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{{PBB_Controls
{{for|the radio frequency range|Band III}}
| update_page = yes
{{Infobox_gene}}
| require_manual_inspection = no
{{infobox protein
| update_protein_box = yes
| Name = solute carrier family 4 (anion exchanger), member 1, adapter protein
| update_summary = no
| caption =
| update_citations = yes
| image = Alpha_Intercalated_Cell_Cartoon.svg
}}
{{GNF_Protein_box
| image = Band_3_Atomic_microscope.jpg
| image_source = Atomic microscope image of Band 3
| Name = Solute carrier family 4, anion exchanger, member 1 (erythrocyte membrane protein band 3, Diego blood group)
| HGNCid = 11027
| Symbol = SLC4A1
| AltSymbols =; WD; AE1; BND3; CD233; DI; EMPB3; EPB3; FR; MGC116750; MGC116753; MGC126619; MGC126623; RTA1A; SW; WD1; WR
| OMIM = 109270
| ECnumber = 
| Homologene = 37290
| MGIid = 109393
| GeneAtlas_image1 = PBB_GE_SLC4A1_205592_at_tn.png
| Function = {{GNF_GO|id=GO:0005452 |text = inorganic anion exchanger activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008509 |text = anion transmembrane transporter activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0030863 |text = cortical cytoskeleton}}
| Process = {{GNF_GO|id=GO:0006820 |text = anion transport}} {{GNF_GO|id=GO:0006873 |text = cell ion homeostasis}}  
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6521
    | Hs_Ensembl = ENSG00000004939
    | Hs_RefseqProtein = NP_000333
    | Hs_RefseqmRNA = NM_000342
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 39682566
    | Hs_GenLoc_end = 39700993
    | Hs_Uniprot = P02730
    | Mm_EntrezGene = 20533
    | Mm_Ensembl = ENSMUSG00000006574
    | Mm_RefseqmRNA = NM_011403
    | Mm_RefseqProtein = NP_035533
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 102164917
    | Mm_GenLoc_end = 102181211
    | Mm_Uniprot = Q3TA19
  }}
}}
{{protein
| Name = solute carrier family 4 (anion exchanger), member 1, adaptor protein
| caption =  
| image = Alpha_Intercalated_Cell_Cartoon.jpg
| width = 250px
| width = 250px
| HGNCid = 13813
| HGNCid = 13813
| Symbol = SLC4A1AP
| Symbol = SLC4A1AP
| AltSymbols =  
| AltSymbols =
| EntrezGene = 22950
| EntrezGene = 22950
| OMIM = 602655
| OMIM = 602655
| RefSeq = NM_018158
| RefSeq = NM_018158
| UniProt = Q9BWU0
| UniProt = P02730
| PDB =  
| PDB =
| ECnumber =  
| ECnumber =
| Chromosome = 2
| Chromosome = 2
| Arm = p
| Arm = p
| Band = 23.3
| Band = 23.3
| LocusSupplementaryData =  
| LocusSupplementaryData =
}}
}}
{{SI}}
{{CMG}}
__NOTOC__


'''Band 3 anion transport protein''', also known as '''anion exchanger 1''' ('''AE1''') or '''band 3'''  or '''solute carrier family 4 member 1''' (SLC4A1), is a [[protein]] that is encoded by the ''SLC4A1'' [[gene]] in humans.


