Human blood groups M-, N-, T-, and Tn-specific substances in lipidic extracts of line 10 hepatocarcinoma of Strain 2 guinea pigs

Springer, Georg F.; Cantrell, John L.; Desai, Pankaja; Tegtmeyer, H.

doi:10.1016/0090-1229(82)90017-4

Cited by 14 publications

(2 citation statements)

References 27 publications

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“…disintegrated cultured cells. 16 Absorption was for 30 minutes at 2 1 to 23 " C and then for 2 hours at 4"C, with occasional a g i t a t i~n .~~.~, The standards were unabsorbed, volume-adjusted, antibody-containing fluids. Anti-serum absorbed with an equal volume of 0 , M M RBC served as a control (except for anti-N, since all RBC have N).…”

Section: Serologic Proceduresmentioning

confidence: 99%

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

Springer

Taylor

Howard

et al. 1985

Cancer

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Tn antigen is the immediate precursor of the carcinoma (CA)‐associated T antigen; both are masked in non‐CA tissues. Tn antigen was detected by absorption of human anti‐Tn antibody in 46 of 50 primary breast CAs and in all 6 metastases originating from Tn‐positive primary CAs. Thirteen of 25 (52%) anaplastic CAs, but only 2 of 15 (13%) well differentiated CAs had more Tn than T; 1 anaplastic CA had neither antigen. Eighteen of 20 benign breast lesions had no Tn; the 2 positive lesions were premalignant. All 19 breast CAs, studied immunohistochemically, reacted strongly with human polyclonal anti‐Tn; benign or normal glandular tissues had minimal or no reactivity. Among live cancer cell lines, the most malignant sublines had more Tn than T on their cell surfaces. Preliminary studies with rodent monoclonal anti‐Tn and anti‐T antibodies gave immunohistochemical reactivity patterns similar to those of the polyclonal antibodies, but the former were less sensitive in absorption tests. Tn is a CA marker that promises to be useful in tumor detection.

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Section: Serologic Proceduresmentioning

confidence: 99%

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

Springer

Taylor

Howard

et al. 1985

Cancer

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“…presence of N-acetyl neuraminic acid (NANA) attached to a protein backbone [2,3], While some investigators presented evidence that specificity of M and N antigens is determined by carbohydrate structures [4,5] and also glycolipids [6], it now appears that both carbohydrate and amino acid residues also involved in formation of M and N determinants [7][8][9][10][11], One group of investigators found no difference in the sialic acid content of M and N RBC [12], which argues against the thesis that the carbohy drates are entirely responsible for M and N activities, while another group [13] found that there was a signifi cant difference in the sialic acid content and that M RBC glycopeptides have more components than N RBC glycopeptides. Significantly, treatment with neuraminidase [14,15] which removes NANA from the surface of RBC or chemial modification of amino groups [ 16] which may also damage carbohydrates, destroy M and N blood group activity.…”

Section: Introductionmentioning

confidence: 99%

Reactions of Murine Monoclonal Antibodies to Blood Group MN Antigens

Rubocki¹,

Milgrom²

1986

Vox Sanguinis

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BALB/c mice were immunized by intraperitoneal injections with human blood group substances; 4 mice with M and 4 with N. Immune spleen cells were fused with murine myeloma cells X63-Ag-8.653. Two clones secreting monoclonal anti-M and seven secreting monoclonal anti-N were identified. All antibodies were of IgG(1) subclass and had κ light chains. Three clones have been maintained that produced antibodies useful for typing purposes: anti-M, A09 originating from a mouse injected with M, anti-N, AH7 originating from a mouse injected with N, and anti-N BO10 originated from a mouse injected with M substance. In typing 370 erythrocyte samples, monoclonal reagents gave identical results with commercial anti-M or anti-N typing sera of rabbit origin. Significantly, anti-N reagent AH7 obtained by immunization with N substance showed serological differences from anti-N reagent BO10 obtained by immunization with M substance in that AH 7 had apparently higher avidity to N specificity on glycophorin A of N erythrocytes than BO10, whereas BO10 showed higher avidity for ‘N’ specificity on glycophorin B of M and N erythrocytes than AH7. These two reagents showed also somewhat different patterns of reaction with enzymatically digested erythrocytes. This apparent serologic difference between N and ‘N’ specificities is at variance with current immunochemical data.

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A study of gastrointestinal cancer‐associated antigen (GICA) in human fetal organs

Raux

Labbé

Fondanèche

et al. 1983

Intl Journal of Cancer

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The gastrointestinal cancer-associated antigen (GICA) characterized by 1116 NS 19-9 monoclonal antibody was studied in human fetal organs by immunohistology and immunofixation on nitrocellulose sheets. It was found in all the gastrointestinal tracts of fetuses and newborns. Other fetal organs, except biliary and pancreatic ducts, were negative. Immunohistological data and enzymatic studies led us to conclude that GICA is predominantly a mucin-type glycoprotein in fetal organs.

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Human blood groups M-, N-, T-, and Tn-specific substances in lipidic extracts of line 10 hepatocarcinoma of Strain 2 guinea pigs

Cited by 14 publications

References 27 publications

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

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

Reactions of Murine Monoclonal Antibodies to Blood Group MN Antigens

A study of gastrointestinal cancer‐associated antigen (GICA) in human fetal organs

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