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Biomedical subjects

G F Springer

Publications and source records attributed to G F Springer.

At least 55 records · Page 3Linked to original sources
PubMed1983

Delayed-type cutaneous hypersensitivity to Thomsen-Friedenreich (T) antigen in patients with pancreatic cancer.

The delayed-type hypersensitivity skin reaction to human erythrocyte-derived Thomsen-Friedenreich (T) antigen was studied in 40 patients with pancreatic disease and in 158 control subjects and its sensitivity and specificity were compared with the carcinoembryonic antigen (CEA) blood levels. The skin reaction to T was positive in 22 of 25 patients with biopsy-proven adenocarcinoma of the pancreas (sensitivity, 88%). In these patients, the CEA levels were elevated above 3.5 ng/ml in 12 of 23 (52%). The skin test to T antigen was negative in 11 of 12 patients with chronic pancreatitis (specificity, 92%), but CEA levels were normal in only five of nine with pancreatitis (56%). Two of the patients with pancreatic carcinoma and one of those with pancreatitis were anergic to mumps and dermatophytin antigens and had thus an invalid skin test. The positive response rate to T antigen was significantly greater (P less than 0.005) in the cancer group than the group with pancreatitis; the CEA response was not significantly different. There were no positive responses to T in 82 healthy volunteers. Among 76 patients with chronic disease including six with malignant tumors of the mesoderm and central nervous system, there were four positive responses: two in heavy smokers and two in patients with chronic lung infection. The specificity of the test overall in 158 controls was thus 97.5%.

Adenocarcinoma↗
PubMed1983

Mechanisms for the removal of senescent human erythrocytes from circulation: specificity of the membrane-bound immunoglobulin G.

Direct antiglobulin (Coombs') tests of erythrocyte (RBC) subpopulations confirmed the presence of membrane-bound immunoglobulin G (IgG) on old (density greater than 1.110) human RBCs but not on the young (density less than 1.110) RBCs. After thermal elution of the bound IgG, this Coombs' reaction was negative, but incubation of thermally eluted IgG (He-IgG) with heat-treated RBCs induced a positive antiglobulin test. A positive direct antiglobulin reaction was also obtained after incubation of heat-treated RBCs with anti-T antibody. Similar results were obtained when young RBCs treated with Vibrio cholerae neuraminidase (VCN) were incubated with anti-T or with IgG eluted by heat from old RBCs. Nevertheless, pre-absorption of heat-eluted IgG with T and/or Tn antigen, did not prevent it from binding to either heat-treated old or VCN-treated young RBCs as assessed by the antiglobulin consumption assay. Pre-treatment of either VCN-treated young or heat-treated old RBCs with anti-T and/or anti-Tn antibodies had no significant effect on the binding of radiolabeled He-IgG (eluted from old RBCs). The results indicate that even though desialylation of the erythrocyte membrane is required for binding of both anti-T-Tn and He-IgG, the specificity and consequently the RBC binding sites for He-IgG and anti-T seem to be different.

Antigens, Tumor-Associated, Carbohydrate↗
PubMed1983

Phenotypic and genotypic differences between high- and low-metastatic related tumor lines and the problem of tumor progression and variant generation.

We have described a number of phenotypic and genotypic differences between defined tumor sublines from the Eb/ESb model system that differ greatly in metastatic capacity. Some of these differences are summarized in Figure 5. It can be seen that the differences are both structural and functional. They include differences in the glycosylation of membrane glycoproteins as well as differences in total membrane protein composition. The functional differences refer particularly to enzymatic activities, cell motility, and invasive capacity. In addition, a change in membrane fluidity and membrane dynamics was seen when we investigated membrane vesicles shed spontaneously from these tumor lines. ESb type cells were found to shed about three times as much membrane material as the low-metastatic, Eb cells. Since such vesicles carried degradative enzyme activity, they could play a role in the invasion process. The vesicles also carried TATA and thus could also play a role in preventing immunological attack against these tumor cells. Another immunological escape mechanism was found to be based on the ability of the high-metastatic cells to generate immunoresistant variants that no longer expressed the respective TATA. A cytogenetic comparison of such immunoresistant variants with the TATA+ line revealed several chromosomal changes. The contribution of chromosomal rearrangements to the ability of malignant cells to generate variants was discussed.

Animals↗
PubMed1982

Extent of desialation of blood group MM, NN, and MN antigens required for reactivity with human anti-T antibody and Arachis hypogaea lectin.

Immunochemical activity of the Arachis hypogaea lectin has been equated, in spite of its different hapten combining requirements, with that of the human anti-T (Thomsen-Friedenreich) antibody population which is of importance in cancer immunology. We show here by gradual desialation of isolated human blood group MM and NN antigens at pH 2.0, 56 degrees C, that A. hypogaea lectin is, in addition, substantially more tolerant to NeuAc in the vicinity of T antigen's immunodominant repeating structures, Gal beta 1 leads to 3 GalNAc, than human anti-T antibodies. Reactivity with the Arachis lectin appeared first at 20-25% release of NeuAc from the antigens, whereas faint reactivity with anti-T was first recognizable at 50-55% NeuAc release from NN and 65-70% from MM antigen. Remarkably, at these degrees of desialation, the NN and MM antigens had about 50% of maximal activity toward the Arachis lectin. The slower appearance of T antigen upon graded desialation of MM antigen is likely due to the higher concentration of NeuAc and difference in some of its linkages on intact MM as compared to NN antigen.

