Document Detail


Accelerated secretion of human lysozyme with a disulfide bond mutation.
MedLine Citation:
PMID:  1572356     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
F Omura; M Otsu; M Kikuchi
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  205     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1992 Apr 
Date Detail:
Created Date:  1992-06-02     Completed Date:  1992-06-02     Revised Date:  2007-07-23    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  551-9     Citation Subset:  IM    
Affiliation:
Protein Engineering Research Institute, Osaka, Japan.
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MeSH Terms
Descriptor/Qualifier:
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:
0/Disulfides; 0/Oligodeoxyribonucleotides; 0/RNA, Messenger; 0/Recombinant Proteins; 56-41-7/Alanine; EC 3.2.1.17/Muramidase

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