bacterial transferrin receptor complex

• 細菌トランスフェリン受容体複合体

WordNet

1. complicated in structure; consisting of interconnected parts; "a complex set of variations based on a simple folk melody"; "a complex mass of diverse laws and customs"
2. a compound described in terms of the central atom to which other atoms are bound or coordinated (同)coordination_compound
3. a conceptual whole made up of complicated and related parts; "the complex of shopping malls, houses, and roads created a new town" (同)composite
4. (psychoanalysis) a combination of emotions and impulses that have been rejected from awareness but still influence a persons behavior
5. (microbiology) single-celled or noncellular spherical or spiral or rod-shaped organisms lacking chlorophyll that reproduce by fission; important as pathogens and for biochemical properties; taxonomy is difficult; often considered to be plants (同)bacterium
6. relating to or caused by bacteria; "bacterial infection"
7. a cellular structure that is postulated to exist in order to mediate between a chemical agent that acts on nervous tissue and the physiological response
8. a globulin in blood plasma that carries iron (同)beta_globulin, siderophilin

PrepTutorEJDIC

1. 『いくつかの部分から成る』,複合の,合成の / 『複雑な』,入りくんだ,こみいった(complicated) / 複合体,合成物 / コンプレックス,複合(抑圧されて心に残った複雑なしこり)
2. 『バクテリア』,細菌
3. バクテリアの,細菌の
4. =sense organ / 受信装置

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/06/17 20:23:27」(JST)

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Transferrin
PDB rendering based on 1a8e.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1A8E, 1A8F, 1B3E, 1BP5, 1BTJ, 1D3K, 1D4N, 1DTG, 1FQE, 1FQF, 1JQF, 1N7W, 1N7X, 1N84, 1OQG, 1OQH, 1RYO, 1SUV, 2HAU, 2HAV, 2O7U, 2O84, 3FGS, 3QYT, 3S9L, 3S9M, 3S9N, 3SKP, 3V83, 3V89, 3V8X, 3VE1, 4H0W
Identifiers
Symbols	TF ; PRO1557; PRO2086; TFQTL1
External IDs	OMIM: 190000 MGI: 98821 HomoloGene: 68153 ChEMBL: 4865 GeneCards: TF Gene
Gene ontology Molecular function • protein binding • ferric iron binding • ubiquitin protein ligase binding Cellular component • extracellular region • extracellular space • early endosome • late endosome • coated pit • basal plasma membrane • cell surface • endosome membrane • cytoplasmic membrane-bounded vesicle • apical plasma membrane • endocytic vesicle • secretory granule lumen • basal part of cell • perinuclear region of cytoplasm • recycling endosome • extracellular vesicular exosome • blood microparticle Biological process • retina homeostasis • platelet degranulation • cellular iron ion homeostasis • blood coagulation • platelet activation • transferrin transport • transmembrane transport Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	7018	22041
Ensembl	ENSG00000091513	ENSMUSG00000032554
UniProt	P02787	Q921I1
RefSeq (mRNA)	NM_001063	NM_133977
RefSeq (protein)	NP_001054	NP_598738
Location (UCSC)	Chr 3: 133.46 – 133.5 Mb	Chr 9: 103.2 – 103.23 Mb
PubMed search	[1]	[2]

Transferrin
Identifiers
Symbol	Transferrin
Pfam	PF00405
InterPro	IPR001156
PROSITE	PDOC00182
SCOP	1lcf
SUPERFAMILY	1lcf
OPM superfamily	161
OPM protein	1lfc
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Transferrins are iron-binding blood plasma glycoproteins that control the level of free iron in biological fluids. Human transferrin is encoded by the TF gene.

Transferrin glycoproteins bind iron tightly, but reversibly. Although iron bound to transferrin is less than 0.1% (4 mg) of total body iron, it forms the most vital iron pool with the highest rate of turnover (25 mg/24 h). Transferrin has a molecular weight of around 80 KDa and contains two specific high-affinity Fe(III) binding sites. The affinity of transferrin for Fe(III) is extremely high (10²³ M⁻¹ at pH 7.4) but decreases progressively with decreasing pH below neutrality.

When not bound to iron, transferrin is known as "apotransferrin" (see also apoprotein).