Antibodies↗
PubMed1982

Patients' immune response to breast and lung carcinoma-associated Thomsen-Friedenreich (T) specificity.

We report here sensitive and specific measurement of immune responses of patients with certain kinds of carcinoma toward the physically and chemically well defined T antigen isolated from healthy human erythrocytes. Over 90% of adenocarcinoma tissues tested possess T-specific immunoreactive structures as determined with human antisera, in contrast to healthy tissues and benign lesions. Adenocarcinoma patients recognize the carcinoma-associated T antigen as foreign. Delayed-type skin hypersensitivity reaction to T antigen (DTHR-T) was positive in all 25 lung adenocarcinoma patients tested, in 88% of 101 patients with ductal, in 43% of 30 patients with lobular or tubular breast carcinoma and in 9/9 patients with adenocarcinoma of body cavities. Patients of all Stages reacted positively. All 7 patients with small cell lung carcinoma and 3/5 with malignant melanoma had a positive DTHR-T. None of 17 patients with malignant brain tumors, leukemia or Hodgkin's disease, sarcoma or thyroid carcinoma reacted. The DTHR-T was specific in that all 77 healthy persons and 48/49 with other diseases, including 23/24 with non-cancer lung disease were negative; one patient with organizing interstitial pneumonitis was positive. This points to a possible source of false positive reactions. 91% of 149 patients with histologically benign breast disease had a negative DTHR-T; the histology of some of the positive ones was reexamined, 2 proved to have carcinoma in situ.

Adenocarcinoma↗
PubMed1981

Origin of anti-Thomsen-Friedenreich (T) and Tn agglutinins in man and in White Leghorn chicks.

Interest in anti-Thomsen-Friedenreich (T) antibodies has increased because of their significance in detection of and their possible interaction with human adenocarcinoma. The origin of anti-T, which all humans possess, has not been ascertained. We determined here that anti-T and -Tn agglutinins could readily be induced via the physiological intestinal route by an enteric bacterium, E. coli O86, which possesses T and Tn activities. One dose of live E. coli O86 given in the drinking water to germfree chicks, who had no anti-T and -Tn antibodies, resulted, in all birds, in formation of saline agglutinating anti-T and -Tn antibodies as well as those detectable only by indirect agglutination. Antibody specificity was confirmed by adsorption on and elution from homologous human erythrocytes and for anti-T also by haemagglutination inhibition. In contrast, control chicks raised under ordinary conditions did have anti-T and -Tn prior to feeding E. coli O86. In humans, six diarrhoeic and five healthy infants and the majority of 13 adults investigated were fed killed rather than live E. coli O86. All infants, but one, suffering from diarrhoea showed a significant increase (greater than or equal to 4-fold) in anti-T and/or anti-Tn antibodies; in some, these antibodies were elicited de novo. All four adults with intestinal lesions had a significant increase of anti-T and/or -Tn subsequent to ingestion of E. coli O86, as did five of nine healthy adults, but to a lesser extent. These findings support the immune nature of demonstrable levels of anti-T and -Tn.

Adult↗
PubMed1981

Further evidence that carbohydrates are the immunodeterminant structures of blood group M and N specificities.

Terminal beta-D-galactopyranosyl (Gal) groups are implied in blood group N but not M specificity by the following findings: (a) Rabbit anti-asialoganglioside sera specific for terminal beta-Gal-(1 leads to 3)-GalNac agglutinate human group 0 M and N erythrocytes, the latter to a significantly higher titer, while rabbit anti-ganglioside GMl sera, whereas sialic acid modifies the antibody specificity, do not. The agglutination score with N erythrocytes was about twice that with M red blood cells. The asialoganglioside antibodies were readily absorbed by group 0 N erythrocytes, which were up to 10 times more efficient than group 0 M erythrocytes. Erythrocyte agglutination by the anti-asialoganglioside sera was inhibited by M and N antigen preparations isolated from group 0 red cells ghosts. N antigen was a better inhibitor. Asialoganglioside effectively inhibited the red cell agglutinations by anti-asialoganglioside serum. Ganglioside GMl did not inhibit. (b) Horse anti-pneumococcus Type XIV serum, which has anti-beta-Gal specificity, precipitated highly active N but not M substances. This precipitation was specifically inhibitable by oligosaccharides with terminal beta-Gal. (c) Beta galactosidase specifically inactivated native N and "acid-produced' N substances with the release of about three moles Gal per subunit of N antigen. It did not affect M antigen.

Absorption↗
PubMed1980

Breast cancer patient's cell-mediated immune response to Thomsen-Friedenreich (T) antigen.

Thomsen-Friedenreich (T) antigenic specificity as determined with human serum anti-T was found in reactive form in breast adenocarcinomata but not in healthy and generally not in benign breast tissues. T-antigenic specificity was demonstrable in all metastatic breast carcinoma lesions. T specificity was also present in adeno- and squamous cell carcinomata from other organs; it was not found in the four melanomata, one glioblastoma, and seven benign non-breast tumors. Breast carcinoma patients but not healthy people showed cellular immunity to T antigen in vivo and in vitro. Most striking was the delayed-type cutaneous hypersensitivity reaction that was positive in over 85% of the ductal breast carcinoma patients tested, negative in over 94% benign breast disease patients, and in all presumably healthy individuals investigated. T antigen is readily available from healthy red blood cells in uncontaminated form, and free of HL-A and Australia antigens.

Adenocarcinoma↗