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Characterization of the surface proteins of SV40‐transformed mouse and human cells: Absence of SV40‐specific proteins
Author(s) -
Rose Timothy M.,
Weil Roger
Publication year - 1983
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910310517
Subject(s) - antiserum , microbiology and biotechnology , antigen , biology , cell culture , immunoprecipitation , membrane protein , immunofluorescence , methionine , antibody , biochemistry , amino acid , membrane , immunology , genetics
The proteins of a number of SV40‐ and spontaneously transformed mouse and human cell lines were compared in an effort to identify a surface protein which would correspond to the SV40 tumor‐specific transplantation antigen (TSTA). Analysis of the one‐ and two‐dimensional electrophoretic patterns of 35 S‐methionine‐labelled total proteins and 125 I‐labelled surface proteins of several of these cell lines failed to reveal the presence of proteins specific to transformation by SV40. Antisera were prepared against SV40‐ and spontaneously transformed mouse cells in syngeneic mice. In serological assays, these antisera reacted with surface antigens common to both SV40‐ and spontaneously transformed mouse cell lines. Electrophoretic analysis of the 125 I‐surface‐labelled proteins which these antisera immunoprecipitated from extracts of SV40‐ and spontaneously transformed mouse and human cells identified a set of common surface proteins with apparent molecular weights of 15, 44, 50, 72, 77, 105, 150 and 230 kdal. No SV40‐specific surface proteins were detected. Two of the transformed cell surface proteins (105 and 150kdal) were present as well in membrane fractions of 35 S‐methionine‐labelled primary mouse kidney cultures. The proteins of the primary cultures could not be iodinated by lactoperoxidase suggesting that these proteins were present at a “cryptic” location at the surface of normal cells. We were not able to obtain serological or immunochemical evidence for the presence of SV40 large T‐antigen at the surface of any of the SV40‐trans‐formed cell lines tested using either hamster anti‐SV40 tumor sera, a rabbit antiserum against SDS‐denatured gel‐purified large T‐antigen or antisera against SV40‐transformed mouse cells. In conjunction with the report that large T‐antigen released from disrupted SV40‐transformed cells will bind to cell surfaces (Lange‐Mutschler and Henning, 1982), we consider the possibility that the specific rejection of SV40‐induced tumors by sensitized animals is the result of immunological reactions against both common transformation‐related surface antigens and SV40 T‐antigen from disrupted cells that has bound to the surface of other tumor cells.