| Accelerated secretion of human lysozyme with a disulfide bond mutation. | |
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MedLine Citation:
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PMID: 1572356 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The mutant human lysozyme, [Ala77, Ala95]lysozyme, in which the disulfide bond Cys77-Cys95 is eliminated, is known to exhibit increased secretion in yeast, compared to wild-type human lysozyme [Taniyama, Y., Yamamoto, Y., Nakao, M., Kikuchi, M. & Ikehara, M. (1988) Biochem. Biophys. Res. Commun. 152, 962-967]. To investigate this phenomenon, mammalian cells were used to analyze the secretion kinetics of [Ala77, Ala95]lysozyme and wild-type human lysozyme. The secretion rate of [Ala77, Ala95]lysozyme during the 150-min chase period was significantly accelerated [half-life (t1/2) = 29 min] compared to that of wild-type human lysozyme (t1/2 = 83 min), when expressed at the same levels within the cells. In contrast, after the 150-min chase, the rates of disappearance of both wild-type and mutant human lysozymes within the cells were similar, and considerably slower (t1/2 = 220 min), respectively. The remaining intracellular wild-type human lysozyme was localized mainly in the endoplasmic reticulum, whereas accelerated transport of the [Ala77, Ala95]lysozyme mutant protein from the endoplasmic reticulum to the Golgi apparatus was observed. Also in yeast cells, similar secretion kinetics and the differences in t1/2 for wild-type and mutant human lysozymes during the early chase period were observed. The two-phase kinetics of disappearance of intracellular human lysozymes suggest that only a proportion of the proteins becomes secretion competent soon after synthesis and is completely secreted during the early chase period, whereas others enter the distinct, slow pathways of intracellular transport and/or degradation. Increased secretion of [Ala77, Ala95]lysozyme is possibly due to enhanced competence for secretion acquired in the endoplasmic reticulum at the early stage of transport events, which is closely connected with the removal of a disulfide bond. |
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Authors:
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F Omura; M Otsu; M Kikuchi |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: European journal of biochemistry / FEBS Volume: 205 ISSN: 0014-2956 ISO Abbreviation: Eur. J. Biochem. Publication Date: 1992 Apr |
Date Detail:
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Created Date: 1992-06-02 Completed Date: 1992-06-02 Revised Date: 2007-07-23 |
Medline Journal Info:
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Nlm Unique ID: 0107600 Medline TA: Eur J Biochem Country: GERMANY |
Other Details:
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Languages: eng Pagination: 551-9 Citation Subset: IM |
Affiliation:
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Protein Engineering Research Institute, Osaka, Japan. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adenocarcinoma Alanine Amino Acid Sequence Animals Base Sequence Cell Line Cloning, Molecular Disulfides Gene Expression Genes, Synthetic Humans Kinetics L Cells (Cell Line) Mice Molecular Sequence Data Muramidase / biosynthesis*, genetics*, metabolism Mutation* Oligodeoxyribonucleotides Plasmids RNA, Messenger / genetics, metabolism Recombinant Proteins / biosynthesis*, metabolism Restriction Mapping Saccharomyces cerevisiae / genetics Transfection Vero Cells |
| Chemical | |
Reg. No./Substance:
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0/Disulfides; 0/Oligodeoxyribonucleotides; 0/RNA, Messenger; 0/Recombinant Proteins; 56-41-7/Alanine; EC 3.2.1.17/Muramidase |
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