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{{Infobox_gene}}
{{Infobox_gene}}
'''Epithelial membrane protein 3''' is a [[protein]] that in humans is encoded by the ''EMP3'' [[gene]].<ref name="pmid8996089">{{cite journal | vauthors = Ben-Porath I, Benvenisty N | title = Characterization of a tumor-associated gene, a member of a novel family of genes encoding membrane glycoproteins | journal = Gene | volume = 183 | issue = 1–2 | pages = 69–75 |date=Feb 1997 | pmid = 8996089 | pmc =  | doi =10.1016/S0378-1119(96)00475-1  }}</ref><ref name="pmid10331954">{{cite journal | vauthors = Liehr T, Kuhlenbaumer G, Wulf P, Taylor V, Suter U, Van Broeckhoven C, Lupski JR, Claussen U, Rautenstrauss B | title = Regional localization of the human epithelial membrane protein genes 1, 2, and 3 (EMP1, EMP2, EMP3) to 12p12.3, 16p13.2, and 19q13.3 | journal = Genomics | volume = 58 | issue = 1 | pages = 106–8 |date=Jul 1999 | pmid = 10331954 | pmc = | doi = 10.1006/geno.1999.5803 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: EMP3 epithelial membrane protein 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2014| accessdate = }}</ref>
'''Epithelial membrane protein 3 (EMP3)''' is a trans-membrane signaling molecule that is encoded by the myelin-related [[gene]] EMP3. EMP3 is a member of the peripheral myelin protein gene family 22-kDa ([[Peripheral myelin protein 22|PMP22]]), which is mainly responsible for the formation of the [[Myelin Sheath|sheath]] of compact [[myelin]].<ref name="Alaminos_2005">{{cite journal | vauthors = Alaminos M, Dávalos V, Ropero S, Setién F, Paz MF, Herranz M, Fraga MF, Mora J, Cheung NK, Gerald WL, Esteller M | title = EMP3, a myelin-related gene located in the critical 19q13.3 region, is epigenetically silenced and exhibits features of a candidate tumor suppressor in glioma and neuroblastoma | journal = Cancer Research | volume = 65 | issue = 7 | pages = 2565–71 | date = April 2005 | pmid = 15805250 | doi = 10.1158/0008-5472.CAN-04-4283 }}</ref><ref name="Mellai_2013">{{cite journal | vauthors = Mellai M, Piazzi A, Caldera V, Annovazzi L, Monzeglio O, Senetta R, Cassoni P, Schiffer D | title = Promoter hypermethylation of the EMP3 gene in a series of 229 human gliomas | journal = BioMed Research International | volume = 2013 | pages = 756302 | date = 2013 | pmid = 24083241 | pmc = 3776370 | doi = 10.1155/2013/756302 }}</ref> Although the detailed functions and mechanisms of EMP3 still remain unclear, it is suggested that EMP3 is possibly epigenetically linked to certain carcinomas.
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==References==
== Structure ==
{{reflist}}
[[File:EMP3.png|thumb|left|The EMP3 structure based on the 163-amino acid sequence. Four yellow helices represent four transmembrane domains.<ref name = "Strausberg_2002">{{cite journal | vauthors = Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA | display-authors = 6 | title = Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 99 | issue = 26 | pages = 16899–903 | date = December 2002 | pmid = 12477932 | pmc = 139241 | doi = 10.1073/pnas.242603899 }}</ref>]]


