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Topic:Ferritin

Ferritin is a protein complex that serves as the primary intracellular iron storage in horses, playing a vital role in iron homeostasis. It enables the safe storage and release of iron, which is essential for various physiological processes, including oxygen transport and DNA synthesis. In equine medicine, ferritin levels are measured to assess iron status and diagnose conditions related to iron metabolism, such as anemia or iron overload. Variations in ferritin concentrations can indicate underlying health issues, making it a valuable parameter in veterinary diagnostics. This page compiles peer-reviewed research studies and scholarly articles that explore the structure, function, and clinical relevance of ferritin in equine health.
Iron-related markers of inflammation in horses with colic.
Journal of equine veterinary science    January 28, 2024   Volume 134 105010 doi: 10.1016/j.jevs.2024.105010
Canola PA, Salles RF, Daneze ER, Sobreira MFR, Oliveira BE, Favero ML, Antonioli ML.The aim of the study was to compare and correlate levels of ferritin, transferrin, iron and APPs in healthy horses and those surgically treated for strangulating colic. On admission, measurements of inflammatory markers related to iron and total protein, fibrinogen, albumin, haptoglobin and ceruloplasmin were made. The study comprised 22 horses, divided into a control group (CG) of healthy horses (n = 10) and horses with surgically treated acute abdomen (n = 12), obstruction group (OG). The OG was subdivided according to the affected intestinal segment (small vs. large) and according to ou...
Adaptive Response of Estrogen-Iron Axis in Pregnant Purebred Spanish Mares of Different Age.
Journal of equine veterinary science    May 27, 2023   Volume 127 104827 doi: 10.1016/j.jevs.2023.104827
Satué K, Fazio E, La Fauci D, Bruschetta G, Medica P.The maintenance of iron (Fe) homeostasis is vital for the physiological function along life. In sexually mature humans and experimental animals, estrogens downregulate hepcidin (Hpc) expression, in order to improve the intestinal absorption and to mobilize Fe stores for maternal erythropoietic expansion and placental development. However, changes of these mechanisms related to regulation of Hpc on the availability of Fe during gestation with advancing age in mares, remain unknown. The objective of this study was to evaluate the interrelationships between serum Fe, Ferritin (Ferr) and Hpc with ...
Serum amyloid A, haptoglobin, and ferritin in horses with colic: Association with common clinicopathological variables and short-term outcome.
Veterinary journal (London, England : 1997)    March 19, 2015   Volume 205, Issue 1 50-55 doi: 10.1016/j.tvjl.2015.03.015
Dondi F, Lukacs RM, Gentilini F, Rinnovati R, Spadari A, Romagnoli N.Equine colic may be associated with an acute phase response (APR). Measurement of acute phase proteins (APPs) allows the detection of an APR and may help clinicians in monitoring the disease; however, the role of APPs in colic is unclear. This study aimed to evaluate the clinical usefulness of serum amyloid A (SAA), haptoglobin and ferritin in combination with an extended clinicopathological profile in equine colic. The medical records of 54 horses were retrospectively selected. Horses were grouped based on outcome (survivors vs. non-survivors), diagnosis (ischaemic/strangulating vs. non-ischa...
On the repair of oxidative damage to apoferritin: a model study with the flavonoids quercetin and rutin in aerated and deaerated solutions.
Free radical research    May 2, 2013   Volume 47, Issue 6-7 463-473 doi: 10.3109/10715762.2013.791024
Morlière P, Mazière JC, Patterson LK, Conte MA, Dupas JL, Ducroix JP, Filipe P, Santus R.Ferritin (Ft) impairment through (•)O2(-), H2O2, and (•)OH production occurs in the cases of ketoses, diabetes mellitus, acute intermittent porphyria and tyrosinemia. In addition to (•)Trp and TyrO(•) radical production, ferrous iron liberation and Ft synthesis stimulation, site-specific oxidation reactions are induced leading to toxic iron accumulation in organs with high Ft content, for example, liver and brain. To elucidate the potential pathways to Ft recovery, repair of oxidative damage to horse spleen apoferritin (apoFt) and Ft by quercetin (QH) or rutin (RH) was studied in the p...
Change of antibody levels to ferritin in the sera of foals after birth: possible passive transfer of maternal anti-ferritin autoantibody via colostrum and age-related anti-ferritin autoantibody production.
