MSRA (gene): Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Peptide methionine sulfoxide reductase''' (Msr) is a family of [[enzyme]]s that in humans is encoded by the ''MSRA'' [[gene]].<ref name="pmid10452521">{{cite journal |vauthors=Kuschel L, Hansel A, Schonherr R, Weissbach H, Brot N, Hoshi T, Heinemann SH | title = Molecular cloning and functional expression of a human peptide methionine sulfoxide reductase (hMsrA) | journal = FEBS Lett | volume = 456 | issue = 1 | pages = 17–21 |date=Sep 1999 | pmid = 10452521 | pmc =  | doi =10.1016/S0014-5793(99)00917-5  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MSRA methionine sulfoxide reductase A| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4482| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Methionine sulfoxide reductase A
| HGNCid = 7377
| Symbol = MSRA
| AltSymbols =;
| OMIM = 601250
| ECnumber = 
| Homologene = 5812
| MGIid = 106916
| GeneAtlas_image1 = PBB_GE_MSRA_219281_at_tn.png
| Function = {{GNF_GO|id=GO:0008113 |text = protein-methionine-S-oxide reductase activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006464 |text = protein modification process}} {{GNF_GO|id=GO:0006555 |text = methionine metabolic process}} {{GNF_GO|id=GO:0006979 |text = response to oxidative stress}} {{GNF_GO|id=GO:0019538 |text = protein metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4482
    | Hs_Ensembl = ENSG00000175806
    | Hs_RefseqProtein = NP_036463
    | Hs_RefseqmRNA = NM_012331
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 8
    | Hs_GenLoc_start = 9949188
    | Hs_GenLoc_end = 10323811
    | Hs_Uniprot = Q9UJ68
    | Mm_EntrezGene = 110265
    | Mm_Ensembl = ENSMUSG00000054733
    | Mm_RefseqmRNA = NM_026322
    | Mm_RefseqProtein = NP_080598
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 14
    | Mm_GenLoc_start = 63076731
    | Mm_GenLoc_end = 63410013
    | Mm_Uniprot = Q5EBQ7
  }}
}}
'''Methionine sulfoxide reductase A''', also known as '''MSRA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MSRA methionine sulfoxide reductase A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4482| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Msr is ubiquitous and highly conserved. Human and animal studies have shown the highest levels of expression in kidney and liver.  It carries out the enzymatic reduction of [[Methionine oxidation|methionine sulfoxide]] (MetO), the oxidized form of the amino acid [[methionine]] (Met), back to methionine, using [[thioredoxin]] to catalyze the enzymatic reduction and repair of oxidized methionine residues.<ref name=StadtmanBBA>{{cite journal |vauthors=Stadtman ER, Van Remmen H, Richardson A, Wehr NB, Levine RL | title=Methionine oxidation and aging | journal=Biochimica et Biophysica Acta | volume=1703 | issue=2 | year=2005 | pages=135–140  | pmid=15680221 | doi=10.1016/j.bbapap.2004.08.010}}</ref> Its proposed function is thus the repair of [[oxidative damage]] to proteins to restore biological activity.<ref name="entrez"/> Oxidation of methionine residues in tissue proteins can cause them to misfold or otherwise render them dysfunctional.<ref name=StadtmanBBA/>
{{PBB_Summary
 
| section_title =
== Clinical significance ==
| summary_text = This protein is ubiquitous and highly conserved. It carries out the enzymatic reduction of methionine sulfoxide to methionine. Human and animal studies have shown the highest levels of expression in kidney and nervous tissue. Its proposed function is the repair of oxidative damage to proteins to restore biological activity.<ref name="entrez">{{cite web | title = Entrez Gene: MSRA methionine sulfoxide reductase A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4482| accessdate = }}</ref>
 
}}
MetO increases with age in body tissues, which is believed by some to contribute to [[senescence|biological ageing]].<ref name=StadtmanBBA/><ref>{{cite journal |vauthors=Shringarpure R, Davies KJ | title=Protein turnover by the proteasome in aging and disease | journal=Free Radical Biology & Medicine | volume=32 | issue=11 | year=2002 | pages=1084–1089  | pmid=12031893 | doi=10.1016/S0891-5849(02)00824-9}}</ref> Moreover, levels of methionine sulfoxide reductase A (MsrA) decline in aging tissues in mice and in association with age-related disease in humans.<ref name=StadtmanBBA/> There is thus a rationale for thinking that by maintaining the structureincreased levels or activity of MsrA might retard the rate of aging.
 
