Literature DB >> 6907092

Caeruloplasmin: a multi-functional metalloprotein of vertebrate plasma.

E Frieden.   

Abstract

Ceruloplasmin is a blue copper protein found in the alpha 2-globulin fraction of vertebrate plasma. It is a single-chain glycoprotein of molecular weight 132 000. It contains six copper atoms per molecule, comprising three or possibly four different types of copper. Its many functions may be related to the heterogeneous nature of these six copper atoms and to the various catalytic activities which they provide. Caeruloplasmin resembles albumin and transferrin in that all three serum proteins are regarded primarily as transport proteins. However, each has numerous other action as important as this transport function. Caeruloplasmin directly mobilizes iron into the serum and provides the major molecular link between copper and iron metabolism; it is the most prominent serum antioxidant, preventing deleterious oxidation of polyenoic acids and other substrates; it scavenges superoxide radicals; it serves as an acute-phase reactant (an endogenous modulator) of the inflammatory response; finally, caeruloplasmin may regulate the serum concentration of the biogenic amines, adrenaline (epinephrine) and serotonin (5-HT).

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Year:  1980        PMID: 6907092     DOI: 10.1002/9780470720622.ch6

Source DB:  PubMed          Journal:  Ciba Found Symp        ISSN: 0300-5208


  18 in total

1.  Caeruloplasmin biosynthesis by the human uterus.

Authors:  M L Schilsky; R J Stockert; J W Pollard
Journal:  Biochem J       Date:  1992-12-01       Impact factor: 3.857

2.  Identification of citrate as the albumin-bound inhibitor of the ferroxidase activity of ceruloplasmin.

Authors:  J Witwicki; M V Chidambaram; E Frieden
Journal:  Biol Trace Elem Res       Date:  1983-04       Impact factor: 3.738

3.  Hereditary deficiency of ferroxidase (aka caeruloplasmin)

Authors:  J I Logan
Journal:  J Neurol Neurosurg Psychiatry       Date:  1996-11       Impact factor: 10.154

4.  The valency state of absorbed iron appearing in the portal blood and ceruloplasmin substitution.

Authors:  P Wollenberg; R Mahlberg; W Rummel
Journal:  Biol Met       Date:  1990

5.  Isolation and characterization of copper-binding sites of human ceruloplasmin.

Authors:  K S Raju
Journal:  Mol Cell Biochem       Date:  1983       Impact factor: 3.396

6.  Internal duplication and evolution of human ceruloplasmin.

Authors:  F E Dwulet; F W Putnam
Journal:  Proc Natl Acad Sci U S A       Date:  1981-05       Impact factor: 11.205

7.  Ceruloplasmin, a copper-transport protein, can act as a growth promoter for some cell lines in serum-free medium.

Authors:  J P Mather
Journal:  In Vitro       Date:  1982-12

8.  Antioxidant potential, paraoxonase 1, ceruloplasmin activity and C-reactive protein concentration in diabetic retinopathy.

Authors:  Mariusz Nowak; Tomasz Wielkoszyński; Bogdan Marek; Beata Kos-Kudła; Elzbieta Swietochowska; Lucyna Siemińska; Jacek Karpe; Dariusz Kajdaniuk; Joanna Głogowska-Szelag; Katarzyna Nowak
Journal:  Clin Exp Med       Date:  2009-12-11       Impact factor: 3.984

9.  Copper toxicosis and tolerance in the rat: IV. Renal tubular excretion of copper.

Authors:  S Haywood; J Trafford; M Loughran
Journal:  Br J Exp Pathol       Date:  1985-12

10.  Hormonally produced changes in caeruloplasmin synthesis and secretion in primary cultured rat hepatocytes. Relationship to hepatic copper metabolism.

Authors:  A L Weiner; R J Cousins
Journal:  Biochem J       Date:  1983-05-15       Impact factor: 3.857

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