User talk:Kab23
Welcome!
[edit]Hello, Kab23, and welcome to Wikipedia! My name is Ian and I work with the Wiki Education Foundation; I help support students who are editing as part of a class assignment.
I hope you enjoy editing here. If you haven't already done so, please check out the student training library, which introduces you to editing and Wikipedia's core principles. You may also want to check out the Teahouse, a community of Wikipedia editors dedicated to helping new users. Below are some resources to help you get started editing.
Handouts
|
|---|
Additional Resources
|
|
If you have any questions, please don't hesitate to contact me on my talk page. Ian (Wiki Ed) (talk) 00:03, 1 October 2016 (UTC)
Article I want to critique
[edit] | This article is written like a personal reflection, personal essay, or argumentative essay that states a Wikipedia editor's personal feelings or presents an original argument about a topic. (July 2008) |
| sarcospan | |
|---|---|
| Identifiers | |
| Symbol | SSPN |
| NCBI gene | 8082 |
| HGNC | 11322 |
| OMIM | 601599 |
| Other data | |
| Locus | Chr. 12 p11.2 |
Sarcospan, discovered by the research group of Kevin Campbell, is a 25-kDa transmembrane protein located in the dystrophin-associated protein complex of skeletal muscle cells. It contains four transmembrane spanning helices with both N- and C-terminal domains located intracellularly.[1] Loss of sarcospan expression occurs in patients with Duchenne muscular dystrophy, indicating that dystrophin is required for proper localization of sarcospan.[1] Sarcospan knockout mice exhibit normal muscle structure and function, indicating that sarcospan is not necessary for muscle to develop.[2].
References
[edit]- ^ a b Crosbie; Heighway, J; Venzke, DP; Lee, JC; Campbell, KP; et al. (1997). "Sarcospan, the 25-kDa transmembrane component of the dystrophin-glycoprotein complex". J Biol Chem. 272 (50): 31221–4. doi:10.1074/jbc.272.50.31221. PMID 9395445.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Lebakken; Venzke, DP; Hrstka, RF; Consolino, CM; Faulkner, JA; Williamson, RA; Campbell, KP; et al. (2000). "Sarcospan-deficient mice maintain normal muscle function". Mol Cell Biol. 20 (5): 1669–77. doi:10.1128/MCB.20.5.1669-1677.2000. PMC 85350. PMID 10669744.
External links
[edit]- Sarcospan at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
 | This cell biology article is a stub. You can help Wikipedia by expanding it. |
 | This article on a gene on human chromosome 12 is a stub. You can help Wikipedia by expanding it. |
Article Critique
[edit]In critiquing Sarcospan, I will remove 'discovered by the research group of kevin campbell' in attempt to make the article more encyclopedic style. I will add an image for sarcospan in mice and elaborate. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3599653/ https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4355028/ http://eds.b.ebscohost.com.webdb.plattsburgh.edu:2048/eds/pdfviewer/pdfviewer?sid=a7319ad1-f4b3-43c1-96a6-7ffe75c8dcb6%40sessionmgr107&vid=0&hid=126
actual critique
[edit]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
[edit]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]
November 2016
[edit]
Hello, and thank you for your contributions to Wikipedia. I've noticed that you have been adding your signature to some of your edits to articles. This is a common mistake to make and has probably already been corrected. Please do not sign your edits to article content, as the article's edit history serves the function of attributing contributions, so you only need to use your signature to make discussions more readable, such as on article talk pages or project pages such as the Village Pump. If you would like further information about distinguishing types of pages, please see What is an article? Again, thank you for contributing, and enjoy your Wikipedia experience! Thank you. Jac16888 Talk 13:51, 13 November 2016 (UTC)
- ^ a b c Marshall, Jamie L; Crosbie-Watson, Rachelle H (2013). "Sarcospan: a small protein with large potential for Duchenne muscular dystrophy". Skeletal Muscle. 3 (1): 1. doi:10.1186/2044-5040-3-1.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ a b Crosbie; Heighway, J; Venzke, DP; Lee, JC; Campbell, KP; et al. (1997). "Sarcospan, the 25-kDa transmembrane component of the dystrophin-glycoprotein complex". J Biol Chem. 272 (50): 31221–4. doi:10.1074/jbc.272.50.31221. PMID 9395445.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ a b Peter, Angela K.; Marshall, Jamie L.; Crosbie, Rachelle H. (3 November 2008). "Sarcospan reduces dystrophic pathology: stabilization of the utrophin–glycoprotein complex". The Journal of Cell Biology. 183 (3): 419–427. doi:10.1083/jcb.200808027.
- ^ Marshall, J. L.; Oh, J.; Chou, E.; Lee, J. A.; Holmberg, J.; Burkin, D. J.; Crosbie-Watson, R. H. (11 December 2014). "Sarcospan integration into laminin-binding adhesion complexes that ameliorate muscular dystrophy requires utrophin and 7 integrin". Human Molecular Genetics. 24 (7): 2011–2022. doi:10.1093/hmg/ddu615.
{{cite journal}}: no-break space character in|title=at position 120 (help) - ^ a b c Marshall, Jamie L.; Holmberg, Johan; Chou, Eric; Ocampo, Amber C.; Oh, Jennifer; Lee, Joy; Peter, Angela K.; Martin, Paul T.; Crosbie-Watson, Rachelle H. (25 June 2012). "Sarcospan-dependent Akt activation is required for utrophin expression and muscle regeneration". The Journal of Cell Biology. 197 (7): 1009–1027. doi:10.1083/jcb.201110032.