==Overview==
Band 3 anion transport protein is a [[phylogenetically]]-preserved [[Membrane transport protein|transport protein]] responsible for mediating the [[Active transport#Antiport|exchange]] of [[chloride]] (Cl<sup>−</sup>) with [[bicarbonate]] (HCO<sub>3</sub><sup>−</sup>) across [[plasma membrane]]s. Functionally similar members of the AE clade are [[SLC4A2|AE2]] and [[SLC4A3|AE3]].<ref>{{cite journal | vauthors = Alper SL | title = Molecular physiology and genetics of Na+-independent SLC4 anion exchangers | journal = Journal of Experimental Biology | volume = 212 | issue = 11 | pages = 1672–1683 | year = 2009 | pmid = 19448077 | pmc = 2683012 | doi = 10.1242/jeb.029454 }}</ref>


'''Anion Exchanger 1''' ('''AE1''') or '''Band 3''' is a [[phylogenetically]] preserved [[transport protein]] responsible for [[catalysing]] the electroneutral exchange of [[chloride]] (Cl-) for [[bicarbonate]] (HCO3-) across a [[plasma membrane]].  
== Function ==
Band 3 is present in the basolateral face of the [[Collecting duct system|α-intercalated cells]] of the collecting ducts of the nephron, which are the main acid-secreting cells of the kidney. They generate [[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 [[V-ATPase|vacuolar H<sup>+</sup> 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. Here it performs two functions:


It is ubiquitous throughout the [[vertebrates]]. In [[humans]] it is present in two specific sites:
* Electroneutral chloride and bicarbonate exchange across the plasma membrane on a one-for-one basis. This is crucial for CO<sub>2</sub> uptake by the red blood cell and conversion (by hydration catalysed by [[carbonic anhydrase]]) into a [[proton]] and a [[bicarbonate]] ion. The bicarbonate is then excreted (in exchange for a chloride) from the cell by band 3.
* the [[erythrocyte]] (red blood cell) cell membrane and
* 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 having to do with membrane skeleton assembly.
* 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]].
== Distribution ==
It is ubiquitous throughout the [[vertebrates]]. In [[mammals]], 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]].


==Discovery==
== Gene products ==
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 erythrocyte and kidney forms are different [[isoforms]] of the same [[protein]].<ref name="pmid3461480">{{cite journal | vauthors = Schlüter K, Drenckhahn D | title = Co-clustering of denatured hemoglobin with band 3: its role in binding of autoantibodies against band 3 to abnormal and aged erythrocytes | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 83 | issue = 16 | pages = 6137–41 | date = August 1986 | pmid = 3461480 | pmc = 386454 | doi = 10.1073/pnas.83.16.6137 | bibcode = 1986PNAS...83.6137S }}</ref>
The chloride-bicarbonate exchanger in the red cell membrane is not a [[Ion pump (biology)|pump]], which would use metabolic energy. Nor is it strictly an [[enzyme]]. It is protein [[counter-transporter]], known as band III. <ref>{{cite journal | author = Hunter M | title = Human erythrocyte anion permeabilities measured under conditions of net charge transfer. | journal = J Physiol | volume = 268 | issue = 1 | pages = 35-49 | year = 1977 | id = PMID 874904}}</ref>


==AE1 in Red Cells==
The erythrocyte isoform of AE1, known as eAE1, is composed of 911 amino acids. eAE1 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 eAE1.
AE1 is an important structural component of the erythrocyte cell membrane, making up to 25% of the cell membrane surface, indeed each red cell contains approximately one million copies of AE1.


===Function===
The kidney isoform of AE1, known as kAE1 (which is 65 amino acids shorter than erythroid AE1) is found in the [[basolateral]] membrane of alpha-intercalated cells in the [[cortical collecting duct]] of the kidney.
Here it performs two functions:


* Electroneutral chloride and bicarbonate exchange across the plasma membrane on a one-for-one basis.This is crucial for CO<sub>2</sub> 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 from the cell by the band 3 molecule.
== Clinical significance ==
Mutations of kidney AE1 cause distal (type 1) [[renal tubular acidosis]], which is an inability to acidify the urine, even if the blood is too [[acidic]]. 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.


* 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.
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 antigen system|Diego]] [[Human blood group systems|blood group]].


