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C L Guikers

Publications and source records attributed to C L Guikers.

10 recordsLinked to original sources
PubMed1995

Cells with UV-specific DNA damage are present in murine lymph nodes after in vivo UV irradiation.

Ultraviolet radiation is absorbed in the skin, especially in the epidermis. After ultraviolet irradiation the number of major histocompatibility complex class II+, adenosine triphosphatase+ Langerhans cells and Thy-1+ dendritic epidermal cells in the epidermis decreases. Whether this decrease is due to migration of these cells or to loss of membrane markers is not clear. To address this question we have used the monoclonal antibody H3 directed against cyclobutyl thymine dimers-a form of DNA damage that is specifically induced by ultraviolet radiation-to investigate whether H3+ cells are present in the draining lymph nodes of the skin after ultraviolet irradiation of hairless, inbred mice (HRA/Skh). After a single dose of ultraviolet radiation (Westinghouse FS40, 1.5 kJ/m2), H3+ cells were present in the paracortex of the draining lymph nodes. No positive cells were found in the blood of irradiated mice. These results suggest that the H3+ cells in the lymph nodes originate from the skin. The number of H3+ cells in the draining lymph nodes increased the first 24 h after irradiation and then stabilized. Immunohistochemical double staining revealed that all H3+ cells were major histocompatibility complex II+, and that only a fraction of the cells were NLDC-145 positive. No V gamma 3 T-cell receptor bearing cells could be found in the lymph nodes after UV irradiation of the skin.

Animals↗
PubMed1986

Antibodies against hen's egg proteins in pigeon breeder's disease.

The serum of patients with pigeon breeder's lung (PBL) contains IgG-class antibodies against pigeon serum proteins. These antibodies cross-react strongly with the sera of other avian species. Cross-reactivity, as demonstrated by precipitation, complement fixation, haemagglutination and microELISA, is also exhibited with the water-soluble proteins in hen's egg yolk and egg white. The phenomenon appears to be due to the presence of hen serum proteins in the eggs, which occur particularly concentrated among the water-soluble proteins in the yolk ('livetins'). It is proposed that anti-egg antibodies may explain the frequent serological finding of 'false-positive' asymptomatic pigeon breeders.

Alveolitis, Extrinsic Allergic↗
PubMed1979

Possible indirect binding of IgE in house dust RAST.

House dust subfractions obtained in the course of purification exhibit increasing skin reactivity in allergic patients, which runs parrallel to both complement-consuming and RAST-binding capacity. Working with highly purified house dust allergen in RAST, the correlation with clinical parameters for house dust allergy was found to remain poor. In a large group of sera a significant statistical correlation was found between total IgE and allergen-binding IgE. Ultracentrifugation experiments demonstrated that IgE binding to allergen in RAST occurs in complex with an unidentified serum protein. These results suggests that IgE binding in house dust RAST is indirect and is mediated by another serum factor.

Allergens↗
PubMed1975

Blood group activity of allergenic preparations.

Haemagglutination-inhibition studies showed that several different allergenic preparations exhibit A and B blood group activity. Most products displayed A-specificity, less often B-specificity; the inhibition titers were usually low. No correlation was evident between isoagglutination-inhibition titers and the complement-consuming capacity or skin-reactivity of the allergens. Absorption of A- and B-isoagglutinins from human serum did not affect the complement consumption by house dust allergens. Hapten-inhibition studies confirmed the non-participation of blood group antibodies in allergen-induced complement consumption. The observed inhibition by D-glucosamine is attributed to a partial structural homology with the lysine-sugar site on house dust allergens.

ABO Blood-Group System↗
PubMed1975

Value of fluid phase complement consumption as a means of 'in vitro' allergen standardization.

Atopic allergens can readily be shown to inactivate hemolytic complement in human serum. This property has been explored as a means of in vitro allergen quantitation and standardization. The purification of house dust allergen, guided by skin tests and complement inactivation, demonstrates that the in vitro technique is clinically relevant. Since human sera differ in their sensitivity to complement inactivation by allergens, it is desirable to prepare a purified house dust allergen as a standard. By referring to this standard, other house dust extracts may then be standardized by using any given serum sample of human origin, provided that such extracts have undergone some degree of purification. Kinetic studies demonstrate that other allergens of the house dust group may be standardized in similar fashion; it was noted that the ratio of the complement inactivating powers of these respective allergens remains constant whatever the serum used. The method is not suited for the quantitation of pollen allergens.

Allergens↗