Document Detail


Caeruloplasmin biosynthesis by the human uterus.
MedLine Citation:
PMID:  1463466     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The blue copper protein caeruloplasmin is synthesized mainly by hepatocytes. An alternative transcript for caeruloplasmin produced in certain extrahepatic tissues, CP-1, contains an additional 12 nucleotides encoding 4 amino acids not present in the hepatic transcript, CP-2 [Yang, Friedrichs, Cupples, Bonifacio, S Sanford, Horton & Bowman (1990) J. Biol. Chem. 265, 10780-10785]. We have demonstrated transcription of caeruloplasmin mRNA by a well-differentiated human uterine epithelial adenocarcinoma cell line, Ishikawa, and by human uterine endometrium and purified endometrial glands. Identical CP-2 nucleotide sequences were obtained for partial caeruloplasmin transcripts from human liver and Ishikawa cells, indicating that CP-2 transcripts are produced by uterine epithelial lining cells. The synthesis of caeruloplasmin protein was demonstrated for Ishikawa cells and another uterine adenocarcinoma cell line, ECC1. Peptide-mapping analysis indicated that caeruloplasmin secreted by Ishikawa cells was structurally identical with the protein synthesized by the human hepatoblastoma cell line HepG2. The secretion of a 135,000-M(r) caeruloplasmin by Ishikawa and ECC1 cells, comparable with that of the human hepatoblastoma cell line, HepG2, indicated similar processing of uterine and hepatic caeruloplasmin. Incorporation of 67Cu into caeruloplasmin was demonstrated for Ishikawa and ECC1 cells, suggesting that the human uterus produces a bioactive form of caeruloplasmin and possesses the necessary metal transporters and intracellular machinery for copper incorporation into this protein.
Authors:
M L Schilsky; R J Stockert; J W Pollard
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Biochemical journal     Volume:  288 ( Pt 2)     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1992 Dec 
Date Detail:
Created Date:  1993-01-08     Completed Date:  1993-01-08     Revised Date:  2010-09-07    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  657-61     Citation Subset:  IM    
Affiliation:
Department of Medicine, Albert Einstein College of Medicine, Bronx, NY.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/D10990;  D10991;  D10992;  D10993;  D10994;  M86481;  X65732;  X65733;  X65734;  X69706
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MeSH Terms
Descriptor/Qualifier:
Base Sequence
Cells, Cultured
Ceruloplasmin / biosynthesis*,  genetics
Copper / metabolism
Female
Gene Expression
Humans
Liver / physiology
Molecular Sequence Data
Oligodeoxyribonucleotides / chemistry
Peptide Mapping
Polymerase Chain Reaction
RNA, Messenger / genetics
Uterus / metabolism*
Grant Support
ID/Acronym/Agency:
DK-01925/DK/NIDDK NIH HHS; DK-32972/DK/NIDDK NIH HHS; HD-25076/HD/NICHD NIH HHS
Chemical
Reg. No./Substance:
0/Oligodeoxyribonucleotides; 0/RNA, Messenger; 7440-50-8/Copper; EC 1.16.3.1/Ceruloplasmin
Comments/Corrections

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