Indeed, transgenic [[Drosophila]] (fruit flies) that overexpress methionine sulfoxide reductase show [[life extension|extended lifespan]].<ref>{{cite journal |vauthors=Ruan H, Tang XD, Chen ML, Joiner ML, Sun G, Brot N, Weissbach H, Heinemann SH, Iverson L, Wu CF, Hoshi T | title=High-quality life extension by the enzyme peptide methionine sulfoxide reductase | journal=[[Proceedings of the National Academy of Sciences of the United States of America]]  | volume=99 | issue=5 | year=2002 | pages=2748–2753  | url = http://www.pnas.org/content/99/5/2748.full| id= | pmid=11867705 | doi=10.1073/pnas.032671199 | pmc=122419}}</ref> However, the effects of MsrA overexpression in mice were ambiguous.<ref name="Salmon2016">{{cite journal|vauthors=Salmon AB, Kim G, Liu C, Wren JD, Georgescu C, Richardson A, Levine RL|title=Effects of transgenic methionine sulfoxide reductase A (MsrA) expression on lifespan and age-dependent changes in metabolic function in mice|journal=Redox Biol|date=December 2016|volume=10|pages=251-256|doi=10.1016/j.redox.2016.10.012|pmid=27821326|url=http://www.sciencedirect.com/science/article/pii/S2213231716301987|accessdate=21 November 2016}}</ref> MsrA is found in both the cytosol and the energy-producing [[mitochondria]], where most of the body's endogenous [[free radicals]] are produced. Transgenically increasing the levels of MsrA in either the cytosol or the mitochondria had no significant effect on lifespan assessed by most standard statistical tests, and may possibly have led to early deaths in the cytosol-specific mice, although the survival curves appeared to suggest a slight increase in maximum (90%) survivorship, as did analysis using Boschloo's Exact test, a [[binomial test]] designed to test greater extreme variation.<ref name="Salmon2016"/>
 
Deletion of this gene has been associated with [[insulin]] resistance in mice,<ref name="pmid23089224">{{cite journal |vauthors=Styskal JL, Nwagwu FA, Watkins YN, Liang H, Richardson A, Musi N, Salmon AB | title = Methionine sulfoxide reductase a affects insulin resistance by protecting insulin receptor function | journal = Free Radic. Biol. Med. | volume = 56| issue = | pages = 123–32|date=October 2012 | pmid = 23089224 | doi = 10.1016/j.freeradbiomed.2012.10.544 }}</ref> while overexpression reduces insulin resistance in old mice.<ref name="Salmon2016"/>
 
==See also==
* [[MSRB2]]
* [[Methionine oxidation]]
* [[SEPX1]]


