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Biomedical subjects

D C Kilpatrick

Publications and source records attributed to D C Kilpatrick.

At least 37 records · Page 2Linked to original sources
PubMed1988

Accessory cell paradox: monocytes enhance or inhibit lectin-mediated human T-lymphocyte proliferation depending on the choice of mitogen.

Monocytes suppressed the mitogenic response of human T lymphocytes to the lectin from Datura stramonium but enhanced the mitogenic response of the same lymphocytes to wheat germ agglutinin under identical culture conditions. The inhibitory action was probably cell-mediated, but was not the result of cytotoxicity. The stimulative activity could be replaced by cell-free conditioned medium.

Humans↗
PubMed1987

Wheat germ agglutinin is mitogenic, nonmitogenic and anti-mitogenic for human lymphocytes.

Wheat germ agglutinin (WGA) was found to stimulate DNA synthesis in human peripheral blood mononuclear cells at relatively low concentrations and to inhibit DNA synthesis at higher concentrations. Both actions were inhibited by oligomers of N-acetyl-D-glucosamine. Significant mitogenic activity was dependent on the use of human (as opposed to fetal calf) serum to supplement the culture medium. Purified T cells responded to WGA very weakly and the incorporation of thymidine into non-T cells in response to WGA was less than the lectin-free control. The full ability of T cells to respond to WGA was restored by the addition of monocytes, but not by any other blood cells. Interleukin 2 partially restored the ability of T cells to respond to WGA; interleukin 1 was less effective. WGA displayed a strong synergistic action with the tumour promoter, 12-O-tetradecanoyl-13-acetate (TPA), in stimulating DNA synthesis in separated T (but not non-T) cell fractions, and in unfractioned mononuclear cells. These results reconcile most of the conflicting reports in the literature concerning the interaction of WGA with human lymphocytes.

Blood↗
PubMed1987

Haplotype frequencies in south-east Scotland.

One hundred and thirty-two families consisting of healthy babies born after normal pregnancies at an Edinburgh maternity unit and their parents were tissue-typed for HLA-A, B and DR antigens. The antigen frequencies and the commonest haplotype frequencies are reported.

Female↗
PubMed1987

Histocompatibility studies in pre-eclampsia.

Full HLA-A, B and DR types were obtained for 22 families (mothers, fathers and neonates) associated with severe (proteinuric) pre-eclampsia, 21 families associated with mild pre-eclampsia, and 132 families associated with normal pregnancies. There was an increased frequency of DR4 (relative risk 3.6: p less than 0.003, uncorrected) in both neonates and mothers of the severe pre-eclampsia families when compared to the normotensive controls. There were no significant differences between either pre-eclampsia group and controls in HLA antigen homozygosity, HLA antigen sharing or in lymphocytotoxin production.

Female↗
PubMed1987

Severe pre-eclampsia in multiparous women: indication of an environmental triggering agent?

Two case histories are described with conflicting implications for the etiopathogenesis of pre-eclampsia. In both, typical proteinuric pre-eclampsia developed despite a history of previous normotensive pregnancy. In the first case, the disease was associated with a change of husband, consistent with the view that pre-eclampsia arises from an inadequate maternal immune response to paternal antigens inherited by the fetus. The second case, however, concerned a woman who developed pre-eclampsia for the first time in her third pregnancy by the same reproductive partner. We conclude that either more than one underlying cause can result in the clinical syndrome of pre-eclampsia, or that pre-eclampsia is caused by an environmental factor. The possibility that pre-eclampsia may be initiated by an infectious agent is briefly explored in the light of the clinical histories described and well-established epidemiological, clinical and laboratory data.

Adult↗
PubMed1987

Feto-maternal HLA compatibility does not have a major influence on human pregnancy except for lymphocytotoxin production.

