Sarcospan: Difference between revisions

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{{essay-like|date=July 2008}}
{{infobox protein
{{infobox protein
| Name = sarcospan
| Name = sarcospan
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Originally identified as Kirsten ras associated gene (krag),<ref name="watson"/> '''Sarcospan''' (SSPN) (is a 25-kDa [[transmembrane protein]] located in the [[dystrophin-associated protein complex]] of [[skeletal muscle]] cells, where it is most abundant.<ref name="watson"/> It contains four transmembrane spanning helices with both N- and C-terminal domains located intracellularly.<ref name="crosbie">{{cite journal |author=Crosbie |title=Sarcospan, the 25-kDa transmembrane component of the dystrophin-glycoprotein complex |journal=J Biol Chem |volume=272 |issue=50 |pages=31221–4 |year=1997 |pmid=9395445 |doi=10.1074/jbc.272.50.31221 |last2=Heighway |first2=J |last3=Venzke |first3=DP |last4=Lee |first4=JC |last5=Campbell |first5=KP |display-authors=etal}}</ref>    Loss of SSPN expression occurs in patients with [[Duchenne muscular dystrophy]]. [[Dystrophin]] is required for proper localization of SSPN.<ref name="crosbie"/>  SSPN is also an essential regulator of Akt signaling pathways. Without SSPN, Akt signaling pathways will be hindered and muscle regeneration will not occur.<ref name="watson">{{cite journal|last1=Marshall|first1=Jamie L|last2=Crosbie-Watson|first2=Rachelle H|title=Sarcospan: a small protein with large potential for Duchenne muscular dystrophy|journal=Skeletal Muscle|date=2013|volume=3|issue=1|pages=1|doi=10.1186/2044-5040-3-1}}</ref>
Originally identified as Kirsten ras associated gene (krag),<ref name="watson"/> '''Sarcospan''' (SSPN) (is a 25-kDa [[transmembrane protein]] located in the [[dystrophin-associated protein complex]] of [[skeletal muscle]] cells, where it is most abundant.<ref name="watson"/> It contains four transmembrane spanning helices with both N- and C-terminal domains located intracellularly.<ref name="crosbie">{{cite journal | vauthors = Crosbie RH, Heighway J, Venzke DP, Lee JC, Campbell KP | title = Sarcospan, the 25-kDa transmembrane component of the dystrophin-glycoprotein complex | journal = The Journal of Biological Chemistry | volume = 272 | issue = 50 | pages = 31221–4 | date = December 1997 | pmid = 9395445 | doi = 10.1074/jbc.272.50.31221 }}</ref>    Loss of SSPN expression occurs in patients with [[Duchenne muscular dystrophy]]. [[Dystrophin]] is required for proper localization of SSPN.<ref name="crosbie"/>  SSPN is also an essential regulator of Akt signaling pathways. Without SSPN, Akt signaling pathways will be hindered and muscle regeneration will not occur.<ref name="watson">{{cite journal | vauthors = Marshall JL, Crosbie-Watson RH | title = Sarcospan: a small protein with large potential for Duchenne muscular dystrophy | journal = Skeletal Muscle | volume = 3 | issue = 1 | pages = 1 | date = January 2013 | pmid = 23282144 | doi = 10.1186/2044-5040-3-1 }}</ref>


