Monoclonal Antibody to a Highly Glycosylated Protein Reacts in Fixed Tissue With Melanoma and Other Tumors
- 1 January 1985
- journal article
- research article
- Published by Mary Ann Liebert Inc in Hybridoma
- Vol. 4 (3) , 243-255
- https://doi.org/10.1089/hyb.1985.4.243
Abstract
A highly glycosylated protein with a molecular weight of 30,000 to 60,000 and a protein core of 20,000 daltons has been identified by antimelanoma monoclonal antibodies. The antigenicity of this melanoma-associated glycoprotein (MAG) was not destroyed in fixed paraffin-embedded melanoma tissue, and was present in malignant cells of cutaneous superficial spreading melanomas in skin (31/33) and in half of all metastatic melanomas examined (5/10). The antigen was not expressed by normal melanocytes. The strong reactivity of dysplastic nevi with the anti-MAG antibodies was comparable to that seen in radial growth phase melanoma. Antigen expression was much weaker in compound nevi where reactivity ranged from moderate in the junctional component and the upper dermis to absent at the base of the nevus.This publication has 18 references indexed in Scilit:
- Biochemical characterization and cellular localization of a formalin‐resistant melanoma‐associated antigen reacting with monoclonal antibody NKI/C‐3International Journal of Cancer, 1985
- Cytogenetics of human malignant melanoma and premalignant lesionsCancer Genetics and Cytogenetics, 1984
- Use of NK1 C3 monoclonal antibody in the assessment of benign and malignant melanocytic lesions.Journal of Clinical Pathology, 1984
- Detection of S-100 protein as an aid to the identification of melanocytic tumorsInternational Journal of Cancer, 1982
- Identification and Isolation of Melanoma-Associated Antigens with Monoclonal AntibodiesHybridoma, 1982
- Comparative Study of the Binding Characteristics of Monoclonal Antimelanoma AntibodiesHybridoma, 1982
- The Sequential Analysis of Cancer DevelopmentAdvances in Cancer Research, 1980
- Tunicamycin inhibition of polyisoprenyl N-acetylglucosaminyl pyrophosphate formation in calf-liver microsomesBiochemical and Biophysical Research Communications, 1975
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONSAnnals of the New York Academy of Sciences, 1949