ITGAE

ITGAE
Identifiers
Aliases	ITGAE, CD103, HUMINAE, integrin subunit alpha E
External IDs	OMIM: 604682; MGI: 1298377; HomoloGene: 113560; GeneCards: ITGAE; OMA:ITGAE - orthologs
Gene location (Human)
Chr.	Chromosome 17 (human)
End	3,801,188 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	73,038,272 bp
RNA expression pattern
	Top expressed in
	oocyte; ; secondary oocyte; ; glutes; ; muscle of arm; ; biceps brachii; ; putamen; ; triceps brachii muscle; ; caudate nucleus; ; monocyte; ; lymph node;
	Top expressed in
	seminiferous tubule; ; spermatid; ; spermatocyte; ; mesenteric lymph nodes; ; Paneth cell; ; lumbar subsegment of spinal cord; ; blood; ; jejunum; ; thymus; ; duodenum;
	More reference expression data
	n/a
Gene ontology
Molecular function	metal ion binding;
Cellular component	integral component of membrane; integrin complex; plasma membrane; external side of plasma membrane; membrane;
Biological process	integrin-mediated signaling pathway; cell adhesion; extracellular matrix organization;
	Sources:Amigo / QuickGO
Orthologs
	3682
	16407
	ENSG00000083457
	ENSMUSG00000005947
	P38570
	Q60677
	NM_002208
	NM_008399; NM_172944; NM_001361245
	NP_002199
	NP_032425; NP_001348174
	Wikidata
View/Edit Human	View/Edit Mouse

Integrin, alpha E (ITGAE) also known as CD103 (cluster of differentiation 103) is an integrin protein that in human is encoded by the ITGAE gene.^[5]^[6] CD103 binds integrin beta 7 (β7– ITGB7) to form the complete heterodimeric integrin molecule αEβ7, which has no distinct name. The αEβ7 complex is often referred to as "CD103" though this strictly refers only to the αE chain. Note that the β7 subunit can bind with other integrin α chains, such as α4 (CD49d).

Tissue distribution

CD103 is expressed widely on intraepithelial lymphocyte (IEL) T cells (both αβ T cells and γδ T cells) and on some peripheral regulatory T cells (Tregs).^[7] It has also been reported on lamina propria T cells.^[8] A subset of dendritic cells in the gut mucosa and mesenteric lymph nodes, known as CD103 dendritic cells, also expresses this marker.^[9]

It is useful in identifying hairy cell leukemia which is positive for this marker in contrast to most other hematologic malignancies which are negative for CD103 except for hairy cell leukemia variant, a fraction of splenic marginal zone lymphomas, and enteropathy-associated T cell lymphoma.^[10]

Function

The chief ligand for αEβ7 is E-cadherin, a cellular adhesion molecule (CAM) found on epithelial cells.^[11] It is probably important for T cell homing to the intestinal sites^[12] and thymocyte contacts with thymic reticuloepithelial cells.^[13]

Tregs are important for decreasing the immune response and appear to play a crucial role in the prevention of autoimmune diseases. Tregs are defined as CD4⁺/CD25⁺/Foxp3⁺ cells.^[14] Some CD4⁺/FoxP3⁻ cells also express CD103 and have been attributed regulatory activity. It is unclear whether the presence of CD103 on Treg cells represents a specialized feature for Treg, or Treg differentiation of IEL T cells.

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000083457 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000005947 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Kilshaw PJ, Higgins JM (October 2002). "Alpha E: no more rejection?". The Journal of Experimental Medicine. 196 (7): 873–875. doi:10.1084/jem.20021404. PMC 2194032. PMID 12370249.
^ "Entrez Gene: integrin".
^ Lehmann J, Huehn J, de la Rosa M, Maszyna F, Kretschmer U, Krenn V, et al. (October 2002). "Expression of the integrin alpha Ebeta 7 identifies unique subsets of CD25+ as well as CD25- regulatory T cells". Proceedings of the National Academy of Sciences of the United States of America. 99 (20): 13031–13036. Bibcode:2002PNAS...9913031L. doi:10.1073/pnas.192162899. PMC 130581. PMID 12242333.
^ Aziz S, Fackler OT, Meyerhans A, Müller-Lantzsch N, Zeitz M, Schneider T (January 2005). "Replication of M-tropic HIV-1 in activated human intestinal lamina propria lymphocytes is the main reason for increased virus load in the intestinal mucosa". Journal of Acquired Immune Deficiency Syndromes. 38 (1): 23–30. doi:10.1097/00126334-200501010-00005. PMID 15608520. S2CID 22884381.
^ Johansson-Lindbom B, Svensson M, Pabst O, Palmqvist C, Marquez G, Förster R, et al. (October 2005). "Functional specialization of gut CD103+ dendritic cells in the regulation of tissue-selective T cell homing". The Journal of Experimental Medicine. 202 (8): 1063–1073. doi:10.1084/jem.20051100. PMC 2213212. PMID 16216890.
^ Swerdlow SH, Campo E, Harris NL, Jaffe ES, Pileri SA, Stein H, et al. (2008). WHO Classification of Tumours of Haematopoietic and Lymphoid Tissues (World Health Organization Classification of Tumours) (4th ed.). Geneva: World Health Organization. ISBN 978-92-832-2431-0.
^ Hadley GA, Bartlett ST, Via CS, Rostapshova EA, Moainie S (October 1997). "The epithelial cell-specific integrin, CD103 (alpha E integrin), defines a novel subset of alloreactive CD8+ CTL". Journal of Immunology. 159 (8): 3748–3756. doi:10.4049/jimmunol.159.8.3748. PMID 9378961.
^ Agace WW, Higgins JM, Sadasivan B, Brenner MB, Parker CM (October 2000). "T-lymphocyte-epithelial-cell interactions: integrin alpha(E)(CD103)beta(7), LEEP-CAM and chemokines". Current Opinion in Cell Biology. 12 (5): 563–568. doi:10.1016/S0955-0674(00)00132-0. PMID 10978890.
^ Kutlesa S, Wessels JT, Speiser A, Steiert I, Müller CA, Klein G (December 2002). "E-cadherin-mediated interactions of thymic epithelial cells with CD103+ thymocytes lead to enhanced thymocyte cell proliferation". Journal of Cell Science. 115 (Pt 23): 4505–4515. doi:10.1242/jcs.00142. PMID 12414996. S2CID 14571087.
^ Allakhverdi Z, Fitzpatrick D, Boisvert A, Baba N, Bouguermouh S, Sarfati M, et al. (December 2006). "Expression of CD103 identifies human regulatory T-cell subsets". The Journal of Allergy and Clinical Immunology. 118 (6): 1342–1349. doi:10.1016/j.jaci.2006.07.034. PMID 17137867.