==References==
==References==
{{reflist|2}}
{{Reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  |vauthors=Hansel A, Heinemann SH, Hoshi T |title=Heterogeneity and function of mammalian MSRs: enzymes for repair, protection and regulation. |journal=Biochim. Biophys. Acta |volume=1703 |issue= 2 |pages= 239–47 |year= 2005 |pmid= 15680232 |doi= 10.1016/j.bbapap.2004.09.010 }}
| citations =
*{{cite journal   |vauthors=Moskovitz J, Jenkins NA, Gilbert DJ, etal |title=Chromosomal localization of the mammalian peptide-methionine sulfoxide reductase gene and its differential expression in various tissues. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 8 |pages= 3205–8 |year= 1996 |pmid= 8622914 |doi=10.1073/pnas.93.8.3205  | pmc=39583 }}
*{{cite journal  | author=Hansel A, Heinemann SH, Hoshi T |title=Heterogeneity and function of mammalian MSRs: enzymes for repair, protection and regulation. |journal=Biochim. Biophys. Acta |volume=1703 |issue= 2 |pages= 239-47 |year= 2005 |pmid= 15680232 |doi= 10.1016/j.bbapap.2004.09.010 }}
*{{cite journal   |vauthors=Hansel A, Kuschel L, Hehl S, etal |title=Mitochondrial targeting of the human peptide methionine sulfoxide reductase (MSRA), an enzyme involved in the repair of oxidized proteins. |journal=FASEB J. |volume=16 |issue= 8 |pages= 911–3 |year= 2002 |pmid= 12039877 |doi= 10.1096/fj.01-0737fje }}
*{{cite journal | author=Moskovitz J, Jenkins NA, Gilbert DJ, ''et al.'' |title=Chromosomal localization of the mammalian peptide-methionine sulfoxide reductase gene and its differential expression in various tissues. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 8 |pages= 3205-8 |year= 1996 |pmid= 8622914 |doi= }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 }}
*{{cite journal  | author=Kuschel L, Hansel A, Schönherr R, ''et al.'' |title=Molecular cloning and functional expression of a human peptide methionine sulfoxide reductase (hMsrA). |journal=FEBS Lett. |volume=456 |issue= 1 |pages= 17-21 |year= 1999 |pmid= 10452521 |doi=  }}
*{{cite journal  |vauthors=Vougier S, Mary J, Friguet B |title=Subcellular localization of methionine sulphoxide reductase A (MsrA): evidence for mitochondrial and cytosolic isoforms in rat liver cells. |journal=Biochem. J. |volume=373 |issue= Pt 2 |pages= 531–7 |year= 2003 |pmid= 12693988 |doi= 10.1042/BJ20030443 | pmc=1223498 }}
*{{cite journal | author=Hansel A, Kuschel L, Hehl S, ''et al.'' |title=Mitochondrial targeting of the human peptide methionine sulfoxide reductase (MSRA), an enzyme involved in the repair of oxidized proteins. |journal=FASEB J. |volume=16 |issue= 8 |pages= 911-3 |year= 2002 |pmid= 12039877 |doi= 10.1096/fj.01-0737fje }}
*{{cite journal   |vauthors=Picot CR, Perichon M, Cintrat JC, etal |title=The peptide methionine sulfoxide reductases, MsrA and MsrB (hCBS-1), are downregulated during replicative senescence of human WI-38 fibroblasts. |journal=FEBS Lett. |volume=558 |issue= 1-3 |pages= 74–8 |year= 2004 |pmid= 14759519 |doi= 10.1016/S0014-5793(03)01530-8 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |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 }}
*{{cite journal   |vauthors=Kantorow M, Hawse JR, Cowell TL, etal |title=Methionine sulfoxide reductase A is important for lens cell viability and resistance to oxidative stress. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 26 |pages= 9654–9 |year= 2004 |pmid= 15199188 |doi= 10.1073/pnas.0403532101 | pmc=470730 }}
*{{cite journal  | author=Vougier S, Mary J, Friguet B |title=Subcellular localization of methionine sulphoxide reductase A (MsrA): evidence for mitochondrial and cytosolic isoforms in rat liver cells. |journal=Biochem. J. |volume=373 |issue= Pt 2 |pages= 531-7 |year= 2003 |pmid= 12693988 |doi= 10.1042/BJ20030443 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |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 }}