==Sarcospan in Muscular Dystrophy ==
==Sarcospan in Muscular Dystrophy ==
The loss of dystrophin results in muscular dystrophy.<ref name="Peter">{{cite journal|last1=Peter|first1=Angela K.|last2=Marshall|first2=Jamie L.|last3=Crosbie|first3=Rachelle H.|title=Sarcospan reduces dystrophic pathology: stabilization of the utrophin–glycoprotein complex|journal=The Journal of Cell Biology|date=3 November 2008|volume=183|issue=3|pages=419–427|doi=10.1083/jcb.200808027|pmid=18981229|pmc=2575773}}</ref> SSPN upregulates the levels of Utrophin-glycoprotein complex (UGC) to make up for the loss of dystrophin in the neuromuscular junction.<ref name="Peter"/> Sarcoglycans bind to SSPN and form the SG-SSPN complex, which interacts with dystroglycans (DG) and Utrophin leading to the formation of the UGC.<ref name="Marshall">{{cite journal|last1=Marshall|first1=J. L.|last2=Oh|first2=J.|last3=Chou|first3=E.|last4=Lee|first4=J. A.|last5=Holmberg|first5=J.|last6=Burkin|first6=D. J.|last7=Crosbie-Watson|first7=R. H.|title=Sarcospan integration into laminin-binding adhesion complexes that ameliorate muscular dystrophy requires utrophin and 7 integrin|journal=Human Molecular Genetics|date=11 December 2014|volume=24|issue=7|pages=2011–2022|doi=10.1093/hmg/ddu615|pmid=25504048|pmc=4355028}}</ref>  SSPN regulates the amount of Utrophin produced by the UGC to restore laminin binding due to the absence of dystrophin.<ref name="holmberg">{{cite journal|last1=Marshall|first1=Jamie L.|last2=Holmberg|first2=Johan|last3=Chou|first3=Eric|last4=Ocampo|first4=Amber C.|last5=Oh|first5=Jennifer|last6=Lee|first6=Joy|last7=Peter|first7=Angela K.|last8=Martin|first8=Paul T.|last9=Crosbie-Watson|first9=Rachelle H.|title=Sarcospan-dependent Akt activation is required for utrophin expression and muscle regeneration|journal=The Journal of Cell Biology|date=25 June 2012|volume=197|issue=7|pages=1009–1027|doi=10.1083/jcb.201110032|pmid=22734004|pmc=3384411}}</ref>  If laminin binding is not restored by SSPN, contraction of the membrane is present.<ref name="holmberg"/>  In dystrophic mdx mice, SSPN increases levels of Utrophin and restores the levels of laminin binding, reducing the symptoms of muscular dystrophy <ref name="holmberg"/>
The loss of dystrophin results in muscular dystrophy.<ref name="Peter">{{cite journal | vauthors = Peter AK, Marshall JL, Crosbie RH | title = Sarcospan reduces dystrophic pathology: stabilization of the utrophin-glycoprotein complex | journal = The Journal of Cell Biology | volume = 183 | issue = 3 | pages = 419–27 | date = November 2008 | pmid = 18981229 | pmc = 2575773 | doi = 10.1083/jcb.200808027 }}</ref> SSPN upregulates the levels of Utrophin-glycoprotein complex (UGC) to make up for the loss of dystrophin in the neuromuscular junction.<ref name="Peter"/> Sarcoglycans bind to SSPN and form the SG-SSPN complex, which interacts with dystroglycans (DG) and Utrophin leading to the formation of the UGC.<ref name="Marshall">{{cite journal | vauthors = Marshall JL, Oh J, Chou E, Lee JA, Holmberg J, Burkin DJ, Crosbie-Watson RH | title = Sarcospan integration into laminin-binding adhesion complexes that ameliorate muscular dystrophy requires utrophin and α7 integrin | journal = Human Molecular Genetics | volume = 24 | issue = 7 | pages = 2011–22 | date = April 2015 | pmid = 25504048 | pmc = 4355028 | doi = 10.1093/hmg/ddu615 }}</ref>  SSPN regulates the amount of Utrophin produced by the UGC to restore laminin binding due to the absence of dystrophin.<ref name="holmberg">{{cite journal | vauthors = Marshall JL, Holmberg J, Chou E, Ocampo AC, Oh J, Lee J, Peter AK, Martin PT, Crosbie-Watson RH | title = Sarcospan-dependent Akt activation is required for utrophin expression and muscle regeneration | journal = The Journal of Cell Biology | volume = 197 | issue = 7 | pages = 1009–27 | date = June 2012 | pmid = 22734004 | pmc = 3384411 | doi = 10.1083/jcb.201110032 }}</ref>  If laminin binding is not restored by SSPN, contraction of the membrane is present.<ref name="holmberg"/>  In dystrophic mdx mice, SSPN increases levels of Utrophin and restores the levels of laminin binding, reducing the symptoms of muscular dystrophy <ref name="holmberg"/>