External links

ITGAE+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
"ITGAE Orthologs". Cell Migration Consortium. Archived from the original on 2014-12-11.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000083457 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000005947 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid12370249-5] Kilshaw PJ, Higgins JM (October 2002). "Alpha E: no more rejection?". The Journal of Experimental Medicine. 196 (7): 873–875. doi:10.1084/jem.20021404. PMC 2194032. PMID 12370249.

[entrez-6] "Entrez Gene: integrin".

[pmid12242333-7] Lehmann J, Huehn J, de la Rosa M, Maszyna F, Kretschmer U, Krenn V, et al. (October 2002). "Expression of the integrin alpha Ebeta 7 identifies unique subsets of CD25+ as well as CD25- regulatory T cells". Proceedings of the National Academy of Sciences of the United States of America. 99 (20): 13031–13036. Bibcode:2002PNAS...9913031L. doi:10.1073/pnas.192162899. PMC 130581. PMID 12242333.

[pmid15608520-8] Aziz S, Fackler OT, Meyerhans A, Müller-Lantzsch N, Zeitz M, Schneider T (January 2005). "Replication of M-tropic HIV-1 in activated human intestinal lamina propria lymphocytes is the main reason for increased virus load in the intestinal mucosa". Journal of Acquired Immune Deficiency Syndromes. 38 (1): 23–30. doi:10.1097/00126334-200501010-00005. PMID 15608520. S2CID 22884381.

[pmid16216890-9] Johansson-Lindbom B, Svensson M, Pabst O, Palmqvist C, Marquez G, Förster R, et al. (October 2005). "Functional specialization of gut CD103+ dendritic cells in the regulation of tissue-selective T cell homing". The Journal of Experimental Medicine. 202 (8): 1063–1073. doi:10.1084/jem.20051100. PMC 2213212. PMID 16216890.

[isbn92-832-2431-0-10] Swerdlow SH, Campo E, Harris NL, Jaffe ES, Pileri SA, Stein H, et al. (2008). WHO Classification of Tumours of Haematopoietic and Lymphoid Tissues (World Health Organization Classification of Tumours) (4th ed.). Geneva: World Health Organization. ISBN 978-92-832-2431-0.

[pmid9378961-11] Hadley GA, Bartlett ST, Via CS, Rostapshova EA, Moainie S (October 1997). "The epithelial cell-specific integrin, CD103 (alpha E integrin), defines a novel subset of alloreactive CD8+ CTL". Journal of Immunology. 159 (8): 3748–3756. doi:10.4049/jimmunol.159.8.3748. PMID 9378961.

[pmid10978890-12] Agace WW, Higgins JM, Sadasivan B, Brenner MB, Parker CM (October 2000). "T-lymphocyte-epithelial-cell interactions: integrin alpha(E)(CD103)beta(7), LEEP-CAM and chemokines". Current Opinion in Cell Biology. 12 (5): 563–568. doi:10.1016/S0955-0674(00)00132-0. PMID 10978890.

[13] Kutlesa S, Wessels JT, Speiser A, Steiert I, Müller CA, Klein G (December 2002). "E-cadherin-mediated interactions of thymic epithelial cells with CD103+ thymocytes lead to enhanced thymocyte cell proliferation". Journal of Cell Science. 115 (Pt 23): 4505–4515. doi:10.1242/jcs.00142. PMID 12414996. S2CID 14571087.

[pmid17137867-14] Allakhverdi Z, Fitzpatrick D, Boisvert A, Baba N, Bouguermouh S, Sarfati M, et al. (December 2006). "Expression of CD103 identifies human regulatory T-cell subsets". The Journal of Allergy and Clinical Immunology. 118 (6): 1342–1349. doi:10.1016/j.jaci.2006.07.034. PMID 17137867.

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v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation)
1–50	CD1 a-c 1A 1B 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50
51–100	CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 - CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100
101–150	CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150
151–200	CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200
201–250	CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 - CD248 CD249
251–300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299
301–350	CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD327 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

ITGAE

Tissue distribution

Function

See also

References

Further reading

External links