WordNet

a stripe or stripes of contrasting color; "chromosomes exhibit characteristic bands"; "the black and yellow banding of bees and wasps" (同)banding, stria, striation
an adornment consisting of a strip of a contrasting color or material (同)banding, stripe
bind or tie together, as with a band
a driving belt in machinery
a restraint put around something to hold it together
a thin flat strip of flexible material that is worn around the body or one of the limbs (especially to decorate the body)
a thin flat strip or loop of flexible material that goes around or over something else, typically to hold it together or as a decoration
a range of frequencies between two limits
instrumentalists not including string players
100 bani equal 1 leu in Moldova
100 bani equal 1 leu in Romania
prohibit especially by legal means or social pressure; "Smoking is banned in this building"
an official prohibition or edict against something (同)banning, forbiddance, forbidding
forbid the public distribution of ( a movie or a newspaper) (同)censor
any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
marked with bands or strips of contrasting color or texture; "a banded rock"
characterized by a band of especially white around the body; "banded cattle"
identified with a band especially around a leg; "kept watch for the return of their banded birds"

PrepTutorEJDIC

『帯』,『バンド』,ひも,(おけの)たが / (色の)すじ,しま / 周波数 / …‘に'バンドを付ける
(人の)『一隊』,『一団』,一群《+『of』+『名』》 / 『楽隊』,バンド / …'を'一隊(一団)にする / 団結する《+『together』》,(…と)一団になる《+『with』+『名』》
(法による)(…に対する)『禁止』,禁制(prohibition)《+『on』+『名』》 / (世論などの)反対,非難 / (教会の)破門 / (法律や社会的圧力によって)…'を'『禁ずる』,禁止する
蛋白(たんばく)質

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2012/07/25 20:59:01」(JST)

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For the radio frequency range, see Band III.

Anion Exchanger 1 (AE1) or Band 3 is a phylogenetically preserved transport protein responsible for mediating the exchange of chloride (Cl-) for bicarbonate (HCO3-) across a plasma membrane. Functionally similar members of the AE clade are AE2 and AE3.^[1]

It is ubiquitous throughout the vertebrates. In humans it is present in two specific sites:

the erythrocyte (red blood cell) cell membrane and
the basolateral surface of the alpha-intercalated cell (the acid secreting cell type) in the collecting duct of the kidney.

The erythrocyte and kidney forms are different isoforms of the same protein.

Discovery

AE1 was discovered following SDS-PAGE gel electrophoresis of erythrocyte cell membrane. The large 'third' band on the electrophoresis gel represented AE1, which was thus initially termed 'Band 3'. The chloride-bicarbonate exchanger in the red cell membrane is not a pump, which would use metabolic energy. Nor is it strictly an enzyme. It is protein counter-transporter, known as band III.^[2]

AE1 in Red Cells

AE1 is an important structural component of the erythrocyte cell membrane, making up to 25% of the cell membrane surface. Each red cell contains approximately one million copies of AE1.

Function

Here it performs two functions:

Electroneutral chloride and bicarbonate exchange across the plasma membrane on a one-for-one basis.This is crucial for CO₂ uptake by the red cell and conversion (by hydration catalysed by carbonic anhydrase) into a proton and a bicarbonate ion. The bicarbonate is then extruded (in exchange for a chloride) from the cell by the band 3 molecule.

Physical linkage of the plasma membrane to the underlying membrane skeleton (via binding with ankyrin and protein 4.2). This appears to be to prevent membrane surface loss, rather than being to do with membrane skeleton assembly.

Pathology

Mutations of erythroid AE1 affecting the extracellular domains of the molecule may cause alterations in the individual's blood group, as band 3 determines the Diego blood group.

More importantly erythroid AE1 mutations cause between 15-25% of cases of Hereditary spherocytosis (a disorder associated with progressive red cell membrane loss), and also cause the hereditary conditions of Hereditary stomatocytosis ^[3] and Southeast Asian Ovalocytosis ^[4]

AE1 in Alpha-Intercalated cells

A different isoform of AE1, known as kAE1 (which is 65 amino acids shorter than erythroid AE1) is found in the basolateral surface of the alpha-intercalated cell in the cortical collecting duct of the kidney.

Function

This is the principal acid secreting cell of the kidney, which generates hydrogen ions and bicarbonate ions from carbon dioxide and water-a reaction catalysed by Carbonic anhydrase.

The hydrogen ions are pumped into the collecting duct tubule by vacuolar H+ATPase, the apical proton pump,which thus excretes acid into the urine.

kAE1 exchanges bicarbonate for chloride on the basolateral surface, essentially returning bicarbonate to the blood.