Transport mechanism

When a transferrin protein loaded with iron encounters a transferrin receptor on the surface of a cell (e.g., to erythroid precursors in the bone marrow), it binds to it and, as a consequence, is transported into the cell in a vesicle by receptor-mediated endocytosis. The pH of the vesicle is reduced by hydrogen ion pumps (H+
ATPases) to about 5.5, causing transferrin to release its iron ions. The receptor (with its ligand, transferrin, bound) is then transported through the endocytic cycle back to the cell surface, ready for another round of iron uptake. Each transferrin molecule has the ability to carry two iron ions in the ferric form (Fe3+
).

The gene coding for transferrin in humans is located in chromosome band 3q21.

Medical professionals may check serum transferrin level in iron deficiency and in iron overload disorders such as hemochromatosis.

Structure

In humans, transferrin consists of a polypeptide chain containing 679 amino acids. The protein is composed of alpha helices and beta sheets that form two domains. The N- and C- terminal sequences are represented by globular lobes and between the two lobes is an iron-binding site.

The amino acids which bind the iron ion to the transferrin are identical for both lobes; two tyrosines, one histidine, and one aspartic acid. For the iron ion to bind, an anion is required, preferably carbonate (CO2−
3).

Transferrin also has a transferrin iron-bound receptor; it is a disulfide-linked homodimer. In humans, each monomer consists of 760 amino acids. It enables ligand bonding to the transferrin, as each monomer can bind to one or two molecules of iron. Each monomer consists of three domains: the protease, the helical, and the apical domains. The shape of a transferrin receptor resembles a butterfly based on the intersection of three clearly-shaped domains.

• Transferrin bound to its receptor.

• Transferrin receptor complex.

Tissue distribution

The liver is the main site of transferrin synthesis but other tissues and organs, including the brain, also produce transferrin. The main role of transferrin is to deliver iron from absorption centers in the duodenum and white blood cell macrophages to all tissues. Transferrin plays a key role in areas where erythropoiesis and active cell division occur. The receptor helps maintain iron homeostasis in the cells by controlling iron concentrations.

Immune system

Transferrin also associated with the innate immune system. It is found in the mucosa and binds iron, thus creating an environment low in free iron that impedes bacterial survival in a process called iron withholding. The level of transferrin decreases in inflammation.

Role in disease

An increased plasma transferrin level is often seen in patients suffering from iron deficiency anemia. A decreased plasma transferrin can occur in iron overload diseases and protein malnutrition. An absence of transferrin results from a rare genetic disorder known as atransferrinemia, a condition characterized by anemia and hemosiderosis in the heart and liver that leads to heart failure and many other complications.

Most recently, transferrin and its receptor have been shown to diminish tumour cells when the receptor is used to attract antibodies.

Other effects

The metal-binding properties of transferrin have a great influence on the biochemistry of plutonium in humans.

Carbohydrate deficient transferrin increases in the blood with heavy ethanol consumption and can be monitored through laboratory testing.

Pathology

Atransferrinemia is associated with a deficiency in transferrin.

Reference ranges

An example reference range for transferrin is 204–360 mg/dL. Laboratory test results should always be interpreted using the reference range provided by the laboratory that performed the test.

Reference ranges for blood tests, comparing blood content of transferrin and other iron-related compounds (shown in brown and orange) with other constituents

A high transferrin level may indicate an iron deficiency anemia. Levels of serum iron and total iron binding capacity (TIBC) are used in conjunction with transferrin to specify any abnormality. See interpretation of TIBC.

Interactions

Transferrin has been shown to interact with insulin-like growth factor 2 and IGFBP3. Transcriptional regulation of transferrin is upregulated by retinoic acid.

Related proteins

Members of the family include blood serotransferrin (or siderophilin, usually simply called transferrin); lactotransferrin (lactoferrin); milk transferrin; egg white ovotransferrin (conalbumin); and membrane-associated melanotransferrin.

See also

• Beta-2 transferrin
• Transferrin receptor
• Total iron-binding capacity
• Transferrin saturation
• Ferritin

References

Further reading

• Hershberger CL, Larson JL, Arnold B et al. (1992). "A cloned gene for human transferrin". Annals of the New York Academy of Sciences 646: 140–54. doi:10.1111/j.1749-6632.1991.tb18573.x. PMID 1809186.  CS1 maint: Explicit use of et al. (link)
• Bowman BH, Yang FM, Adrian GS (1989). "Transferrin: evolution and genetic regulation of expression". Adv. Genet. Advances in Genetics 25: 1–38. doi:10.1016/S0065-2660(08)60457-5. ISBN 9780120176250. PMID 3057819. 
• Parkkinen J, von Bonsdorff L, Ebeling F, Sahlstedt L (2003). "Function and therapeutic development of apotransferrin". Vox Sang. 83 (Suppl 1): 321–6. doi:10.1111/j.1423-0410.2002.tb05327.x. PMID 12617162. 