==Further reading==
EMP3 is a protein composed of a 163-amino acid sequence, which is expressed from its gene located on the band of the 19q13.3 in the ''[[Homo sapiens]]'' chromosome.<ref name = "Strausberg_2002" /> EMP3 has the highest expression in the peripheral blood leukocytes compared to the expression in other body tissues.<ref>{{cite journal | vauthors = Taylor V, Suter U | title = Epithelial membrane protein-2 and epithelial membrane protein-3: two novel members of the peripheral myelin protein 22 gene family | journal = Gene | volume = 175 | issue = 1-2 | pages = 115–20 | date = October 1996 | pmid = 8917086 }}</ref> The protein is characterized by 4 transmembrane domains and two N-linked glycosylation sites in the first extracellular loop.<ref name="Alaminos_2005" />
{{refbegin |30em}}
{{PBB_Further_reading
| citations =
*{{cite journal  | vauthors=Lobsiger CS, Magyar JP, Taylor V |title=Identification and characterization of a cDNA and the structural gene encoding the mouse epithelial membrane protein-1 |journal=Genomics |volume=36 |issue= 3 |pages= 379–87 |year= 1997 |pmid= 8884260 |doi=10.1006/geno.1996.0482  |display-authors=etal}}
*{{cite journal | vauthors=Taylor V, Suter U |title=Epithelial membrane protein-2 and epithelial membrane protein-3: two novel members of the peripheral myelin protein 22 gene family |journal=Gene |volume=175 |issue= 1–2 |pages= 115–20 |year= 1996 |pmid= 8917086 |doi=10.1016/0378-1119(96)00134-5  }}
*{{cite journal  | vauthors=Bolin LM, McNeil T, Lucian LA |title=HNMP-1: a novel hematopoietic and neural membrane protein differentially regulated in neural development and injury |journal=J. Neurosci. |volume=17 |issue= 14 |pages= 5493–502 |year= 1997 |pmid= 9204931 |doi=  |display-authors=etal}}
*{{cite journal  | vauthors=Yus-Najera E, Santana-Castro I, Villarroel A |title=The identification and characterization of a noncontinuous calmodulin-binding site in noninactivating voltage-dependent KCNQ potassium channels |journal=J. Biol. Chem. |volume=277 |issue= 32 |pages= 28545–53 |year= 2002 |pmid= 12032157 |doi= 10.1074/jbc.M204130200 }}
*{{cite journal  | vauthors=Wilson HL, Wilson SA, Surprenant A, North RA |title=Epithelial membrane proteins induce membrane blebbing and interact with the P2X7 receptor C terminus |journal=J. Biol. Chem. |volume=277 |issue= 37 |pages= 34017–23 |year= 2002 |pmid= 12107182 |doi= 10.1074/jbc.M205120200 }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |display-authors=etal}}
*{{cite journal  | vauthors=Schwake M, Jentsch TJ, Friedrich T |title=A carboxy-terminal domain determines the subunit specificity of KCNQ K+ channel assembly |journal=EMBO Rep. |volume=4 |issue= 1 |pages= 76–81 |year= 2003 |pmid= 12524525 |doi= 10.1038/sj.embor.embor715  | pmc=1315815 }}
*{{cite journal  | vauthors=Yus-Nájera E, Muñoz A, Salvador N |title=Localization of KCNQ5 in the normal and epileptic human temporal neocortex and hippocampal formation |journal=Neuroscience |volume=120 |issue= 2 |pages= 353–64 |year= 2003 |pmid= 12890507 |doi=10.1016/S0306-4522(03)00321-X  |display-authors=etal}}
*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 |display-authors=etal}}
*{{cite journal  | vauthors=Nielsen K, Heegaard S, Vorum H |title=Altered expression of CLC, DSG3, EMP3, S100A2, and SLPI in corneal epithelium from keratoconus patients |journal=Cornea |volume=24 |issue= 6 |pages= 661–8 |year= 2005 |pmid= 16015083 |doi=10.1097/01.ico.0000153556.59407.69  |display-authors=etal}}
*{{cite journal  | vauthors=Li KK, Pang JC, Chung NY |title=EMP3 overexpression is associated with oligodendroglial tumors retaining chromosome arms 1p and 19q |journal=Int. J. Cancer |volume=120 |issue= 4 |pages= 947–50 |year= 2007 |pmid= 17187361 |doi= 10.1002/ijc.22415 |display-authors=etal}}
*{{cite journal  | vauthors=Kunitz A, Wolter M, van den Boom J |title=DNA hypermethylation and aberrant expression of the EMP3 gene at 19q13.3 in Human Gliomas |journal=Brain Pathol. |volume=17 |issue= 4 |pages= 363–70 |year= 2007 |pmid= 17610521 |doi= 10.1111/j.1750-3639.2007.00083.x |display-authors=etal}}
}}
{{refend}}