Pathology

Mutations of kidney AE1 cause distal (type1) renal tubular acidosis, which is an inability to acidify the urine, even if the blood is too acid. These mutations are disease causing as they cause mistargetting of the mutant band 3 proteins so that they are retained within the cell or occasionally addressed to the wrong (i.e. apical) surface.

Interactions

Band 3 has been shown to interact with Carbonic anhydrase II^[5]^[6]^[7]^[8] and CA4.^[9]

References

^ Alper, S. L. (2009). "Molecular physiology and genetics of Na+-independent SLC4 anion exchangers". Journal of Experimental Biology 212 (11): 1672–1683. DOI:10.1242/jeb.029454. PMC 2683012. PMID 19448077. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2683012. edit
^ Hunter M (1977). "Human erythrocyte anion permeabilities measured under conditions of net charge transfer". J Physiol 268 (1): 35–49. PMC 1283651. PMID 874904. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1283651.
^ LJ Bruce; Robinson, HC; Guizouarn, H; Borgese, F; Harrison, P; King, MJ; Goede, JS; Coles, SE et al. (November 2005). "Monovalent cation leaks in human red cells caused by single amino-acid substitutions in the transport domain of the band 3 chloride-bicarbonate exchanger, AE1". Nature Genetics 37 (11): 1258–63. DOI:10.1038/ng1656. PMID 16227998.
^ Jarolim p; Palek, J; Amato, D; Hassan, K; Sapak, P; Nurse, GT; Rubin, HL; Zhai, S et al. (1991). "Deletion in erythrocyte band 3 gene in malaria-resistant Southeast Asian ovalocytosis". PNAS 88 (24): 11022–11026. Bibcode 1991PNAS...8811022J. DOI:10.1073/pnas.88.24.11022. PMC 53065. PMID 1722314. http://www.pnas.org/cgi/content/abstract/88/24/11022.
^ Sterling, D; Reithmeier R A, Casey J R (Dec. 2001). "A transport metabolon. Functional interaction of carbonic anhydrase II and chloride/bicarbonate exchangers". J. Biol. Chem. (United States) 276 (51): 47886–94. DOI:10.1074/jbc.M105959200. ISSN 0021-9258. PMID 11606574.
^ Vince, J W; Reithmeier R A (October 1998). "Carbonic anhydrase II binds to the carboxyl terminus of human band 3, the erythrocyte C1-/HCO3- exchanger". J. Biol. Chem. (UNITED STATES) 273 (43): 28430–7. DOI:10.1074/jbc.273.43.28430. ISSN 0021-9258. PMID 9774471.
^ Vince, J W; Carlsson U, Reithmeier R A (November 2000). "Localization of the Cl-/HCO3- anion exchanger binding site to the amino-terminal region of carbonic anhydrase II". Biochemistry (UNITED STATES) 39 (44): 13344–9. DOI:10.1021/bi0015111. ISSN 0006-2960. PMID 11063570.
^ Vince, J W; Reithmeier R A (May 2000). "Identification of the carbonic anhydrase II binding site in the Cl(-)/HCO(3)(-) anion exchanger AE1". Biochemistry (UNITED STATES) 39 (18): 5527–33. DOI:10.1021/bi992564p. ISSN 0006-2960. PMID 10820026.
^ Sterling, Deborah; Alvarez Bernardo V, Casey Joseph R (July 2002). "The extracellular component of a transport metabolon. Extracellular loop 4 of the human AE1 Cl-/HCO3- exchanger binds carbonic anhydrase IV". J. Biol. Chem. (United States) 277 (28): 25239–46. DOI:10.1074/jbc.M202562200. ISSN 0021-9258. PMID 11994299.

External links

Diego blood group system at BGMUT Blood Group Antigen Gene Mutation Database at NCBI, NIH
Band+3+Protein at the US National Library of Medicine Medical Subject Headings (MeSH)
Chloride-Bicarbonate+Antiporters at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

1. 遺伝性球状赤血球症：溶血の機序および原因 hereditary spherocytosis mechanism of hemolysis and pathogenesis
2. 赤血球水分量の制御 control of red blood cell hydration
3. 赤血球細胞膜の動態および機構 red blood cell membrane dynamics and organization
4. 遺伝性楕円赤血球症：遺伝学と病因 hereditary elliptocytosis genetics and pathogenesis
5. Overview and pathophysiology of renal tubular acidosis and the effect on potassium balance

English Journal

Antiepileptic carbamazepine drug treatment induces alteration of membrane in red blood cells: Possible positive effects on metabolism and oxidative stress.