Animal science journal = Nihon chikusan Gakkaiho    April 18, 2013   Volume 84, Issue 12 782-789 doi: 10.1111/asj.12069
Numata M, Kondo T, Nambo Y, Yoshikawa Y, Watanabe K, Orino K.Antibody (immunoglobulin G (IgG), IgM or IgA) levels relative to ferritin in six foal sera (three male and three female) after birth (day 0 and 2, 6, 10, 20, 28, 36, 40, 52 and 56 weeks of age) were semi-quantitatively measured with normalization with antibody activity to ferritin in one adult horse serum. After addition of horse spleen ferritin to the serum sample, the complex formed between antibodies to ferritin in the serum and ferritin was co-immunoprecipitated using antibody to horse spleen ferritin. Antibody classes of the co-immnoprecipitate were detected with antibodies specific for h...
Change of Ferritin-binding Activity in the Serum of Foal after Birth.
Journal of equine science    February 28, 2012   Volume 22, Issue 4 73-76 doi: 10.1294/jes.22.73
Ohya T, Kondo T, Yoshikawa Y, Watanabe K, Orino K.In mammal circulation, various ferritin-binding proteins (FBPs) are thought to be involved in the clearance of circulating ferritin after complex formation with it. However, horse FBPs are known to cause inhibitory effects on ferritin immunoassay due to the concealment of the ferritin molecule to anti-ferritin antibodies used in the ferritin immunoassay. These inhibitory effects are eliminated by heat treatment of horse serum at 75°C for 15 min. The inhibitory effects on ferritin immunoassay in the sera of ten foal sera (5 females and 5 males) from 1 to 18 months were detected during all peri...
Ferritin-catalyzed consumption of hydrogen peroxide by amine buffers causes the variable Fe2+ to O2 stoichiometry of iron deposition in horse spleen ferritin.
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry    July 29, 2006   Volume 11, Issue 8 1075-1086 doi: 10.1007/s00775-006-0141-6
Zhang B, Wilson PE, Watt GD.Ferritin catalyzes the oxidation of Fe2+ by O2 to form a reconstituted Fe3+ oxy-hydroxide mineral core, but extensive studies have shown that the Fe2+ to O2 stoichiometry changes with experimental conditions. At Fe2+ to horse spleen ferritin (HoSF) ratios greater than 200, an upper limit of Fe2+ to O2 of 4 is typically measured, indicating O2 is reduced to 2H2O. In contrast, a lower limit of Fe2+ to O2 of approximately 2 is measured at low Fe2+ to HoSF ratios, implicating H2O2 as a product of Fe2+ deposition. Stoichiometric amounts of H2O2 have not been measured, and H2O2 is proposed to react ...
Miscibility of binary monolayers at the air-water interface and interaction of protein with immobilized monolayers by surface plasmon resonance technique.
Langmuir : the ACS journal of surfaces and colloids    June 28, 2006   Volume 22, Issue 14 6195-6202 doi: 10.1021/la0605642
Wang Y, Du X.The miscibility and stability of the binary monolayers of zwitterionic dipalmitoylphosphatidylcholine (DPPC) and cationic dioctadecyldimethylammonium bromide (DOMA) at the air-water interface and the interaction of ferritin with the immobilized monolayers have been studied in detail using surface pressure-area isotherms and surface plasmon resonance technique, respectively. The surface pressure-area isotherms indicated that the binary monolayers of DPPC and DOMA at the air-water interface were miscible and more stable than the monolayers of the two individual components. The surface plasmon re...
Effect of exercise on plasma ferritin concentrations: implications for the measurement of iron status.
Equine veterinary journal. Supplement    October 31, 2002   Issue 34 186-190 doi: 10.1111/j.2042-3306.2002.tb05416.x
Hyyppä S, Höyhtyä M, Nevalainen M, Pösö AR.Iron is of key importance for aerobic metabolism, and natural feeds of the horse are fairly rich sources of iron. Accordingly, the known incidence of iron deficiency anaemia is apparently rare in performance horses; despite this, iron deficiency in performance horses continues to be of concern to trainers and veterinarians. Effects of exercise on plasma ferritin concentrations were therefore studied in Standardbreds, Finnhorses and half-bred riding horses. Blood samples were taken after a moderate exercise test on a racetrack, a competition exercise test on a treadmill and a race. Even moderat...
Permeation of small molecules into the cavity of ferritin as revealed by proton nuclear magnetic resonance relaxation.