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== Function ==
{{PBB_Controls
EMP3 is a transmembrane protein which participates in cell to cell interaction and [[Cell growth|cell proliferation]].<ref name="Jun_2017">{{cite journal | vauthors = Jun F, Hong J, Liu Q, Guo Y, Liao Y, Huang J, Wen S, Shen L | title = Epithelial membrane protein 3 regulates TGF-β signaling activation in CD44-high glioblastoma | journal = Oncotarget | volume = 8 | issue = 9 | pages = 14343–14358 | date = February 2017 | pmid = 27527869 | pmc = 5362410 | doi = 10.18632/oncotarget.11102 }}</ref> Overexpression and silencing of EMP3 both interrupt the normal expression of the EMP3 gene, which induces the progression(and formation) of cancers. Based on these properties of EMP3 and the prognostic analyses on several types of tumors and cancers, EMP3 has a tumor-suppressor-like role in regulating differentiation, [[apoptosis]] and development of cancer cells. However, the detailed mechanism still needs to be investigated.<ref name="Alaminos_2005" /><ref name="Mellai_2013" /><ref name="Zhou_2009">{{cite journal | vauthors = Zhou W, Jiang Z, Li X, Xu F, Liu Y, Wen P, Kong L, Hou M, Yu J | title = EMP3 overexpression in primary breast carcinomas is not associated with epigenetic aberrations | journal = Journal of Korean Medical Science | volume = 24 | issue = 1 | pages = 97–103 | date = February 2009 | pmid = 19270820 | pmc = 2650972 | doi = 10.3346/jkms.2009.24.1.97 }}</ref>
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=== Tumorgenesis and carcinogenesis ===
==== Primary breast carcinomas ====
The detailed functions as well as the mechanism of EMP3 in the development of various [[Carcinoma|carcinomas]] have remained unclear.<ref name="Alaminos_2005" /><ref name="Mellai_2013" /> However, it was found that the levels of expression of EMP3 mRNA have a positive correlation in [[Breast cancer|primary breast carcinomas]]. According to the study, EMP3 mRNA has a higher level of expression in the carcinoma compared to normal breast tissues. The overexpression of EMP3 has a significant correlation with histological grade III, lymph node metastasis, and strong Her-2 expression. Additionally, the [[Methylation|hypermethylation]] on the [[Promoter (genetics)|promoter]] region of EMP3 has appeared in about 35% of the studies breast carcinoma cases. However, higher EMP3 expression levels occur in patients with both types of breast carcinomas, regardless of the promoter regions of EMP3 being hypermethylated or unmethylated.<ref name="Zhou_2009" />
==== Hepatocellular carcinoma (HCC) ====
[[Hepatocellular carcinoma|Hepatocellular carcinoma (HCC)]], which is mainly caused by the chronic infections of hepatitis B virus and hepatitis C virus, become one of the major causes of cancer mortality worldwide in the recent years.<ref>{{cite journal | vauthors = Torre LA, Bray F, Siegel RL, Ferlay J, Lortet-Tieulent J, Jemal A | title = Global cancer statistics, 2012 | journal = Ca | volume = 65 | issue = 2 | pages = 87–108 | date = March 2015 | pmid = 25651787 | doi = 10.3322/caac.21262 }}</ref><ref>{{cite journal | vauthors = Degasperi E, Colombo M | title = Distinctive features of hepatocellular carcinoma in non-alcoholic fatty liver disease | journal = The Lancet. Gastroenterology & Hepatology | volume = 1 | issue = 2 | pages = 156–164 | date = October 2016 | pmid = 28404072 | doi = 10.1016/S2468-1253(16)30018-8 }}</ref> EMP3 expression in HCC tumor cells has a higher expression level than that it does in normal tissues at similar regions of the liver. It was also found that the HCC patients who have a relatively lower historlogical grade inversely possess a higher level of expression in EMP3. Then, the researchers found that knockdown ([[gene silencing]]) of EMP3 resulted in reduction of cell proliferation and arrest of cell cycle, which suggests a potential role of EMP3 in tumor-suppressing.<ref name="Hsieh_2015">{{cite journal | vauthors = Hsieh YH, Hsieh SC, Lee CH, Yang SF, Cheng CW, Tang MJ, Lin CL, Lin CL, Chou RH | title = Targeting EMP3 suppresses proliferation and invasion of hepatocellular carcinoma cells through inactivation of PI3K/Akt pathway | journal = Oncotarget | volume = 6 | issue = 33 | pages = 34859–74 | date = October 2015 | pmid = 26472188 | pmc = 4741495 | doi = 10.18632/oncotarget.5414 }}</ref>
==== Brain cancer ====
EMP3 is found to play a large role in the progression of [[Neuroblastoma|neuroblastomas]] and [[Glioblastoma|glioblastomas]], which are two of the most common types of brain cancers. Both have fast [[Carcinogenesis|carinogenesis]] result in a high rate of mortality.<ref name="Alaminos_2005" /><ref name="Jun_2017" /> EMP3 is proposed as an [[oncogene]] whose overexpression in the progression correlated with [[Glioblastoma|glioblastoma (GBM)]].<ref name="Jun_2017" /> Reduction in EMP3 expression in CD44-high GBM cell lines promotes apoptosis of the cancer cell lines and disables potential tumorigenesis.<ref name="Jun_2017" />
One of the signaling activation pathway involving EMP3 in the progression of glioblastoma was identified in 2016. The pathway was identified as [[TGF β|TGF-β]]/[[SMAD (protein)|Smad]]2/3 signaling, in which the unregulated TGF-β signaling promotes tumorigenesis in various human cells, especially CD44-high glioma cells.<ref name="Jun_2017" /> The interaction between EMP3 and the receptor of TGF-β regulate the [[TGF β|TGF-β]]/[[SMAD (protein)|Smad]]2/3 signaling activation, which eventually suppresses cell proliferation and weakens tumorigenesis in glioblastoma.<ref name="Jun_2017" />
== Clinical significance ==
Due to the controversial effects of EMP3 on tumor suppression, the applicable treatments for certain carcinomas related to EMP3 are still unvalidated in humans.<ref name="Hsieh_2015" /><ref name = "Morris_2015">{{cite journal | vauthors = Morris LG, Chan TA | title = Therapeutic targeting of tumor suppressor genes | journal = Cancer | volume = 121 | issue = 9 | pages = 1357–68 | date = May 2015 | pmid = 25557041 | pmc = 4526158 | doi = 10.1002/cncr.29140 }}</ref> However, some animal experiments have showed a positive result on suppressing the tumorous tissues by modifying the EMP3 gene.<ref name="Hsieh_2015" />
== References ==
{{Reflist}}