==References==
== References ==
<references/>
{{Reflist|32em}}


==External links==
== External links ==
* {{MeshName|Sarcospan}}
* {{MeshName|Sarcospan}}


{{Muscle tissue}}
{{Muscle tissue}}


{{cell-biology-stub}}
{{cell-biology-stub}}
{{gene-12-stub}}
{{gene-12-stub}}

Latest revision as of 20:53, 6 February 2018

sarcospan
Identifiers
SymbolSSPN
Entrez8082
HUGO11322
OMIM601599
Other data
LocusChr. 12 p11.2

Originally identified as Kirsten ras associated gene (krag),[1] Sarcospan (SSPN) (is a 25-kDa transmembrane protein located in the dystrophin-associated protein complex of skeletal muscle cells, where it is most abundant.[1] It contains four transmembrane spanning helices with both N- and C-terminal domains located intracellularly.[2] Loss of SSPN expression occurs in patients with Duchenne muscular dystrophy. Dystrophin is required for proper localization of SSPN.[2] SSPN is also an essential regulator of Akt signaling pathways. Without SSPN, Akt signaling pathways will be hindered and muscle regeneration will not occur.[1]

Sarcospan in Muscular Dystrophy

The loss of dystrophin results in muscular dystrophy.[3] SSPN upregulates the levels of Utrophin-glycoprotein complex (UGC) to make up for the loss of dystrophin in the neuromuscular junction.[3] Sarcoglycans bind to SSPN and form the SG-SSPN complex, which interacts with dystroglycans (DG) and Utrophin leading to the formation of the UGC.[4] SSPN regulates the amount of Utrophin produced by the UGC to restore laminin binding due to the absence of dystrophin.[5] If laminin binding is not restored by SSPN, contraction of the membrane is present.[5] In dystrophic mdx mice, SSPN increases levels of Utrophin and restores the levels of laminin binding, reducing the symptoms of muscular dystrophy [5]

References

  1. ↑ 1.0 1.1 1.2 Marshall JL, Crosbie-Watson RH (January 2013). "Sarcospan: a small protein with large potential for Duchenne muscular dystrophy". Skeletal Muscle. 3 (1): 1. doi:10.1186/2044-5040-3-1. PMID 23282144.
  2. ↑ 2.0 2.1 Crosbie RH, Heighway J, Venzke DP, Lee JC, Campbell KP (December 1997). "Sarcospan, the 25-kDa transmembrane component of the dystrophin-glycoprotein complex". The Journal of Biological Chemistry. 272 (50): 31221–4. doi:10.1074/jbc.272.50.31221. PMID 9395445.
  3. ↑ 3.0 3.1 Peter AK, Marshall JL, Crosbie RH (November 2008). "Sarcospan reduces dystrophic pathology: stabilization of the utrophin-glycoprotein complex". The Journal of Cell Biology. 183 (3): 419–27. doi:10.1083/jcb.200808027. PMC 2575773. PMID 18981229.
  4. ↑ Marshall JL, Oh J, Chou E, Lee JA, Holmberg J, Burkin DJ, Crosbie-Watson RH (April 2015). "Sarcospan integration into laminin-binding adhesion complexes that ameliorate muscular dystrophy requires utrophin and α7 integrin". Human Molecular Genetics. 24 (7): 2011–22. doi:10.1093/hmg/ddu615. PMC 4355028. PMID 25504048.
  5. ↑ 5.0 5.1 5.2 Marshall JL, Holmberg J, Chou E, Ocampo AC, Oh J, Lee J, Peter AK, Martin PT, Crosbie-Watson RH (June 2012). "Sarcospan-dependent Akt activation is required for utrophin expression and muscle regeneration". The Journal of Cell Biology. 197 (7): 1009–27. doi:10.1083/jcb.201110032. PMC 3384411. PMID 22734004.

External links

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