The Biochemical journal    April 1, 1995   Volume 307 ( Pt 1), Issue Pt 1 253-256 doi: 10.1042/bj3070253
Yang D, Nagayama K.The NMR relaxation technique was used to investigate the permeation of molecules into the cavity of ferritin. Spin-lattice relaxation times in the rotating frame of various probe molecules were measured for solutions of recombinant horse L-apoferritin without iron and horse spleen apoferritin with very small amounts of ferric ions. The results show that molecules larger than the size of the ferritin channels can pass through the channels into the ferritin interior, and that the maximum size of molecules for the permeation is smaller than maltotriose.
Fibrinogen as a ferritin-binding protein in horse plasma.
The Journal of veterinary medical science    October 1, 1993   Volume 55, Issue 5 785-787 doi: 10.1292/jvms.55.785
Orino K, Yamamoto S, Watanabe K.Lower apparent concentrations of ferritin were observed in horse plasma than in serum using the enzyme-linked immunosorbent assay (ELISA). However, the ferritin concentrations in plasma and serum were increased to the same level on heating the samples at 75 degrees C for 15 min. These results suggest that horse plasma has specific ferritin-binding protein(s) which inhibit(s) the ferritin assay. The apparent ferritin concentrations in horse serum were markedly decreased by adding horse fibrinogen to the serum. It was also found that fibrinogen bound to spleen ferritin and inhibited the immunoas...
Ferritin: the role of aluminum in ferritin function.
Neurobiology of aging    September 1, 1991   Volume 12, Issue 5 413-418 doi: 10.1016/0197-4580(91)90066-s
Fleming JT, Joshi JG.We previously showed that human brain ferritin (HBF) binds aluminum (Al) in vivo and in vitro and HBF isolated from Alzheimer's brain had more Al bound compared to aged matched controls (7). To further understand the role ferritin may play in Al neurotoxicity, we have studied in vitro the effect of Al on the function of human ferritin isolated from Alzheimer's (AD) and normal brain tissue, and compared the results with other mammalian ferritins. Al causes a concentration-dependent decrease in the initial rate of iron loading into apo-horse spleen and human brain ferritin and the rates were sim...
Structural and functional studies on ferritins.
Biochemical Society transactions    August 1, 1987   Volume 15, Issue 4 744-748 doi: 10.1042/bst0150744
Harrison PM, Ford GC, Rice DW, Smith JM, Treffry A, White JL.No abstract available
Iron deposition in apoferritin. Evidence for the formation of a mixed valence binuclear iron complex.
The Journal of biological chemistry    March 10, 1985   Volume 260, Issue 5 2926-2929 
Chasteen ND, Antanaitis BC, Aisen P.A preliminary EPR investigation of iron accumulation in apoferritin has identified paramagnetic species generated during the early stage of iron deposition within the apoprotein shell. A featureless resonance at g' = 4.3, attributable to solitary high spin Fe3+ ions bound to the protein, is generated when Fe(II) is added to apoferritin at a level of 0.5 Fe/subunit (12 Fe/molecule) followed by air oxidation. This resonance accounts for 36% of the added iron. The remainder is EPR-silent and is probably present as oligomeric Fe3+ species. The intensity of the g' = 4.3 signal is reduced 3-fold upo...
The preparative separation of horse and human ferritins by chromatofocusing.
Journal of chromatography    June 1, 1984   Volume 292, Issue 2 454-457 doi: 10.1016/s0021-9673(01)83628-1
Addison JM, Lewis WG, Harrison PM.No abstract available
Rat lymphocyte proliferative in vitro response to horse spleen ferritin.
Journal of the Reticuloendothelial Society    September 1, 1981   Volume 30, Issue 3 227-234 
Lause DB, Houston JA, Bockman DE.No abstract available
Iron mobilization from ferritin by chelating agents.
Journal of inorganic biochemistry    December 1, 1980   Volume 13, Issue 4 305-316 doi: 10.1016/s0162-0134(00)80251-2
Crichton RR, Roman F, Roland F.The release of iron from horse spleen ferritin by the chelating agents desferrioxamine B, rhodotorulic acid, 2,3-dihydroxybenzoate, 2,2'-bipyridyl and pyridine-2-aldehyde-2-pyridyl hydrazone (Paphy) has been studied in vitro. Ferritin prepared by classical procedures involving thermal denaturation releases its iron less effectively than ferritin isolated by a modified procedure that avoids this step. Desferrioxamine B and rhodotorulic acid are the most effective in releasing iron from both preparations of ferritin. When FMN is added, iron release by desferrioxamine B, rhodotorulic acid, and 2,...