===Pathology===
More importantly erythroid AE1 mutations cause 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]]<ref name="pmid16227998">{{cite journal | vauthors = Bruce LJ, Robinson HC, Guizouarn H, Borgese F, Harrison P, King MJ, Goede JS, Coles SE, Gore DM, Lutz HU, Ficarella R, Layton DM, Iolascon A, Ellory JC, Stewart GW | title = 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 | journal = Nat. Genet. | volume = 37 | issue = 11 | pages = 1258–63 | year = 2005 | pmid = 16227998 | doi = 10.1038/ng1656 }}</ref> and Southeast Asian [[Ovalocytosis]]<ref name="pmid1722314">{{cite journal | vauthors = Jarolim P, Palek J, Amato D, Hassan K, Sapak P, Nurse GT, Rubin HL, Zhai S, Sahr KE, Liu SC | title = Deletion in erythrocyte band 3 gene in malaria-resistant Southeast Asian ovalocytosis | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 88 | issue = 24 | pages = 11022–6 | year = 1991 | pmid = 1722314 | pmc = 53065 | doi = 10.1073/pnas.88.24.11022 | bibcode = 1991PNAS...8811022J }}</ref>
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]] <ref>{{cite journal
== Interactions ==
| quotes =  
Band 3 has been shown to [[Protein-protein interaction|interact]] with [[Carbonic anhydrase II|CA2]]<ref name = pmid11606574>{{cite journal | vauthors = Sterling D, Reithmeier RA, Casey JR | title = A transport metabolon. Functional interaction of carbonic anhydrase II and chloride/bicarbonate exchangers | journal = J. Biol. Chem. | volume = 276 | issue = 51 | pages = 47886–94 | date = Dec 2001 | pmid = 11606574 | doi = 10.1074/jbc.M105959200 }}</ref><ref name = pmid9774471>{{cite journal | vauthors = Vince JW, Reithmeier RA | title = Carbonic anhydrase II binds to the carboxyl terminus of human band 3, the erythrocyte C1-/HCO3- exchanger | journal = J. Biol. Chem. | volume = 273 | issue = 43 | pages = 28430–7 | date = October 1998 | pmid = 9774471 | doi = 10.1074/jbc.273.43.28430 }}</ref><ref name = pmid11063570>{{cite journal | vauthors = Vince JW, Carlsson U, Reithmeier RA | title = Localization of the Cl-/HCO3- anion exchanger binding site to the amino-terminal region of carbonic anhydrase II | journal = Biochemistry | volume = 39 | issue = 44 | pages = 13344–9 | date = November 2000 | pmid = 11063570 | doi = 10.1021/bi0015111 }}</ref><ref name = pmid10820026>{{cite journal | vauthors = Vince JW, Reithmeier RA | title = Identification of the carbonic anhydrase II binding site in the Cl(-)/HCO(3)(-) anion exchanger AE1 | journal = Biochemistry | volume = 39 | issue = 18 | pages = 5527–33 | date = May 2000 | pmid = 10820026 | doi = 10.1021/bi992564p }}</ref> and [[Carbonic anhydrase 4|CA4]].<ref name = pmid11994299>{{cite journal | vauthors = Sterling D, Alvarez BV, Casey JR | title = The extracellular component of a transport metabolon. Extracellular loop 4 of the human AE1 Cl-/HCO3- exchanger binds carbonic anhydrase IV | journal = J. Biol. Chem. | volume = 277 | issue = 28 | pages = 25239–46 | date = July 2002 | pmid = 11994299 | doi = 10.1074/jbc.M202562200 }}</ref>
| author = LJ Bruce
| date =  
| year = 2005
| month = Nov
| title = 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.
| journal = Nature Genetics
| volume = 37
| issue = 11
| pages = 1258-63
| doi =  
| id =  
| url = http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=16227998&dopt=Abstract
| format =  
| accessdate =  
}} </ref> and Southeast Asian [[Ovalocytosis]] <ref>{{cite journal
| quotes =  
| author = Jarolim p
| date =
| year = 1991
| month =
| title = Deletion in Erythrocyte Band 3 Gene in Malaria-Resistant Southeast Asian Ovalocytosis
| journal = PNAS
| volume = 88
| issue =  
| pages = 11022-11026
| doi =  
| id =  
| url = http://www.pnas.org/cgi/content/abstract/88/24/11022
| format =
| accessdate =
}}. </ref>
==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===
== Discovery ==
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]].  
AE1 was discovered following [[SDS-PAGE]] ( sodium dodecyl sulfate polyacrylamide gel electrophoresis ) of erythrocyte [[cell membrane]]. The large 'third' band on the electrophoresis gel represented AE1, which was thus initially termed 'Band 3'.