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Latest revision as of 02:25, 17 December 2018

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Epithelial membrane protein 3 (EMP3) is a trans-membrane signaling molecule that is encoded by the myelin-related gene EMP3. EMP3 is a member of the peripheral myelin protein gene family 22-kDa (PMP22), which is mainly responsible for the formation of the sheath of compact myelin.[1][2] Although the detailed functions and mechanisms of EMP3 still remain unclear, it is suggested that EMP3 is possibly epigenetically linked to certain carcinomas.

Structure

File:EMP3.png
The EMP3 structure based on the 163-amino acid sequence. Four yellow helices represent four transmembrane domains.[3]

EMP3 is a protein composed of a 163-amino acid sequence, which is expressed from its gene located on the band of the 19q13.3 in the Homo sapiens chromosome.[3] EMP3 has the highest expression in the peripheral blood leukocytes compared to the expression in other body tissues.[4] The protein is characterized by 4 transmembrane domains and two N-linked glycosylation sites in the first extracellular loop.[1]

Function

EMP3 is a transmembrane protein which participates in cell to cell interaction and cell proliferation.[5] Overexpression and silencing of EMP3 both interrupt the normal expression of the EMP3 gene, which induces the progression(and formation) of cancers. Based on these properties of EMP3 and the prognostic analyses on several types of tumors and cancers, EMP3 has a tumor-suppressor-like role in regulating differentiation, apoptosis and development of cancer cells. However, the detailed mechanism still needs to be investigated.[1][2][6]

Tumorgenesis and carcinogenesis

Primary breast carcinomas

The detailed functions as well as the mechanism of EMP3 in the development of various carcinomas have remained unclear.[1][2] However, it was found that the levels of expression of EMP3 mRNA have a positive correlation in primary breast carcinomas. According to the study, EMP3 mRNA has a higher level of expression in the carcinoma compared to normal breast tissues. The overexpression of EMP3 has a significant correlation with histological grade III, lymph node metastasis, and strong Her-2 expression. Additionally, the hypermethylation on the promoter region of EMP3 has appeared in about 35% of the studies breast carcinoma cases. However, higher EMP3 expression levels occur in patients with both types of breast carcinomas, regardless of the promoter regions of EMP3 being hypermethylated or unmethylated.[6]

Hepatocellular carcinoma (HCC)

Hepatocellular carcinoma (HCC), which is mainly caused by the chronic infections of hepatitis B virus and hepatitis C virus, become one of the major causes of cancer mortality worldwide in the recent years.[7][8] EMP3 expression in HCC tumor cells has a higher expression level than that it does in normal tissues at similar regions of the liver. It was also found that the HCC patients who have a relatively lower historlogical grade inversely possess a higher level of expression in EMP3. Then, the researchers found that knockdown (gene silencing) of EMP3 resulted in reduction of cell proliferation and arrest of cell cycle, which suggests a potential role of EMP3 in tumor-suppressing.[9]