Cross-reactivity in the radioimmunoassay of ferritin with cells from high- and low-responder mice.
Biochemical Society transactions    January 1, 1977   Volume 5, Issue 1 256-258 doi: 10.1042/bst0050256
Deacon NJ, Ebringer A.No abstract available
Studies on iron uptake and micelle formation in ferritin and apoferritin.
Molecular and cellular biochemistry    October 30, 1976   Volume 13, Issue 1 55-61 doi: 10.1007/BF01732396
Stefanini S, Chiancone E, Vecchini P, Antonini E.Iron uptake and micelle formation in ferritin and apoferritin have been followed both spectrophotometrically and by means of sedimentation velocity experiments. Information was thus obtained on the molecular weight distribution of the reconstitution product. To achieve incorporation 'native' ferritin (whole ferritin as purified from horse spleen), 'native' apoferritin (apoferritin prepared by fractionation of ferritin preparations) and 'reduced' apoferritin (apoferritin prepared by reduction of ferritin by dithionite or ascorbic acid) have been incubated with ferrous salts in the presence of o...
A tetragonal crystal form of horse spleen apoferritin and its relationship to the cubic modification.
Journal of molecular biology    June 25, 1974   Volume 86, Issue 2 301-308 doi: 10.1016/0022-2836(74)90020-5
Hoy TG, Harrison PM, Hoare RJ.Horse spleen apoferritin has been crystallized as tetragonal plates and needles with a unit cell with a = b = 147 ± 0.5 A and c = 154.4±0.5 A. The space group is P4212 and the unit cell contains two molecules in a pseudo-body-centred arrangement. The intensity distributions and calculated rotation functions of tetragonal and cubic crystals have been compared. The symmetry of the dif-fraction patterns from cubic crystals indicates that the molecules have 432 sym metry with their 4-fold axes lying along the cube axes. In the tetragonal crystals one molecular 4-fold axis lies parallel to c, the...
The release of iron from horse spleen ferritin to 1,10-phenanthroline.
The Biochemical journal    January 1, 1974   Volume 137, Issue 1 67-70 doi: 10.1042/bj1370067
Hoy TG, Harrison PM, Shabbir M, Macara IG.The rate of release of iron to 1,10-phenanthroline from ferritin fractions of different iron contents has been studied. The experimental results could be interpreted by a simple hypothetical model of the shape of the hydrous ferric oxide micelle at different iron contents, and reasonable correlation obtained between the rate of release and the calculated micelle surface areas. Initial rates of release did not correlate significantly with protein concentration.
Synthesis of liver ferritin on free and membrane-bound polyribosomes of different sizes.
FEBS letters    December 1, 1973   Volume 37, Issue 2 249-252 doi: 10.1016/0014-5793(73)80471-5
Konijn AM, Baliga BS, Munro HN.No abstract available
The biochemistry of ferritin.
British journal of haematology    June 1, 1973   Volume 24, Issue 6 677-680 doi: 10.1111/j.1365-2141.1973.tb01695.x
Crichton RR.The researchers investigated the biochemical properties of ferritin, a protein responsible for iron storage in the body. They identified its distribution and structure, noting variations in different species and tissues. […]
Ferritin and ferritin iron measurement in tissues by a quantitative immunoprecipitation technique.
Analytical biochemistry    September 1, 1970   Volume 37, Issue 1 64-72 doi: 10.1016/0003-2697(70)90258-7
Leslie AJ, Kaldor I.No abstract available
Microheterogeneity in ferritin molecules.
Biochimica et biophysica acta    April 28, 1970   Volume 207, Issue 1 256-258 doi: 10.1016/0005-2795(70)90158-3
Drysdale JW.No abstract available
[Comparative studies on ferritin isolated from various animal species. 3. I. Fractionation of ferritin from the spleen of dolphin (Dolphinus cetacea). II. Comparative studies of ferritin from the spleens of terrestial mammals (horses, rabbits) and marine mammals (tunafish, dolphins)].
Seikagaku. The Journal of Japanese Biochemical Society    February 1, 1969   Volume 41, Issue 2 61-71 
Kato T.No abstract available
[Immunological analogies of ferritin and equine hemosiderin].
Bulletin de la Societe de chimie biologique    January 1, 1963   Volume 45 377-382 
de BORNIER B.No abstract available