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]].
== See also ==
* [[Cluster of differentiation]]
* [[Anion exchanger family]]


kAE1 exchanges bicarbonate for chloride on the basolateral surface, essentially returning bicarbonate to the blood.
== References ==
{{reflist|30em}}


===Pathology===
== Further reading ==
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]].
{{Refbegin | 2}}
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 (ie apical) surface.
* {{cite journal | vauthors = Tanner MJ | title = Molecular and cellular biology of the erythrocyte anion exchanger (AE1) | journal = Semin. Hematol. | volume = 30 | issue = 1 | pages = 34–57 | year = 1993 | pmid = 8434259 | doi =  }}
* {{cite journal | vauthors = Chambers EJ, Askin D, Bloomberg GB, Ring SM, Tanner MJ | title = Studies on the structure of a transmembrane region and a cytoplasmic loop of the human red cell anion exchanger (band 3, AE1) | journal = Biochem. Soc. Trans. | volume = 26 | issue = 3 | pages = 516–20 | year = 1998 | pmid = 9765907 | doi = }}
* {{cite journal | vauthors = Inaba M | title = [Band 3: expanding knowledge on its functions] | journal = Seikagaku | volume = 73 | issue = 12 | pages = 1431–5 | year = 2002 | pmid = 11831035 | doi =  }}
* {{cite journal | vauthors = Tanner MJ | title = Band 3 anion exchanger and its involvement in erythrocyte and kidney disorders | journal = Curr. Opin. Hematol. | volume = 9 | issue = 2 | pages = 133–9 | year = 2002 | pmid = 11844997 | doi = 10.1097/00062752-200203000-00009 }}
* {{cite journal | vauthors = Shayakul C, Alper SL | title = Defects in processing and trafficking of the AE1 Cl<sup>−</sup>/HCO<sub>3</sub><sup>−</sup> exchanger associated with inherited distal renal tubular acidosis | journal = Clin. Exp. Nephrol. | volume = 8 | issue = 1 | pages = 1–11 | year = 2004 | pmid = 15067510 | doi = 10.1007/s10157-003-0271-x }}
{{Refend}}


==See also==
== External links ==
* [[Cluster of differentiation]]
* [https://www.ncbi.nlm.nih.gov/projects/mhc/xslcgi.fcgi?cmd=bgmut/systems_info&system=diego Diego blood group system] at [[BGMUT]] Blood Group Antigen Gene Mutation Database at [[National Center for Biotechnology Information|NCBI]], [[NIH]]
 
==References==
{{Reflist|2}}
 
==External links==
* [http://www.ncbi.nlm.nih.gov/projects/mhc/xslcgi.fcgi?cmd=bgmut/systems_info&system=diego Diego blood group system at BGMUT] Blood Group Antigen Gene Mutation Database at [[NCBI]], [[NIH]]
* {{MeshName|Band+3+Protein}}
* {{MeshName|Band+3+Protein}}
* {{MeshName|Chloride-Bicarbonate+Antiporters}}
* {{MeshName|Chloride-Bicarbonate+Antiporters}}
* {{UCSC gene info|SLC4A1}}


