Identification of a 220-kDa Membrane Tumor-Associated Antigen by Human Anti-UK114 Monoclonal Antibodies Selected from the Immunoglobulin Repertoire of a Cancer Patient

A perchloric acid-soluble protein extracted from goat liver and designated as UK 114 is known to be expressed over the cell membrane of (some) human cancer cell lines. This protein is antigenic, and specific antibodies elicit complement-dependent cytolysis of neoplastic target cells. In this study we demonstrate that administration of UK 114, either pure or as a crude extract (designated UK 101), inhibits the growth of mammary carcinomas induced in female Sprague-Dawley rats by dimethylbenzanthracene (DMBA). The mechanism of the tumour inhibitory activity of UK 114 is probably related to induction of immunosurveillance.

Growth inhibition of DMBA-induced rat mammary carcinomas by UK 114

The immunopathology of herpes simplex virus (HSV)-associated neuroinflammation is a captivating and intricate field of study within the scientific community. HSV, renowned for its latent infection capability, gives rise to a spectrum of neurological expressions, ranging from mild symptoms to severe encephalitis. The enigmatic interplay between the virus and the host's immune responses profoundly shapes the outcome of these infections. This review delves into the multifaceted immune reactions triggered by HSV within neural tissues, intricately encompassing the interplay between innate and adaptive immunity. Furthermore, this analysis delves into the delicate equilibrium between immune defence and the potential for immunopathology-induced neural damage. It meticulously dissects the roles of diverse immune cells, cytokines, and chemokines, unravelling the intricacies of neuroinflammation modulation and its subsequent effects. By exploring HSV's immune manipulation and exploitation mechanisms, this review endeavours to unveil the enigmas surrounding the immunopathology of HSV-associated neuroinflammation. This comprehensive understanding enhances our grasp of viral pathogenesis and holds promise for pioneering therapeutic strategies designed to mitigate the neurological ramifications of HSV infections.

Immunopathology of herpes simplex virus-associated neuroinflammation: Unveiling the mysteries.

The finding of a nuclear antigen by anticomplement immunofluorescence in cells treated with cytosine-arabinoside after infection of Herpes Simplex Virus (HSV), opens a new approach to the problem of the role of this virus in certain human cancers. Complement-fixing tests of HSV markers with cancer and control human sera as well as with hyperimmune guinea pig antisera are discussed, suggesting another parameter for studies of squamous cell carcinomas. The finding of HSV antigens in selected tumors as the expression of repressed viral genome proves a continuing release of virus specific message and supports the important role of the virus in the development of the tumor.

Herpes simplex virus nuclear nonvirion antigens detected by anticomplement immunofluorescence.

This chapter describes a method to assay the activity of reactive intermediate deaminases (Rid), a large family of conserved soluble enzymes, which have been proposed to prevent damages from metabolic intermediates such as the highly reactive and unstable compounds enamines/imines. In this method, the flavin adenine dinucleotide-dependent L- or D-amino acid oxidases generate an imino acid starting from a L- or D- amino acid, respectively. This reaction is coupled to the hydrolysis of the imino acid to the corresponding α-keto acid and ammonium ion catalyzed by a Rid enzyme. The spectrophotometric assay consists of measuring the decrease of the initial rate of formation of the semicarbazone, derived from the spontaneous reaction of the imino acid and semicarbazide, caused by the presence of the Rid enzyme. The set-up and testing of this method imply a preliminary characterization of the ability of the amino acid oxidase to release the imino acid required for the subsequent reactions. To this purpose, the activity of the L- or D-amino acid oxidases with different amino acids can be measured as production of hydrogen peroxide or formation of semicarbazone in parallel assays. The advantages and limitations of this assay of Rid activity are discussed.

Using D- and L-Amino Acid Oxidases to Generate the Imino Acid Substrate to Measure the Activity of the Novel Rid (Enamine/Imine Deaminase) Class of Enzymes.

Purification and partial characterization of proteins present in a perchloric acid extract of goat liver (UK101)

Biochemical and radioimmunological studies have indicated the presence of a nonvirion antigen associated with herpes virus. Guinea pig kidney cells were grown in culture and infected (I-cells) for 3h with herpes virus. Uninfected cells (N-cells) served as control. The cells were collected and sonicated to obtain, after centrifugation, "soluble extract" (SI, SN). The pellets were extracted with KCl (ISP, NSP). SN, SI were submitted to gel-filtration on Sephadex G-200. Extracts from I and N cells gave similar patterns. After labelling with 125I, greater resolution was obtained in a second gel-filtration with a much smaller load. ISP contained protein species not present in NSP. Polyacrylamide gel electrophoresis of peaks from SN and SI showed that SI contained some radioactive bands not found in SN. Labelled materials from SI and SN were incubated with sera from cancer patients and normal subjects. No differences in binding were seen with SN, but SI showed 14-30% more 125I binding with sera of cancer patients than with sera from normal subjects. No such difference was seen between ISP and NSP.

Preliminary studies of nonvirion antigens associated with herpes simplex virus 1 and 2 (HSV1 - HSV2).

Enzyme-linked immunosorbent assays (ELISA) for the detection of antibodies to UK114 and UK150

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Purification and partial characterization of proteins present in a perchloric acid extract of goat liver (UK101)

Preliminary studies of nonvirion antigens associated with herpes simplex virus 1 and 2 (HSV1 - HSV2).

Enzyme-linked immunosorbent assays (ELISA) for the detection of antibodies to UK114 and UK150