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G F Springer

Publications and source records attributed to G F Springer.

At least 73 records · Page 4Linked to original sources
PubMed1980

Sialylation of Thomsen-Friedenreich (T) and blood type NM antigens by transferases in human sera measured by [14C]NAN uptake.

Human erythrocyte T & NN antigens were exposed to fresh sera from single human donors and CMP-[14C]sialic acid without activators in a single 24 hr incubation at 37 degrees C. There was similar sialic acid (NAN) uptake, on the average 2.7 mol/mol T antigen subunit (mol wt 40,000), with various NN- and MM-derived T antigens and transferase sera in all different combinations. Sera from donors with the M gene but not from those lacking it incorporated NAN into NN antigen (c. 1 mol NAN/mol NN antigen subunit, mol wt 50,000). The profound difference in sialyltransferase action between sera from donors with the M gene and those lacking it was substantiated by repeated incubations of NN-derived T antigen with CMP-NAN and MM donor transferase serum, which incorporated 32% more NAN than did repeated incubations of the same antigen with CMP-NAN and NN donor transferase serum. The greater NAN incorporation by sera of donors with the M gene is due to an additional transferase-modifier substance present only in persons possessing the M gene.

Blood Group Antigens↗
PubMed1979

Delayed-type skin hypersensitivity reaction (DTH) to Thomsen-Friedenreich (T) antigen as diagnostic test for human breast adenocarcinoma.

One intradermal (i.d.) injection of human erythrocyte T antigen in the upper outer arm contralateral to any breast lesion elicits a delayed tuberculin-type hypersensitivity reaction (DTH) in breast carcinoma patients. It is necessary to inject simultaneously but separately the same quantity of MN antigen (about 6--8 cm apart), from which the T Antigen has been prepared, since particularly patients with Stage I breast carcinoma (Internatl. nomenclature) and those with benign breast disease may significantly react to it. The extent of reaction to MN antigen must be subtracted from the reaction to T antigen before interpreting results. DTH response to T antigen was 85% accurate among 67 patients with ductal breast carcinoma of all Stages (including non-invasive), 95% accurate (5% so far falsely positive) among 95 patients with benign breast disease and it was 100% accurate (no false positives) among 36 "healthy" persons tested. Among 18 patients with the comparatively rare and less ominous lobular and tubular breast carcinomata, the DTH reaction was positive in 8 of 16 (50%) patients with lobular, and in none of 2 patients with tubular breast carcinoma.

Adolescent↗
PubMed1979

Human carcinoma-associated precursor antigens of the NM blood group system.

Blood group NM specificities occur in healthy, benign and carcinomatous breast glands and those of the gastrointestinal (G.I.) tract, but the precursors in their biosynthesis, T (Thomsen-Friedenreich) and Tn, are found in adenocarcinomata and not in benign or healthy tissues. T- and Tn-antigenic specificities are thus human carcinoma-associated. All humans possess anti-T and anti-Tn antibodies. Patients with breast or G.I. tract carcinoma show statistically significant alteration of anti-T titer levels when compared to patients with benign disease and to healthy controls. Breast carcinoma patients but not healthy people showed cellular immunity to T antigen in vitro and in vivo. Most striking was the delayed-type hypersensitivity reaction, which was positive in over 90% of ductal breast carcinoma patients tested and negative in all presumably healthy individuals. T antigen is readily prepared from healthy human red blood cells in uncontaminated form, and free of HL-A and Au antigens. T antigen and anti-T antibodies may be useful in combating some human adenocarcinomata.

Adenocarcinoma↗
PubMed1979

Biosynthesis of human blood group T-, N- and M-specific immunodeterminants on human erythrocyte antigens.

We synthesized on Tn erythrocytes with human sera, UDP-Gal, and activators T-specific haptenic structures in satisfactory yield. The specificity of this biosynthesis was ascertained by agglutination with human and animal anti-T, by specific absorption of human anti-T as well as by agglutination inhibition assays. With isolated human erythrocyte T antigen as substrate we synthesized N- and M-specific structures with sera from individual human donors in presence of CMP-sialic acid by incubation for 24 hr at 37 degrees C. Serology on the recovered product was carried out with nineteen monospecific human and animal sera under strictly standardized and controlled conditions with the mandatory tube assay. All M- as well as N-derived T antigens tested acquired N specificity with all transferase sera of all MN types. In contrast, M-activation of M- and N-drived T antigens tested acquired N specificity with all transferase sera of all MN types. In contrast, M-activation of M- and N-derived T antigens occurred only if the transferase donor had the M gene. The nine M transferase sera used all gave M-activation of MM- and NN-derived T antigens. None of twelve transferase sera from NN donors M-activated any T antigen. NN antigen was transformed to a M-specific one by all transferase sera from MM donors but by none from NN donors. We have not yet established the biochemical-genetic relation of M to N; N may be the immediate precursor of M or M may originate directly from T. The sialyltransferase responsible for M activation may be a N transferase 'modified' by the M gene product or an entirely different sialyltransferase.

ABO Blood-Group System↗
PubMed1978

Effect of periodate oxidation on specific activities and carbohydrate components of human blood group N- and M-specific glycoproteins and glycopeptides.

Mild as well as strong periodate oxidation of isolated erythrocyte N and M glycoproteins and glycopeptides gave extensive to complete destruction of N-specificities as measured with Vicia graminea extracts and of N- as well as M- activities determined with all but 1 of 8 animal anti-N and 13 anti-M sera. Results with human antisera differed somewhat, while the specificity of mildly oxidized N-glycoprotein was completely destroyed as determined with all 8 human anti-N sera used, that of strongly oxidized N-active substance was completely inactivated towards one of the human antisera; the remainder showed 63--94% destruction, and 2 sera indicated no effect of oxidation. Similarly, while 10 of 14 human anti-M indicated complete inactivation of M-specific glycoproteins and glycopeptides after mild or strong oxidation, 2 showed partial inactivation and 2 human anti-M sera showed no inactivating effect of oxidation. The most relevant findings of quantitative carbohydrate analysis of periodate oxidized N- and M-specific substance were extensive transformation of N-acetylneuraminic acid (NAN) to its C8 and C1 analogues on mild oxidation and pronounced destruction of NAN and its analogues on strong oxidation; however, some intact NAN always remained. In all instances galactose (Gal) was destroyed to a much larger extent in N-derived than in M-derived glycoproteins and glycopeptides.

Amino Acids↗
PubMed1976

Blood group MN precursors as human breast carcinoma-associated antigens and "naturally" occurring human cytotoxins against them.

Blood groups MN active substances were found in benign and malignant human mammary glands. However, the precursor T (Thomsen-Friedenreich) antigen, as determined with human sera, occurred in all cancerous breast tissues tested but not in the benign mammary glands. Anti-T antibody, which is present in all human sera, was severely depressed in 21.16% of 189 breast carcinoma patients, compared with 3.62% of 470 persons of similar age without cancer. Of 720 persons tested approximately 85% of those with severely depressed anti-T had carcinoma; their IgG, IgM and IgA concentrations were of normal range. A greater than 25%-90% increase in anti-T titer score was found in 65.6% of 32 patients bled 1-14 months after mastectomy for carcinoma as compared with 3.1% of 32 patients with breast biopsy who had no carcinoma. All differences in anti-T titer score changes reported are statistically highly significant. Injection of T antigen from human erythrocytes increased anti-T titer scores.

Adolescent↗