==Further reading==
{{PDB Gallery|geneid=6521}}
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Tanner MJ |title=Molecular and cellular biology of the erythrocyte anion exchanger (AE1). |journal=Semin. Hematol. |volume=30 |issue= 1 |pages= 34-57 |year= 1993 |pmid= 8434259 |doi=  }}
*{{cite journal  | author=Chambers EJ, Askin D, Bloomberg GB, ''et al.'' |title=Studies on the structure of a transmembrane region and a cytoplasmic loop of the human red cell anion exchanger (band 3, AE1). |journal=Biochem. Soc. Trans. |volume=26 |issue= 3 |pages= 516-20 |year= 1998 |pmid= 9765907 |doi=  }}
*{{cite journal  | author=Inaba M |title=[Band 3: expanding knowledge on its functions] |journal=Seikagaku |volume=73 |issue= 12 |pages= 1431-5 |year= 2002 |pmid= 11831035 |doi=  }}
*{{cite journal  | author=Tanner MJ |title=Band 3 anion exchanger and its involvement in erythrocyte and kidney disorders. |journal=Curr. Opin. Hematol. |volume=9 |issue= 2 |pages= 133-9 |year= 2002 |pmid= 11844997 |doi=  }}
*{{cite journal  | author=Shayakul C, Alper SL |title=Defects in processing and trafficking of the AE1 Cl-/HCO3- exchanger associated with inherited distal renal tubular acidosis. |journal=Clin. Exp. Nephrol. |volume=8 |issue= 1 |pages= 1-11 |year= 2004 |pmid= 15067510 |doi= 10.1007/s10157-003-0271-x }}
}}
{{refend}}
<br>


{{Clusters of differentiation}}
{{Clusters of differentiation}}
{{Ion pumps}}
{{Ion pumps}}
{{Membrane transport proteins}}
{{Solute carrier family|bg|bg0}}


[[Category:Blood]]
[[Category:Blood proteins]]
[[Category:Blood antigen systems]]
[[Category:Blood antigen systems]]
[[Category:Catalysts]]
[[Category:Enzymes]]
[[Category:Clusters of differentiation]]
[[Category:Clusters of differentiation]]
[[Category:Hematology]]
[[Category:Solute carrier family]]
[[Category:Solute carrier family]]
[[Category:Transfusion medicine]]
[[Category:Transfusion medicine]]
{{WH}}
{{WikiDoc Sources}}

Latest revision as of 10:33, 22 September 2018

For the radio frequency range, see Band III.
VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human
solute carrier family 4 (anion exchanger), member 1, adapter protein
Error creating thumbnail: File missing
Identifiers
SymbolSLC4A1AP
Entrez22950
HUGO13813
OMIM602655
RefSeqNM_018158
UniProtP02730
Other data
LocusChr. 2 p23.3

Band 3 anion transport protein, also known as anion exchanger 1 (AE1) or band 3 or solute carrier family 4 member 1 (SLC4A1), is a protein that is encoded by the SLC4A1 gene in humans.

Band 3 anion transport protein is a phylogenetically-preserved transport protein responsible for mediating the exchange of chloride (Cl−) with bicarbonate (HCO3−) across plasma membranes. Functionally similar members of the AE clade are AE2 and AE3.[1]

Function

Band 3 is present in the basolateral face of the α-intercalated cells of the collecting ducts of the nephron, which are the main acid-secreting cells of the kidney. They generate 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. 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 blood cell and conversion (by hydration catalysed by carbonic anhydrase) into a proton and a bicarbonate ion. The bicarbonate is then excreted (in exchange for a chloride) from the cell by band 3.
  • 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 having to do with membrane skeleton assembly.

Distribution

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

Gene products

The erythrocyte and kidney forms are different isoforms of the same protein.[2]

The erythrocyte isoform of AE1, known as eAE1, is composed of 911 amino acids. eAE1 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 eAE1.

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

Clinical significance

Mutations of kidney AE1 cause distal (type 1) renal tubular acidosis, which is an inability to acidify the urine, even if the blood is too acidic. 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.

