antigens on their cell surfaces, 14) to the corresponding ligands was the first step after the recognition of hepatocyte ligands. Moreover, cultured breast CA DU4475 cells and desialylated, isologous erythrocytes [TRBC] bound specifically to the Gal/GalNAc receptors of rat Kupffer cells and of hepatocytes. 15,16) These findings suggest that T and/or Tn antigens on released cancer cells might have a role in adhesion of these cells to normal cells in the early ...

show abstract

“…The Tn antigen has also been described by Springer and associates as the precursor of the Thomsen-Friedenreich antigen (T antigen), and both Tn and T antigens are expressed in breast cancer tissue (27). More recently, Springer and associates observed a weak anti-Tn antibody in normal human antisera and applied it in the detection of the cancer-associated Tn antigen by immunohistology and absorption assay (28). They claimed that Tn antigen expression (in terms of absorption titer) in highly metastatic tumors was greater than in less metastatic differentiated tumors.…”

Section: Discussionmentioning

confidence: 99%

Blood group A cross-reacting epitope defined by monoclonal antibodies NCC-LU-35 and -81 expressed in cancer of blood group O or B individuals: its identification as Tn antigen.

Hirohashi¹,

Clausen²,

Yamada³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

162

View full text Add to dashboard Cite

Two monoclonal antibodies, NCC-LU-35 and NCC-LU-81, have been established after immunization of mice with membrane preparations of human lung cancer Lu65 tumor xenograft cells grown in vivo and intact cells cultured in vitro, respectively. These two antibodies react specifically with a majority of human adenocarcinomas, irrespective of the host's blood group ABO status, as well as with normal tissues and erythrocytes of blood group A individuals. The antigenicity is associated with a high molecular weight mucin-like glycoprotein separated by gel filtration of Lu65 tumor extracts. The epitope of the mucin-like glycoprotein has been identified as a-N-acetylgalactosaminyl residue directly linked O-glycosidically to serine or threonine residues of polypeptides. This epitope was serologically detected several years ago and given the name Tn. Our identification of the epitope is based on the following results: (i) The antigen is sensitive to a-Nacetylgalactosaminidase, but not to sialidase or a-fucosidase.(ii) Various mono-and difucosyl A determinants, either type 1 or type 2 chain, cross-react with both antibodies. (ii) The reactivity with both antibodies can be created by treatment of glycophorin A of normal erythrocytes with sialidase followed by 13-galactosidase. Monoclonal antibodies NCC-LU-35 and NCC-LU-81 were established after immunization of mice with lung carcinoma Lu65 cells. The antigen defined by both antibodies is not expressed in various normal tissues of blood group B and 0 hosts, but it is strongly expressed in various adenocarcinomas derived from blood group B and 0 as well as A hosts.

show abstract

Tn, a carcinoma-associated antigen, reacts with anti-Tn of normal human sera

Cited by 75 publications

References 36 publications

ABO blood group A transferases catalyze the biosynthesis of FORS blood group FORS1 antigen upon deletion of exon 3 or 4

ABO blood group A transferases catalyze the biosynthesis of FORS blood group FORS1 antigen upon deletion of exon 3 or 4

Specific Role of T and Tn Tumor‐associated Antigens in Adhesion between a Human Breast Carcinoma Cell Line and a Normal Human Breast Epithelial Cell Line

Blood group A cross-reacting epitope defined by monoclonal antibodies NCC-LU-35 and -81 expressed in cancer of blood group O or B individuals: its identification as Tn antigen.

Contact Info

Product

Resources

About