Isolation, purification, and characterization of a mouse plasmacytoma cell surface glycoprotein involved in the resistance of the tumor cells to immune destruction

Y. Rosenstein, M. Theelen, I. Sanchez, Esteban Celis

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Abstract

Cells of a subline of the mouse plasmacytoma LPC-1 are resistant to lysis by cytotoxic T-lymphocytes, probably as a result of the blocking of the major histocompatibility gene complex-encoded cell surface antigens by a trypsin-sensitive glycoprotein of approximately 160 kilodaltons. The glycoprotein (gp160) was extracted from LPC-1 cells with 1.5 M urea and was further purified by ammonium sulfate precipitation with Sephacryl S-300 gel filtration. The gp160 consists of a single peptide chain rich in sialic acid residues (10% of total molecular weight) and has an acidic isoelectric point. The amino acid composition of gp160 is compatible with the linkage of carbohydrates (galactose, glucosamine, and sialic acid) to the protein portion. The apparent weak attachment of gp160 to the cell membrane could explain the finding that LPC-1 cells easily revert from the resistant to the sensitive to the immune lysis phenotype.

Original languageEnglish (US)
Pages (from-to)609-616
Number of pages8
JournalJournal of the National Cancer Institute
Volume74
Issue number3
StatePublished - Jan 1 1985
Externally publishedYes

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Plasmacytoma
Membrane Glycoproteins
N-Acetylneuraminic Acid
Glycoproteins
Carbohydrate Conformation
Neoplasms
Glucosamine
Isoelectric Point
Ammonium Sulfate
Cytotoxic T-Lymphocytes
Surface Antigens
Major Histocompatibility Complex
Galactose
Trypsin
Gel Chromatography
Urea
Molecular Weight
Cell Membrane
Phenotype
Amino Acids

ASJC Scopus subject areas

  • Oncology
  • Cancer Research

Cite this

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abstract = "Cells of a subline of the mouse plasmacytoma LPC-1 are resistant to lysis by cytotoxic T-lymphocytes, probably as a result of the blocking of the major histocompatibility gene complex-encoded cell surface antigens by a trypsin-sensitive glycoprotein of approximately 160 kilodaltons. The glycoprotein (gp160) was extracted from LPC-1 cells with 1.5 M urea and was further purified by ammonium sulfate precipitation with Sephacryl S-300 gel filtration. The gp160 consists of a single peptide chain rich in sialic acid residues (10{\%} of total molecular weight) and has an acidic isoelectric point. The amino acid composition of gp160 is compatible with the linkage of carbohydrates (galactose, glucosamine, and sialic acid) to the protein portion. The apparent weak attachment of gp160 to the cell membrane could explain the finding that LPC-1 cells easily revert from the resistant to the sensitive to the immune lysis phenotype.",
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T1 - Isolation, purification, and characterization of a mouse plasmacytoma cell surface glycoprotein involved in the resistance of the tumor cells to immune destruction

AU - Rosenstein, Y.

AU - Theelen, M.

AU - Sanchez, I.

AU - Celis, Esteban

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N2 - Cells of a subline of the mouse plasmacytoma LPC-1 are resistant to lysis by cytotoxic T-lymphocytes, probably as a result of the blocking of the major histocompatibility gene complex-encoded cell surface antigens by a trypsin-sensitive glycoprotein of approximately 160 kilodaltons. The glycoprotein (gp160) was extracted from LPC-1 cells with 1.5 M urea and was further purified by ammonium sulfate precipitation with Sephacryl S-300 gel filtration. The gp160 consists of a single peptide chain rich in sialic acid residues (10% of total molecular weight) and has an acidic isoelectric point. The amino acid composition of gp160 is compatible with the linkage of carbohydrates (galactose, glucosamine, and sialic acid) to the protein portion. The apparent weak attachment of gp160 to the cell membrane could explain the finding that LPC-1 cells easily revert from the resistant to the sensitive to the immune lysis phenotype.

AB - Cells of a subline of the mouse plasmacytoma LPC-1 are resistant to lysis by cytotoxic T-lymphocytes, probably as a result of the blocking of the major histocompatibility gene complex-encoded cell surface antigens by a trypsin-sensitive glycoprotein of approximately 160 kilodaltons. The glycoprotein (gp160) was extracted from LPC-1 cells with 1.5 M urea and was further purified by ammonium sulfate precipitation with Sephacryl S-300 gel filtration. The gp160 consists of a single peptide chain rich in sialic acid residues (10% of total molecular weight) and has an acidic isoelectric point. The amino acid composition of gp160 is compatible with the linkage of carbohydrates (galactose, glucosamine, and sialic acid) to the protein portion. The apparent weak attachment of gp160 to the cell membrane could explain the finding that LPC-1 cells easily revert from the resistant to the sensitive to the immune lysis phenotype.

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