Ficarra S, Misiti F, Russo A, Carelli-Alinovi C, Bellocco E, Barreca D, Laganà G, Leuzzi U, Toscano G, Giardina B, Galtieri A, Tellone E.SourceDepartment of Chemical Sciences, University of Messina, Viale Ferdinando Stagno d'Alcontres 31, 98166 Messina, Italy. Electronic address: sficarra@unime.it.
Biochimie.Biochimie.2013 Apr;95(4):833-41. doi: 10.1016/j.biochi.2012.11.018. Epub 2012 Dec 12.
Carbamazepine (CBZ) is an iminostilbene derivative commonly used for treatment of neuralgic pain and bipolar affective disorders. CBZ blood levels of treated patients are within the range of micromolar concentrations and therefore, significant interactions of this drug with erythrocytes are very lik
PMID 23246915

Sickle hemoglobin disturbs normal coupling among erythrocyte O2 content, glycolysis, and antioxidant capacity.

Rogers SC, Ross JG, d'Avignon A, Gibbons LB, Gazit V, Hassan MN, McLaughlin D, Griffin S, Neumayr T, Debaun M, Debaun MR, Doctor A.SourceDivision of Critical Care Medicine, Department of Pediatrics, School of Medicine.
Blood.Blood.2013 Feb 28;121(9):1651-62. doi: 10.1182/blood-2012-02-414037. Epub 2013 Jan 7.
Key Points Hb-conformation-dependent interaction with band 3 protein regulates glycolysis in RBCs. In hypoxia, HbS disrupts this system, disabling RBC antioxidant defense.
PMID 23297128

Hereditary spherocytosis due to band 3 deficiency: 15 novel mutations in SLC4A1.

Van Zwieten R, François JJ, Van Leeuwen K, Van Wesel AC, Van Bruggen R, Van Solinge WW, Roos D, Verhoeven AJ, Van Wijk R.
American journal of hematology.Am J Hematol.2013 Feb;88(2):159-60. doi: 10.1002/ajh.23363. Epub 2012 Dec 17.
PMID 23255290

Japanese Journal

Purification and biochemical characterization of a cellulase from the digestive organs of the short-spined sea urchin Strongylocentrotus intermedius

Hasegawa Syuto,Ura Kazuhiro,Tanaka Hiroyuki [他]
Fisheries Science 78(5), 1107-1115, 2012-09
… The isolated cellulase was stained as a single band by Congo red. …
NAID 40019415751

A thiol-mediated active membrane transport of selenium by erythroid anion exchanger 1 protein

Hongoh Masafumi,Haratake Mamoru,Fuchigami Takeshi,Nakayama Morio
Dalton Transactions 41(24), 7340-7349, 2012-06-28
… In this paper, we describe a thiol-mediated and energy-dependent membrane transport of selenium by erythroid anion exchanger 1 (AE1, also known as band 3 protein). … The AE1 is the most abundant integral protein of red cell membranes and plays a critical role in the carbon dioxide transport system in which carbon dioxide is carried as bicarbonate in the plasma. …
NAID 120004754248

Related Pictures

★リンクテーブル★

リンク元	「バンド3タンパク質」「erythrocyte anion exchange protein 1」「バンド3蛋白」
関連記事	「band」「ban」「banding」

「バンド3タンパク質」

solute carrier family 4 (anion exchanger), member 1, adapter protein
Identifiers
Symbol	SLC4A1AP
Entrez	22950
HUGO	13813
OMIM	602655
RefSeq	NM_018158
UniProt	Q9BWU0
Other data
Locus	Chr. 2 p23.3

Solute carrier family 4, anion exchanger, member 1 (erythrocyte membrane protein band 3, Diego blood group)
	; Atomic microscope image of Band 3
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1BH7, 1BNX, 1BTQ, 1BTR, 1BTS, 1BTT, 1BZK, 1HYN, 2BTA, 2BTB, 3BTB
Identifiers
Symbols	SLC4A1; AE1; BND3; CD233; DI; EMPB3; EPB3; FR; RTA1A; SW; WD; WD1; WR
External IDs	OMIM: 109270 MGI: 109393 HomoloGene: 37290 GeneCards: SLC4A1 Gene
Gene Ontology
Molecular function	• actin binding; • inorganic anion exchanger activity; • protein binding; • protein C-terminus binding; • anion transmembrane transporter activity; • chloride transmembrane transporter activity; • anion:anion antiporter activity; • ankyrin binding; • protein homodimerization activity; • protein anchor;
Cellular component	• plasma membrane; • integral to plasma membrane; • integral to membrane; • basolateral plasma membrane; • Z disc; • cortical cytoskeleton;
Biological process	• ion transport; • anion transport; • chloride transport; • cellular ion homeostasis; • bicarbonate transport; • transmembrane transport;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	This box: view; talk; edit;