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Surface membrane glycoproteins of cultured human pancreatic cancer cells
Author(s) -
Kim Young S.,
Tsao Dean,
Hicks James,
McIntyre Laurence J.
Publication year - 1981
Publication title -
cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.052
H-Index - 304
eISSN - 1097-0142
pISSN - 0008-543X
DOI - 10.1002/1097-0142(19810315)47:6+<1590::aid-cncr2820471422>3.0.co;2-l
Subject(s) - lactoperoxidase , galactose oxidase , glycoprotein , antiserum , microbiology and biotechnology , gel electrophoresis , membrane glycoproteins , biochemistry , concanavalin a , cell , cell culture , lectin , chemistry , affinity chromatography , cell membrane , polyacrylamide gel electrophoresis , antigen , sepharose , biology , enzyme , peroxidase , immunology , in vitro , genetics
The cell‐surface glycoproteins and proteins of four human pancreatic cell lines (MIA PaCa‐2, PANC‐1, HS766T, and CAPAN‐1) were separately tritiated using galactose oxidase/NaB( 3 H) 4 and iodinated using lactoperoxidase/ 12 I. Gel electrophoresis showed that the cell lines had very different surface components. All four cell lines were tested for cell‐surface antigens that cross‐reacted with antisera raised against carcinoembryonic antigen and against the membrane fractions of MIA PaCa‐2 and CAPAN‐1 cells. CAPAN‐1 cells reacted most strongly with all three antisera. Seventeen cell‐surface proteins can be detected when CAPAN‐1 cells are labeled using lactoperoxidase. The labeled membranes were solubilized in detergent and subjected to affinity chromatography on Sepharose‐conjugated lectins. The bound proteins were eluted and analyzed on gel electrophoresis. All 17 proteins capable of being labeled by lactoperoxidase bound to at least one lectin column, indicating they are all glycoproteins.