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 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]

Interactions

Band 3 has been shown to interact with CA2[5][6][7][8] and CA4.[9]

Discovery

AE1 was discovered following SDS-PAGE ( sodium dodecyl sulfate polyacrylamide gel electrophoresis ) of erythrocyte cell membrane. The large 'third' band on the electrophoresis gel represented AE1, which was thus initially termed 'Band 3'.

See also

References

  1. ↑ Alper SL (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.
  2. ↑ Schlüter K, Drenckhahn D (August 1986). "Co-clustering of denatured hemoglobin with band 3: its role in binding of autoantibodies against band 3 to abnormal and aged erythrocytes". Proc. Natl. Acad. Sci. U.S.A. 83 (16): 6137–41. Bibcode:1986PNAS...83.6137S. doi:10.1073/pnas.83.16.6137. PMC 386454. PMID 3461480.
  3. ↑ Bruce LJ, Robinson HC, Guizouarn H, Borgese F, Harrison P, King MJ, Goede JS, Coles SE, Gore DM, Lutz HU, Ficarella R, Layton DM, Iolascon A, Ellory JC, Stewart GW (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". Nat. Genet. 37 (11): 1258–63. doi:10.1038/ng1656. PMID 16227998.
  4. ↑ Jarolim P, Palek J, Amato D, Hassan K, Sapak P, Nurse GT, Rubin HL, Zhai S, Sahr KE, Liu SC (1991). "Deletion in erythrocyte band 3 gene in malaria-resistant Southeast Asian ovalocytosis". Proc. Natl. Acad. Sci. U.S.A. 88 (24): 11022–6. Bibcode:1991PNAS...8811022J. doi:10.1073/pnas.88.24.11022. PMC 53065. PMID 1722314.
  5. ↑ Sterling D, Reithmeier RA, Casey JR (Dec 2001). "A transport metabolon. Functional interaction of carbonic anhydrase II and chloride/bicarbonate exchangers". J. Biol. Chem. 276 (51): 47886–94. doi:10.1074/jbc.M105959200. PMID 11606574.
  6. ↑ Vince JW, Reithmeier RA (October 1998). "Carbonic anhydrase II binds to the carboxyl terminus of human band 3, the erythrocyte C1-/HCO3- exchanger". J. Biol. Chem. 273 (43): 28430–7. doi:10.1074/jbc.273.43.28430. PMID 9774471.
  7. ↑ Vince JW, Carlsson U, Reithmeier RA (November 2000). "Localization of the Cl-/HCO3- anion exchanger binding site to the amino-terminal region of carbonic anhydrase II". Biochemistry. 39 (44): 13344–9. doi:10.1021/bi0015111. PMID 11063570.
  8. ↑ Vince JW, Reithmeier RA (May 2000). "Identification of the carbonic anhydrase II binding site in the Cl(-)/HCO(3)(-) anion exchanger AE1". Biochemistry. 39 (18): 5527–33. doi:10.1021/bi992564p. PMID 10820026.
  9. ↑ Sterling D, Alvarez BV, Casey JR (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. 277 (28): 25239–46. doi:10.1074/jbc.M202562200. PMID 11994299.

Further reading

  • Tanner MJ (1993). "Molecular and cellular biology of the erythrocyte anion exchanger (AE1)". Semin. Hematol. 30 (1): 34–57. PMID 8434259.
  • Chambers EJ, Askin D, Bloomberg GB, Ring SM, Tanner MJ (1998). "Studies on the structure of a transmembrane region and a cytoplasmic loop of the human red cell anion exchanger (band 3, AE1)". Biochem. Soc. Trans. 26 (3): 516–20. PMID 9765907.
  • Inaba M (2002). "[Band 3: expanding knowledge on its functions]". Seikagaku. 73 (12): 1431–5. PMID 11831035.
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External links

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