External links

• Transferrin at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

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• 1. 慢性疾患の貧血（慢性炎症時の貧血） anemia of chronic disease anemia of chronic inflammation
• 2. 胎児および新生児における免疫細胞の発達 the development of immune cells in the fetus and neonate
• 3. 関節リウマチの血液学的所見 hematologic manifestations of rheumatoid arthritis
• 4. HIV感染の血液学的症状：貧血 hematologic manifestations of hiv infection anemia
• 5. 乳幼児における鉄欠乏：スクリーニング、予防、臨床症状、および診断 iron deficiency in infants and young children screening prevention clinical manifestations and diagnosis

English Journal

• Modulation of iron transport, metabolism and reactive oxygen status by quercetin-iron complexes in vitro.

• Horniblow RD1, Henesy D1, Iqbal TH1, Tselepis C2.
• Molecular nutrition & food research.Mol Nutr Food Res.2016 Oct 29. doi: 10.1002/mnfr.201600692. [Epub ahead of print]
• SCOPE: Excess free-iron is detrimental to health through its ability to participate in free radical generation and amplification of oncogenic pathways. The study aims were to identify polyphenols with iron-chelating potential.METHODS AND RESULTS: Of four polyphenols tested quercetin demonstrated pot
• PMID 27794191

• The STX6-VTI1B-VAMP3 complex facilitates xenophagy by regulating the fusion between recycling endosomes and autophagosomes.

• Nozawa T1, Minowa-Nozawa A1, Aikawa C1, Nakagawa I1.
• Autophagy.Autophagy.2016 Oct 28:0. [Epub ahead of print]
• Macroautophagy/autophagy plays a critical role in immunity by directly degrading invading pathogens such as Group A Streptococcus (GAS), through a process that has been named xenophagy. We previously demonstrated that autophagic vacuoles directed against GAS, termed GAS-containing autophagosome-like
• PMID 27791468

• Predicting long term cooperativity and specific modulators of receptor interactions in human transferrin from dynamics within a single microstate.

• Abdizadeh H1, Atilgan C1.
• Physical chemistry chemical physics : PCCP.Phys Chem Chem Phys.2016 Mar 21;18(11):7916-26. doi: 10.1039/c5cp05107j.
• Transferrin (Tf) is an essential transport protein circulating iron in the blood and delivering it to tissues. It displays highly pH dependent cooperativity between the two lobes each carrying an iron, and forms a tight complex with the receptor during endocytosis and recycling back to the serum. We
• PMID 26955866

Japanese Journal

• Siderophore-Mediated Utilization of Transferrin- and Lactoferrin-Bound Iron by Acinetobacter baumannii

• Journal of health science 45(6), 297-302, 1999-12-31
• NAID 110003641575

Related Links

• Bacterial Transferrin Receptor Complex | Colorado PROFILES

"Bacterial Transferrin Receptor Complex" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure, which enables

• Bacterial transferrin receptor complex synonyms, Bacterial ...

Synonyms for Bacterial transferrin receptor complex in Free Thesaurus. Antonyms for Bacterial transferrin receptor complex. 2 synonyms for transferrin: beta globulin, siderophilin. What are synonyms for Bacterial transferrin

• What does bacterial transferrin receptor complex mean?

Definition of bacterial transferrin receptor complex in the Definitions.net dictionary. Meaning of bacterial transferrin receptor complex. What does bacterial transferrin receptor complex mean? Information and translations of bacterial ...

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★リンクテーブル★

リンク元	「細菌トランスフェリン受容体複合体」
関連記事	「complex」「bacterial」「complexed」「receptor complex」「complexes」

「細菌トランスフェリン受容体複合体」

　　[★]

英

bacterial transferrin receptor complex

「complex」

　　[★]

• n.

• 複合体、錯体、複合物、合成物、(心理)コンプレックス

• adj.

• 複雑な、複合の

関

complexes、complicated、composite、conjugate、intricate

　 　 　 　 　

「bacterial」

　　[★]

• adj.

• 細菌性の、細菌の、細菌的な

関

bacteria、bacterially、bacterio、bacterium

　 　

「complexed」

　　[★]

• adj.

• 複合型の、混合型の

関

hybrid、mixed lineage、mixed type、mixed-type

「receptor complex」

　　[★]

• 受容体複合体、レセプター複合体

「complexes」

　　[★]

• n.

• 複合体

関

complex、composite