*{{cite journal | author=Picot CR, Perichon M, Cintrat JC, ''et al.'' |title=The peptide methionine sulfoxide reductases, MsrA and MsrB (hCBS-1), are downregulated during replicative senescence of human WI-38 fibroblasts. |journal=FEBS Lett. |volume=558 |issue= 1-3 |pages= 74-8 |year= 2004 |pmid= 14759519 |doi= 10.1016/S0014-5793(03)01530-8 }}
*{{cite journal  |vauthors=De Luca A, Sacchetta P, Di Ilio C, Favaloro B |title=Identification and analysis of the promoter region of the human methionine sulphoxide reductase A gene. |journal=Biochem. J. |volume=393 |issue= Pt 1 |pages= 321–9 |year= 2006 |pmid= 16162094 |doi= 10.1042/BJ20050973 | pmc=1383691 }}
*{{cite journal | author=Kantorow M, Hawse JR, Cowell TL, ''et al.'' |title=Methionine sulfoxide reductase A is important for lens cell viability and resistance to oxidative stress. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 26 |pages= 9654-9 |year= 2004 |pmid= 15199188 |doi= 10.1073/pnas.0403532101 }}
*{{cite journal   |vauthors=Picot CR, Petropoulos I, Perichon M, etal |title=Overexpression of MsrA protects WI-38 SV40 human fibroblasts against H2O2-mediated oxidative stress. |journal=Free Radic. Biol. Med. |volume=39 |issue= 10 |pages= 1332–41 |year= 2006 |pmid= 16257642 |doi= 10.1016/j.freeradbiomed.2005.06.017 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |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 }}
*{{cite journal   |vauthors=Lee JW, Gordiyenko NV, Marchetti M, etal |title=Gene structure, localization and role in oxidative stress of methionine sulfoxide reductase A (MSRA) in the monkey retina. |journal=Exp. Eye Res. |volume=82 |issue= 5 |pages= 816–27 |year= 2006 |pmid= 16364291 |doi= 10.1016/j.exer.2005.10.003 | pmc=2825745 }}
*{{cite journal  | author=De Luca A, Sacchetta P, Di Ilio C, Favaloro B |title=Identification and analysis of the promoter region of the human methionine sulphoxide reductase A gene. |journal=Biochem. J. |volume=393 |issue= Pt 1 |pages= 321-9 |year= 2006 |pmid= 16162094 |doi= 10.1042/BJ20050973 }}
*{{cite journal   |vauthors=Schallreuter KU, Rübsam K, Chavan B, etal |title=Functioning methionine sulfoxide reductases A and B are present in human epidermal melanocytes in the cytosol and in the nucleus. |journal=Biochem. Biophys. Res. Commun. |volume=342 |issue= 1 |pages= 145–52 |year= 2006 |pmid= 16480945 |doi= 10.1016/j.bbrc.2006.01.124 }}
*{{cite journal | author=Picot CR, Petropoulos I, Perichon M, ''et al.'' |title=Overexpression of MsrA protects WI-38 SV40 human fibroblasts against H2O2-mediated oxidative stress. |journal=Free Radic. Biol. Med. |volume=39 |issue= 10 |pages= 1332-41 |year= 2006 |pmid= 16257642 |doi= 10.1016/j.freeradbiomed.2005.06.017 }}
*{{cite journal   |vauthors=Lei KF, Wang YF, Zhu XQ, etal |title=Identification of MSRA gene on chromosome 8p as a candidate metastasis suppressor for human hepatitis B virus-positive hepatocellular carcinoma. |journal=BMC Cancer |volume=7 |issue=  |pages= 172 |year= 2007 |pmid= 17784942 |doi= 10.1186/1471-2407-7-172 | pmc=2000900 }}
*{{cite journal | author=Lee JW, Gordiyenko NV, Marchetti M, ''et al.'' |title=Gene structure, localization and role in oxidative stress of methionine sulfoxide reductase A (MSRA) in the monkey retina. |journal=Exp. Eye Res. |volume=82 |issue= 5 |pages= 816-27 |year= 2006 |pmid= 16364291 |doi= 10.1016/j.exer.2005.10.003 }}
*{{cite journal | author=Schallreuter KU, Rübsam K, Chavan B, ''et al.'' |title=Functioning methionine sulfoxide reductases A and B are present in human epidermal melanocytes in the cytosol and in the nucleus. |journal=Biochem. Biophys. Res. Commun. |volume=342 |issue= 1 |pages= 145-52 |year= 2006 |pmid= 16480945 |doi= 10.1016/j.bbrc.2006.01.124 }}
*{{cite journal | author=Lei KF, Wang YF, Zhu XQ, ''et al.'' |title=Identification of MSRA gene on chromosome 8p as a candidate metastasis suppressor for human hepatitis B virus-positive hepatocellular carcinoma. |journal=BMC Cancer |volume=7 |issue=  |pages= 172 |year= 2007 |pmid= 17784942 |doi= 10.1186/1471-2407-7-172 }}
}}
{{refend}}
{{refend}}


