The cell surface has been one of the focal points in the studies on malignancy. General changes in structures of cell surface glycoconjugates as well as the presence of unique glycoconjugates in malignant cell surface have been reported. The long-range objective of this study is to contribute to the structure-function relationships of cancer cell surface glycoproteins and malignancy. The emphasis will be on the high molecular weight cell surface sialoglycoproteins (termed Ca antigen) which are detectable by Cal monoclonal antibody on a wide variety of human malignant cells. The primary objective is to carry out full biochemical characterization of the Ca antigen. Cal monoclonal antibody will be employed as affinity ligand for the isolation of the Ca antigen from human laryngeal carcinoma cells. The 390K and 350K species of the Ca antigen will be purified and their detailed chemical structure elucidated. The carbohydrate and protein composition, oligosaccharide type and location, and subunit structure are some of the aspects which will be studied. The counterpart of Ca antigen from human melanoma cells and the Ca antigen-like glycoproteins present in normal human urine will also be purified. The structural and immunological relationships of these materials and Ca antigen will be established. Polyclonal and monoclonal antibodies to the purified Ca antigen glycoproteins will be produced and used for understanding the above relationship. It is hoped that the information obtained in these studies will help to establish the potential use of Ca antigen as a human tumor marker. This glycoprotein antigen could be of use for the early diagnosis of cancer, for monitoring the course of disease, for localizing tumors, and for directing drugs to the tumor. (1)

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Research Project (R01)
Project #
5R01CA038797-06
Application #
3177107
Study Section
Pathobiochemistry Study Section (PBC)
Project Start
1984-12-01
Project End
1994-11-30
Budget Start
1991-12-01
Budget End
1992-11-30
Support Year
6
Fiscal Year
1992
Total Cost
Indirect Cost
Name
Pennsylvania State University
Department
Type
Schools of Medicine
DUNS #
129348186
City
Hershey
State
PA
Country
United States
Zip Code
17033
Bhavanandan, V P; Zhu, Q; Yamakami, K et al. (1998) Purification and characterization of the MUC1 mucin-type glycoprotein, epitectin, from human urine: structures of the major oligosaccharide alditols. Glycoconj J 15:37-49
Zhu, Q; Bhavanandan, V P (1995) Analysis of serine/threonine-linked oligosaccharides derived by alkaline-borohydride treatment of mucin glycoproteins electroblotted onto membranes: comparison of the saccharide profiles of the 390 kDa and 350 kDa forms of epitectin. Glycoconj J 12:639-44
DiIulio, N A; Bhavanandan, V P (1995) The saccharides of the MUC 1 mucin-type glycoprotein, epitectin, produced by H.Ep.2 cells in the presence of aryl-N-acetyl-alpha-galactosaminides. Glycobiology 5:195-9
Kelleher, F M; Bhavanandan, V P; Reinhold, V N (1994) The formation of a dimeric product of raffinose by the action of galactose oxidase. Int J Biochem 26:73-8
Hu, R H; Mellors, A; Bhavanandan, V P (1994) Cleavage of epitectin, a mucin-type sialoglycoprotein, from the surface of human laryngeal carcinoma cells by a glycoprotease from Pasteurella haemolytica. Arch Biochem Biophys 310:300-9
Bhavanandan, V P; Sheykhnazari, M (1993) Adaptation of the periodate-resorcinol method for determination of sialic acids to a microassay using microtiter plate reader. Anal Biochem 213:438-40
Devaraj, N; Devaraj, H; Bhavanandan, V P (1992) Purification of mucin glycoproteins by density gradient centrifugation in cesium trifluoroacetate. Anal Biochem 206:142-6
Bhavanandan, V P (1991) Cancer-associated mucins and mucin-type glycoproteins. Glycobiology 1:493-503
Bhavanandan, V P; Sheykhnazari, M; Devaraj, H (1990) Colorimetric determination of N-acetylhexosamine-terminating O-glycosidically linked saccharides in mucins and glycoproteins. Anal Biochem 188:142-8
Bardales, R M; Bhavanandan, V P (1989) Transglycosylation and transfer reaction activities of endo-alpha-N-acetyl-D-galactosaminidase from Diplococcus (Streptococcus) pneumoniae. J Biol Chem 264:19893-7

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