Brain cancer

EMP3 is found to play a large role in the progression of neuroblastomas and glioblastomas, which are two of the most common types of brain cancers. Both have fast carinogenesis result in a high rate of mortality.[1][5] EMP3 is proposed as an oncogene whose overexpression in the progression correlated with glioblastoma (GBM).[5] Reduction in EMP3 expression in CD44-high GBM cell lines promotes apoptosis of the cancer cell lines and disables potential tumorigenesis.[5]

One of the signaling activation pathway involving EMP3 in the progression of glioblastoma was identified in 2016. The pathway was identified as TGF-β/Smad2/3 signaling, in which the unregulated TGF-β signaling promotes tumorigenesis in various human cells, especially CD44-high glioma cells.[5] The interaction between EMP3 and the receptor of TGF-β regulate the TGF-β/Smad2/3 signaling activation, which eventually suppresses cell proliferation and weakens tumorigenesis in glioblastoma.[5]

Clinical significance

Due to the controversial effects of EMP3 on tumor suppression, the applicable treatments for certain carcinomas related to EMP3 are still unvalidated in humans.[9][10] However, some animal experiments have showed a positive result on suppressing the tumorous tissues by modifying the EMP3 gene.[9]

References

  1. ↑ 1.0 1.1 1.2 1.3 1.4 Alaminos M, Dávalos V, Ropero S, Setién F, Paz MF, Herranz M, Fraga MF, Mora J, Cheung NK, Gerald WL, Esteller M (April 2005). "EMP3, a myelin-related gene located in the critical 19q13.3 region, is epigenetically silenced and exhibits features of a candidate tumor suppressor in glioma and neuroblastoma". Cancer Research. 65 (7): 2565–71. doi:10.1158/0008-5472.CAN-04-4283. PMID 15805250.
  2. ↑ 2.0 2.1 2.2 Mellai M, Piazzi A, Caldera V, Annovazzi L, Monzeglio O, Senetta R, Cassoni P, Schiffer D (2013). "Promoter hypermethylation of the EMP3 gene in a series of 229 human gliomas". BioMed Research International. 2013: 756302. doi:10.1155/2013/756302. PMC 3776370. PMID 24083241.
  3. ↑ 3.0 3.1 Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, et al. (December 2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proceedings of the National Academy of Sciences of the United States of America. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  4. ↑ Taylor V, Suter U (October 1996). "Epithelial membrane protein-2 and epithelial membrane protein-3: two novel members of the peripheral myelin protein 22 gene family". Gene. 175 (1–2): 115–20. PMID 8917086.
  5. ↑ 5.0 5.1 5.2 5.3 5.4 5.5 Jun F, Hong J, Liu Q, Guo Y, Liao Y, Huang J, Wen S, Shen L (February 2017). "Epithelial membrane protein 3 regulates TGF-β signaling activation in CD44-high glioblastoma". Oncotarget. 8 (9): 14343–14358. doi:10.18632/oncotarget.11102. PMC 5362410. PMID 27527869.
  6. ↑ 6.0 6.1 Zhou W, Jiang Z, Li X, Xu F, Liu Y, Wen P, Kong L, Hou M, Yu J (February 2009). "EMP3 overexpression in primary breast carcinomas is not associated with epigenetic aberrations". Journal of Korean Medical Science. 24 (1): 97–103. doi:10.3346/jkms.2009.24.1.97. PMC 2650972. PMID 19270820.
  7. ↑ Torre LA, Bray F, Siegel RL, Ferlay J, Lortet-Tieulent J, Jemal A (March 2015). "Global cancer statistics, 2012". Ca. 65 (2): 87–108. doi:10.3322/caac.21262. PMID 25651787.
  8. ↑ Degasperi E, Colombo M (October 2016). "Distinctive features of hepatocellular carcinoma in non-alcoholic fatty liver disease". The Lancet. Gastroenterology & Hepatology. 1 (2): 156–164. doi:10.1016/S2468-1253(16)30018-8. PMID 28404072.
  9. ↑ 9.0 9.1 9.2 Hsieh YH, Hsieh SC, Lee CH, Yang SF, Cheng CW, Tang MJ, Lin CL, Lin CL, Chou RH (October 2015). "Targeting EMP3 suppresses proliferation and invasion of hepatocellular carcinoma cells through inactivation of PI3K/Akt pathway". Oncotarget. 6 (33): 34859–74. doi:10.18632/oncotarget.5414. PMC 4741495. PMID 26472188.
  10. ↑ Morris LG, Chan TA (May 2015). "Therapeutic targeting of tumor suppressor genes". Cancer. 121 (9): 1357–68. doi:10.1002/cncr.29140. PMC 4526158. PMID 25557041.
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