Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
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Target Concepts:
Gene/Protein
Disease
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Drug
Enzyme
Compound
Query: EC:1.16.3.1 (
ceruloplasmin
)
5,074
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Ceruloplasmin, the blue copper-protein of the blood plasma, is believed by some workers to be involved in the metabolic management of 5-hydroxytryptamine (serotonin) during pregnancy.
5-Hydroxytryptamine
is abortifacient in experimental animals. By some authors, a role has been suggested for it in human abortion. The plasma concentrations of 5-hydroxytryptamine, copper and
ceruloplasmin
were measured in non-pregnant women, in normal early pregnancy and in cases of spontaneous abortion. Compared with normal early pregnancy, cases of inevitable abortion show lower values for both plasma copper and
ceruloplasmin
and higher values for plasma 5-hydroxytryptamine. The possible implications of these findings are discussed in view of the alterations in
ceruloplasmin
values in pregnancy and in the light of what is known of the pharmacology and metabolism of 5-hydroxytryptamine. It it believed that these alterations in plasma copper,
ceruloplasmin
and 5-hydroxytryptamine in cases of inevitable abortion are the effect, rather than the cause, of abortion.
...
PMID:5-Hydroxytryptamine (serotonin), copper and ceruloplasmin plasma concentrations in spontaneous abortion. 26 87
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
).
...
PMID:Caeruloplasmin: a multi-functional metalloprotein of vertebrate plasma. 690 92
The aim of the current study was to determine the physiological response to feed restriction in female broiler breeders using a range of conventional and novel indicators. One hundred female breeders were subjected to one of five feeding regimens from d 28 to 42 as follows (i) ad libitum feeding (AL), (ii-v) 75, 60, 45, and 30% of ad libitum feed intake. Blood heterophil to lymphocyte ratio (HLR), and plasma circulating corticosterone (CORT), ghrelin (GHR), serotonin (
5-HT
), and dopamine (DA) and serum acute phase proteins (APP) concentrations together with brain heat shock protein (HSP) 70 level were measured. The results showed a significant effect of feed restriction on blood HLR and plasma CORT, GHR,
5-HT
, DA, and brain HSP 70 levels. However, feed restriction had no effect on serum levels of APP of alpha-1 acid glycoprotein, ovotransferin, and
ceruloplasmin
. Serum levels of
5-HT
and GHR varied curvilinearly with the feed restriction level. The relationship between brain HSP 70 and level of feed restriction was negligible. However, significant linear relationships between HLR, CORT, DA, and the level of feed restriction were noted. Thus, these 3 parameters appear to represent a straight forward relation with severity of feed restriction.
...
PMID:The effect of different degrees of feed restriction on heat shock protein 70, acute phase proteins, and other blood parameters in female broiler breeders. 2631 43
Human
ceruloplasmin
(hCP) is a multi-copper oxidase with
ferroxidase
and amine oxidase activities. Molecular dynamics simulation (MDS) and docking analysis of biogenic monoamines with
ceruloplasmin
explain the role of Asp1025, Glu935, Glu272, Glu232 and Glu230 together with the binding site water molecules (referred as conserved water molecules) in the stabilization of neurotransmitter (
Serotonin
, Norepinephrine and Epinephrine) molecules within the binding cavity of hCP. Conserved water molecules are found at specific positions interacting with the protein structures that have sequence similarity. The ethylamine side chain nitrogen atom (N1) of neurotransmitter molecules interacts with water molecules in the binding cavity formed by Asp1025, Glu935 and Glu232 residues. These residues form an acidic triad mimicking a substrate binding cavity. The hydroxyl groups attached to the catechol ring of epinephrine and norepinephrine have been stabilized by Asp230 and Asp232 residues. Data suggests that the recognition of biogenic amines mediates through the N+(amine) ...Asp1025-His1026-Cu
Cis-His
path. The potential recognition path of biogenic monoamines to trinuclear copper cluster supported by active site water molecules (referred as conserved water molecules) is described in this report.
...
PMID:Insights from molecular dynamics simulation of human ceruloplasmin (ferroxidase enzyme) binding with biogenic monoamines. 3183 58