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Revision as of 06:57, 4 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Peptide methionine sulfoxide reductase (Msr) is a family of enzymes that in humans is encoded by the MSRA gene.[1][2]

Function

Msr is ubiquitous and highly conserved. Human and animal studies have shown the highest levels of expression in kidney and liver. It carries out the enzymatic reduction of methionine sulfoxide (MetO), the oxidized form of the amino acid methionine (Met), back to methionine, using thioredoxin to catalyze the enzymatic reduction and repair of oxidized methionine residues.[3] Its proposed function is thus the repair of oxidative damage to proteins to restore biological activity.[2] Oxidation of methionine residues in tissue proteins can cause them to misfold or otherwise render them dysfunctional.[3]

Clinical significance

MetO increases with age in body tissues, which is believed by some to contribute to biological ageing.[3][4] Moreover, levels of methionine sulfoxide reductase A (MsrA) decline in aging tissues in mice and in association with age-related disease in humans.[3] There is thus a rationale for thinking that by maintaining the structureincreased levels or activity of MsrA might retard the rate of aging.

Indeed, transgenic Drosophila (fruit flies) that overexpress methionine sulfoxide reductase show extended lifespan.[5] However, the effects of MsrA overexpression in mice were ambiguous.[6] MsrA is found in both the cytosol and the energy-producing mitochondria, where most of the body's endogenous free radicals are produced. Transgenically increasing the levels of MsrA in either the cytosol or the mitochondria had no significant effect on lifespan assessed by most standard statistical tests, and may possibly have led to early deaths in the cytosol-specific mice, although the survival curves appeared to suggest a slight increase in maximum (90%) survivorship, as did analysis using Boschloo's Exact test, a binomial test designed to test greater extreme variation.[6]

Deletion of this gene has been associated with insulin resistance in mice,[7] while overexpression reduces insulin resistance in old mice.[6]

See also

References

  1. ↑ Kuschel L, Hansel A, Schonherr R, Weissbach H, Brot N, Hoshi T, Heinemann SH (Sep 1999). "Molecular cloning and functional expression of a human peptide methionine sulfoxide reductase (hMsrA)". FEBS Lett. 456 (1): 17–21. doi:10.1016/S0014-5793(99)00917-5. PMID 10452521.
  2. ↑ 2.0 2.1 "Entrez Gene: MSRA methionine sulfoxide reductase A".
  3. ↑ 3.0 3.1 3.2 3.3 Stadtman ER, Van Remmen H, Richardson A, Wehr NB, Levine RL (2005). "Methionine oxidation and aging". Biochimica et Biophysica Acta. 1703 (2): 135–140. doi:10.1016/j.bbapap.2004.08.010. PMID 15680221.
  4. ↑ Shringarpure R, Davies KJ (2002). "Protein turnover by the proteasome in aging and disease". Free Radical Biology & Medicine. 32 (11): 1084–1089. doi:10.1016/S0891-5849(02)00824-9. PMID 12031893.
  5. ↑ Ruan H, Tang XD, Chen ML, Joiner ML, Sun G, Brot N, Weissbach H, Heinemann SH, Iverson L, Wu CF, Hoshi T (2002). "High-quality life extension by the enzyme peptide methionine sulfoxide reductase". Proceedings of the National Academy of Sciences of the United States of America. 99 (5): 2748–2753. doi:10.1073/pnas.032671199. PMC 122419. PMID 11867705.
  6. ↑ 6.0 6.1 6.2 Salmon AB, Kim G, Liu C, Wren JD, Georgescu C, Richardson A, Levine RL (December 2016). "Effects of transgenic methionine sulfoxide reductase A (MsrA) expression on lifespan and age-dependent changes in metabolic function in mice". Redox Biol. 10: 251–256. doi:10.1016/j.redox.2016.10.012. PMID 27821326. Retrieved 21 November 2016.
  7. ↑ Styskal JL, Nwagwu FA, Watkins YN, Liang H, Richardson A, Musi N, Salmon AB (October 2012). "Methionine sulfoxide reductase a affects insulin resistance by protecting insulin receptor function". Free Radic. Biol. Med. 56: 123–32. doi:10.1016/j.freeradbiomed.2012.10.544. PMID 23089224.

Further reading


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