Several studies have supported the hypothesis that the maternal immune response to incompatible paternal HLA antigens present on the conceptus may influence pregnancy outcome. In order to relate feto-maternal histocompatibility directly to pregnancy course and characteristics, complete HLA-A, B and DR types were obtained from 132 healthy family groups consisting of mothers, fathers and neonates. The distribution of feto-maternal HLA compatibility was heavily skewed towards incompatibility, with 90% of fetuses being mismatched at 2 or 3 loci. There was no segregation distortion of paternal haplotypes, however, and the number of feto-maternal mismatches was close to that expected theoretically. More than 2% of the neonates were perfectly HLA-A, B and DR compatible with their mothers. The degree of feto-maternal HLA disparity showed no significant correlation with sex of neonate, birthweight, placental weight, maternal plasma alpha-fetoprotein or parity of the mother. Feto-maternal HLA disparity did, however, correlate significantly with maternal lymphocytotoxin production, even after allowance was made for parity (P less than 0.01). We conclude that feto-maternal HLA compatibility per se does not have a major influence on pregnancy outcome, and in particular is unlikely to predispose to spontaneous abortion; so an absence of antigen sharing between spouses experiencing recurrent spontaneous abortions should not be regarded in itself as a contraindication to offering immunotherapy to such couples.

Antilymphocyte Serum↗
PubMed1986

Inhibition of human lymphocyte transformation by tomato lectin.

The lectin from tomato (Lycopersicon esculentum) fruits was found to be non-mitogenic for human lymphocytes in culture and actually suppressed spontaneous DNA synthesis. It also inhibited the transformation of human peripheral blood lymphocytes induced by recall antigens or allogeneic cells in vitro. This inhibition was most effective when the lectin was present from the beginning of the culture period, and could be abolished by the simultaneous addition of oligomers of N-acetylglucosamine. The tomato lectin was able to bind to several major lymphocyte cell surface glycoproteins, but not to the major histocompatibility (HLA) antigens. The binding of tomato lectin to lymphocytes could be inhibited by wheat germ agglutinin (WGA), but not by concanavalin A. Tomato lectin could agglutinate monocytes and B lymphocytes as well as T lymphocytes. Human serum used to supplement the culture medium supporting lymphocyte transformation was equally effective after passage through a tomato lectin-Sepharose column. The inhibition of lymphocyte transformation brought about by tomato lectin was not stopped by exogenously added interleukin 1 and/or interleukin 2, even at very high concentrations.

Binding, Competitive↗
PubMed1985

Tomato lectin resists digestion in the mammalian alimentary canal and binds to intestinal villi without deleterious effects.

Experiments were designed to investigate whether orally consumed tomato lectin could resist the digestive process and function as a lectin within the alimentary canal. Rats fed on a tomato lectin-rich diet passed faeces containing serologically detectable tomato lectin, and the lectin could be shown by immunoperoxidase staining bound to intestinal villi. Moreover, radioactivity was mainly recovered from the alimentary canal 3h after 125I-labelled tomato lectin administration with only traces in the circulation or internal organs. Radioactivity absorbed into the human circulation after consumption of 125I-labelled tomato lectin was also less than that expected for a digestable protein.

Administration, Oral↗
PubMed1985

A diffusable factor in Scottish coagulation factor concentrates can inhibit lymphocyte transformation in vitro.

Coagulation factor VIII and IX concentrates produced in Scotland inhibited human lymphocyte transformation induced by lectins or the recall antigen, purified protein derivative of tuberculin (PPD). Although concanavalin A could bind factor VIII directly and PHA could bind factor IX directly, most of the inhibition was not due to direct clotting factor - lectin interaction nor to simple toxicity. Most of the inhibitory activity from both clotting factors could be removed by dialysis. A similar degree of inhibition was observed when the buffers used to prepare the concentrates were substituted for the concentrates themselves, and a comparable concentration of sodium citrate was also found to be inhibitory. Coagulation factor VIII partially purified by gel filtration was not found to have an appreciable effect on lymphocyte transformation in vitro.

Cells, Cultured↗