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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1994-9-6
|
| pubmed:abstractText |
A protein of molecular weight 60 kDa was purified from the culture medium of a murine colon carcinoma cell line, colon26, and its partial amino-acid sequence determined. Extremely high homology was found with the deduced sequence from cDNA of rat ERp61, earlier found to be an endoplasmic reticulum (ER)-resident protein with redox activity and a similar structure to protein disulfide isomerase (PDI). Western blotting analysis showed that colon26 cells secrete a significant amount of ERp61 into culture medium, although most remains intracellular. The thiol:protein disulfide oxidoreductase activity of the purified mouse ERp61 was demonstrated by insulin-reduction assay. The ER location of the protein in fibroblasts was immunocytochemically confirmed by double staining for ERp61 and another ER-resident protein, PDI or Hsp47. Immunohistochemical studies of murine tissues showed a ubiquitous distribution of ERp61 in a wide variety of cell types. However, it was particularly abundant in plasma cells, mucus-secreting cells in various tissues, neuroendocrine cells including neurons, and follicular epithelia of thyroid gland that actively synthesize and secrete proteins containing cysteine residues. Furthermore, a high correlation was observed between intracellular amounts of ERp61 and immunoglobulin production by hybridoma cells. These results indicate that ERp61 may be involved in disulfide bond formation for such proteins.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/Grp58 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin G,
http://linkedlifedata.com/resource/pubmed/chemical/Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Disulfide-Isomerases
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0014-4827
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
213
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
N
|
| pubmed:pagination |
348-58
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading |
pubmed-meshheading:8050492-Amino Acid Sequence,
pubmed-meshheading:8050492-Animals,
pubmed-meshheading:8050492-Base Sequence,
pubmed-meshheading:8050492-Blotting, Western,
pubmed-meshheading:8050492-Colonic Neoplasms,
pubmed-meshheading:8050492-DNA, Neoplasm,
pubmed-meshheading:8050492-Endoplasmic Reticulum,
pubmed-meshheading:8050492-Heat-Shock Proteins,
pubmed-meshheading:8050492-Hybridomas,
pubmed-meshheading:8050492-Immunoglobulin G,
pubmed-meshheading:8050492-Immunohistochemistry,
pubmed-meshheading:8050492-Isomerases,
pubmed-meshheading:8050492-Mice,
pubmed-meshheading:8050492-Molecular Sequence Data,
pubmed-meshheading:8050492-Organ Specificity,
pubmed-meshheading:8050492-Oxidation-Reduction,
pubmed-meshheading:8050492-Protein Disulfide-Isomerases,
pubmed-meshheading:8050492-Tumor Cells, Cultured
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
Tissue distribution of ERp61 and association of its increased expression with IgG production in hybridoma cells.
|
| pubmed:affiliation |
Second Department of Pathology, Nagoya University School of Medicine, Japan.
|
| pubmed:publicationType |
Journal Article
|