Immunological Approach to the Identification and Development of Vaccines to Various Toxins

Experimental Amyloidosis Induced by Immune Complex

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100066978 ◽

1971 ◽

Vol 29 ◽

pp. 582-583

Author(s):

A. Kawaoi

Keyword(s):

Immune Complex ◽

Systemic Amyloidosis ◽

Human Diseases ◽

Experimental Amyloidosis ◽

Freund’S Complete Adjuvant ◽

Freund's Complete Adjuvant ◽

Immunological Approach ◽

Experimentally Induced

Numbers of immunological approach have been made to the amyloidosis through the variety of predisposing human diseases and the experimentally induced animals by the greater number of agents. The results suggest an important role of impaired immunity involving both humoral and cell-mediated aspects.Recently the author has succeeded in producing amyloidosis in the rabbits and mice by the injections of immune complex of heat denatured DNA.The aim of this report is to demonstrate the details of the ultrastructure of the amyloidosis induced by heterologous insoluble immune complex. Eleven of twelve mice, dd strain, subcutaneously injected twice a week with Freund's complete adjuvant and four of seven animals intraperitonially injected developed systemic amyloidosis two months later from the initial injections. The spleens were electron microscopically observed.

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Preparation of antiserum against a tryptic fragment (fragment A) of dynein and an immunological approach to the subunit composition of dynein

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)41089-2 ◽

1975 ◽

Vol 250 (16) ◽

pp. 6476-6483

Author(s):

K Ogawa ◽

H Mori

Keyword(s):

Subunit Composition ◽

Tryptic Fragment ◽

Immunological Approach ◽

Preparation Of Antiserum

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Development and characterization of a novel mAb against bilitranslocase - a new biomarker of renal carcinoma

Radiology and Oncology ◽

10.2478/raon-2013-0026 ◽

2013 ◽

Vol 47 (2) ◽

pp. 128-137 ◽

Cited By ~ 8

Author(s):

Sendi Montanic ◽

Michela Terdoslavich ◽

Uros Rajcevic ◽

Luigina De Leo ◽

Serena Department of Medical Sciences, Uni ◽

...

Keyword(s):

Renal Cell Carcinoma ◽

Monoclonal Antibodies ◽

Cell Carcinoma ◽

Renal Cell ◽

Renal Carcinoma ◽

Vascular Endothelial Cells ◽

Polyclonal Antibodies ◽

Functional Characterization ◽

Immunological Approach

Background. Bilitranslocase (TC 2.A.65.1.1) is a bilirubin-specific membrane transporter, found on absorptive (stomach and intestine) and excretory (kidney and liver) epithelia and in vascular endothelium. Polyclonal antibodies have been raised in rabbits in the past, using a synthetic peptide corresponding to AA65-77 of rat liver bilitranslocase, as an antigen. Affinity-purified antibodies from immune sera have been found to inhibit various membrane transport functions, including the bilirubin uptake into human hepatocytes and the uptake of some flavonoids into human vascular endothelial cells. It was described by means of immunohistochemistry using polyclonal antibodies that bilitranslocase expression is severely down-regulated in clear cell renal carcinoma. The aim of our work was development and characterization of high-affinity, specific mAbs against bilitranslocase, which can be used as a potential diagnostic tool in renal cell carcinoma as well as in a wide variety of biological assays on different human tissues. Materials and methods. Mice were immunized with a multi-antigen peptide corresponding to segment 65-75 of predicted primary structure of the bilitranslocase protein. By a sequence of cloning, immune- and functional tests, we aimed at obtaining a specific monoclonal antibody which recognizes a 37 kDa membrane protein, and influences the transport activity of bilitranslocase. Results. On the basis of previous results, specific IgM monoclonal antibodies were produced in BALB/c mice, in order to further improve and extend the immunological approach to the study of bilitranslocase in renal cancer cells as well as to develop its potential diagnostics use. Conclusions. In this article we show an immunological approach, based on newly developed monoclonal antibodies, to a detailed biochemical and functional characterization of a protein whose gene and protein structure is still unknown. We were able to demonstrate our novel mAb as a tumor marker candidate of renal cell carcinoma, which may prove useful in the diagnostic procedures.

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