Expression of murine and human granulocyte‐macrophage colony‐stimulating factors in S. cerevisiae: mutagenesis of the potential glycosylation sites
Murine (m) and human (h) granulocyte‐‐macrophage colony‐stimulating factors (GM‐CSF) have been expressed in large quantities in Saccharomyces cerevisiae using a secretion vector containing the promoter and leader sequences of the mating pheromone alpha‐factor. Functionally active mGM‐CSF was identif...
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Published in | The EMBO journal Vol. 5; no. 6; pp. 1193 - 1197 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
London
Nature Publishing Group
01.06.1986
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Abstract | Murine (m) and human (h) granulocyte‐‐macrophage colony‐stimulating factors (GM‐CSF) have been expressed in large quantities in Saccharomyces cerevisiae using a secretion vector containing the promoter and leader sequences of the mating pheromone alpha‐factor. Functionally active mGM‐CSF was identified by a proliferation assay with a factor‐dependent cell line and by a granulocyte‐‐macrophage colony formation assay using bone marrow cells. The activity of hGM‐CSF was confirmed by stimulation of granulocyte‐‐macrophage colony formation using human cord blood cells. Murine GM‐CSF with various apparent mol. wts (13, 18, 24, 34 and 40 kd, as well as a smear of higher mol. wts) was detected in yeast culture medium by protein blotting using a rat monoclonal antibody specific for the mGM‐CSF N‐terminal region peptide. Protein blotting using a rat monoclonal antibody specific for the hGM‐CSF N‐terminal region demonstrated that a 15.6‐kd and higher mol. wt heterogeneous species were secreted. Mutations introduced at each of the two potential N‐linked glycosylation sites in mGM‐CSF showed that the 13‐kd protein is not glycosylated and the major 18‐kd protein is mainly glycosylated at the more C‐terminal site, whereas the heterogeneous higher mol. wt species were not affected by the mutations. The N‐terminal amino acid of the 13‐kd protein was shown to be Ser which was four amino acids in the C‐terminal direction from the fusion point. |
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AbstractList | Murine (m) and human (h) granulocyte-macrophage colony-stimulating factors (GM-CSF) have been expressed in large quantities in Saccharomyces cerevisiae using a secretion vector containing the promoter and leader sequences of the mating pheromone alpha -factor. Functionally active mGM-CSF was identified. The activity of hGM-CSF was confirmed. Murine GM-CSF with various apparent mol. wts was detected in yeast culture medium. Protein blotting demonstrated that a 15.6-kd and higher mol. wt heterogeneous species were secreted. Mutations introduced at each of the two potential N-linked glycosylation sites in mGM-CSF showed that the 13-kd protein is not glycosylated and the major 18-kd protein is mainly glycosylated at the more C-terminal site, whereas the heterogeneous higher mol. wt species were not affected by the mutations. The N-terminal amino acid of the 13-kd protein was shown to be Ser which was four amino acids in the C-terminal direction from the fusion point. Murine (m) and human (h) granulocyte--macrophage colony-stimulating factors (GM-CSF) have been expressed in large quantities in Saccharomyces cerevisiae using a secretion vector containing the promoter and leader sequences of the mating pheromone alpha-factor. Functionally active mGM-CSF was identified by a proliferation assay with a factor-dependent cell line and by a granulocyte--macrophage colony formation assay using bone marrow cells. The activity of hGM-CSF was confirmed by stimulation of granulocyte--macrophage colony formation using human cord blood cells. Murine GM-CSF with various apparent mol. wts (13, 18, 24, 34 and 40 kd, as well as a smear of higher mol. wts) was detected in yeast culture medium by protein blotting using a rat monoclonal antibody specific for the mGM-CSF N-terminal region peptide. Protein blotting using a rat monoclonal antibody specific for the hGM-CSF N-terminal region demonstrated that a 15.6-kd and higher mol. wt heterogeneous species were secreted. Mutations introduced at each of the two potential N-linked glycosylation sites in mGM-CSF showed that the 13-kd protein is not glycosylated and the major 18-kd protein is mainly glycosylated at the more C-terminal site, whereas the heterogeneous higher mol. wt species were not affected by the mutations. The N-terminal amino acid of the 13-kd protein was shown to be Ser which was four amino acids in the C-terminal direction from the fusion point. |
Author | Bond, M.W. Abrams, J.S. Schreurs, J. Otsu, K. Arai, K. Miyajima, A. |
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Keywords | Human Yeast Secretion Rodentia Glycosylation Gene expression Biological activity Fungi Vertebrata Mammalia Mutagenesis Mouse Ascomycetes Molecular cloning Saccharomyces cerevisiae Vector Granulocyte macrophage colony stimulating activity Thallophyta |
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Snippet | Murine (m) and human (h) granulocyte‐‐macrophage colony‐stimulating factors (GM‐CSF) have been expressed in large quantities in Saccharomyces cerevisiae using... Murine (m) and human (h) granulocyte--macrophage colony-stimulating factors (GM-CSF) have been expressed in large quantities in Saccharomyces cerevisiae using... Murine (m) and human (h) granulocyte-macrophage colony-stimulating factors (GM-CSF) have been expressed in large quantities in Saccharomyces cerevisiae using a... |
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SubjectTerms | Amino Acids - analysis Animals Antibodies, Monoclonal Base Sequence Biological and medical sciences Biotechnology Colony-Stimulating Factors - genetics Colony-Stimulating Factors - isolation & purification Colony-Stimulating Factors - pharmacology Fundamental and applied biological sciences. Psychology Genetic engineering Genetic technics Glycosides - analysis Humans Methods. Procedures. Technologies Mice Molecular cloning Molecular Weight Mutation Plasmids Saccharomyces cerevisiae Saccharomyces cerevisiae - genetics |
Title | Expression of murine and human granulocyte‐macrophage colony‐stimulating factors in S. cerevisiae: mutagenesis of the potential glycosylation sites |
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