#PAGE_PARAMS# #ADS_HEAD_SCRIPTS# #MICRODATA#

α-Actinin-3: Why Gene Loss Is an Evolutionary Gain


article has not abstract


Vyšlo v časopise: α-Actinin-3: Why Gene Loss Is an Evolutionary Gain. PLoS Genet 11(1): e32767. doi:10.1371/journal.pgen.1004908
Kategorie: Perspective
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.pgen.1004908

Souhrn

article has not abstract


Zdroje

1. Danecek P, Auton A, Abecasis G, Albers CA, Banks E, et al. (2011) The variant call format and VCFtools. Bioinformatics 27: 2156–2158. doi: 10.1093/bioinformatics/btr330 21653522

2. Head SI, Chan S, Houweling PJ, Quinlan KGR, Murphy R, et al. (2015) Altered Ca2+ kinetics associated with α-actinin-3 deficiency may explain positive selection for ACTN3 null allele in human evolution. PLoS Genet 11: e1004862.

3. North KN, Beggs AH (1996) Deficiency of a skeletal muscle isoform of alpha-actinin (alpha-actinin-3) in merosin-positive congenital muscular dystrophy. Neuromuscul Disord 6: 229–235. doi: 10.1016/0960-8966(96)00361-6 8887951

4. MacArthur DG, Seto JT, Raftery JM, Quinlan KG, Huttley GA, et al. (2007) Loss of ACTN3 gene function alters mouse muscle metabolism and shows evidence of positive selection in humans. Nat Genet 39: 1261–1265. doi: 10.1038/ng2122 17828264

5. Friedlander SM, Herrmann AL, Lowry DP, Mepham ER, Lek M, et al. (2013) ACTN3 allele frequency in humans covaries with global latitudinal gradient. PLoS ONE 8: e52282. doi: 10.1371/journal.pone.0052282 23359641

6. Vincent B, De Bock K, Ramaekers M, Van den Eede E, Van Leemputte M, et al. (2007) ACTN3 (R577X) genotype is associated with fiber type distribution. Physiol Genomics 32: 58–63. doi: 10.1152/physiolgenomics.00173.2007 17848603

7. Bruton JD, Aydin J, Yamada T, Shabalina IG, Ivarsson N, et al. (2010) Increased fatigue resistance linked to Ca2+-stimulated mitochondrial biogenesis in muscle fibres of cold-acclimated mice. J Physiol 588: 4275–4288. doi: 10.1113/jphysiol.2010.198598 20837639

8. Mills M, Yang N, Weinberger R, Vander Woude DL, Beggs AH, et al. (2001) Differential expression of the actin-binding proteins, alpha-actinin-2 and -3, in different species: implications for the evolution of functional redundancy. Hum Mol Genet 10: 1335–1346. doi: 10.1093/hmg/10.13.1335 11440986

9. Tonkonogi M, Harris B, Sahlin K (1997) Increased activity of citrate synthase in human skeletal muscle after a single bout of prolonged exercise. Acta Physiol Scand 161: 435–436. doi: 10.1046/j.1365-201X.1997.00233.x 9401597

10. Seto JT, Quinlan KG, Lek M, Zheng XF, Garton F, et al. (2013) ACTN3 genotype influences muscle performance through the regulation of calcineurin signaling. J Clin Invest 123: 4255–4263. doi: 10.1172/JCI67691 24091322

11. Tavi P, Westerblad H (2011) The role of in vivo Ca2+ signals acting on Ca2+–calmodulin-dependent proteins for skeletal muscle plasticity. J Physiol 589: 5021–5031. doi: 10.1113/jphysiol.2011.212860 21911615

12. Wright DC, Geiger PC, Han DH, Jones TE, Holloszy JO (2007) Calcium induces increases in peroxisome proliferator-activated receptor gamma coactivator-1alpha and mitochondrial biogenesis by a pathway leading to p38 mitogen-activated protein kinase activation. J Biol Chem 282: 18793–18799. doi: 10.1074/jbc.M611252200 17488713

13. Wu Z, Puigserver P, Andersson U, Zhang C, Adelmant G, et al. (1999) Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1. Cell 98: 115–124. doi: 10.1016/S0092-8674(00)80611-X 10412986

14. Arany Z (2008) PGC-1 coactivators and skeletal muscle adaptations in health and disease. Curr Opin Genet Dev 18: 426–434. doi: 10.1016/j.gde.2008.07.018 18782618

15. Cannon B, Nedergaard J (2011) Nonshivering thermogenesis and its adequate measurement in metabolic studies. J Exp Biol 214: 242–253. doi: 10.1242/jeb.050989 21177944

16. Murphy RM, Larkins NT, Mollica JP, Beard NA, Lamb GD (2009) Calsequestrin content and SERCA determine normal and maximal Ca2+ storage levels in sarcoplasmic reticulum of fast- and slow-twitch fibres of rat. J Physiol 587: 443–460. doi: 10.1113/jphysiol.2008.163162 19029185

17. Bellinger AM, Reiken S, Dura M, Murphy PW, Deng SX, et al. (2008) Remodeling of ryanodine receptor complex causes “leaky” channels: a molecular mechanism for decreased exercise capacity. PNAS 105: 2198–2202. doi: 10.1073/pnas.0711074105 18268335

18. Bellinger AM, Reiken S, Carlson C, Mongillo M, Liu X, et al. (2009) Hypernitrosylated ryanodine receptor calcium release channels are leaky in dystrophic muscle. Nat Med 15: 325–330. doi: 10.1038/nm.1916 19198614

19. Andersson DC, Betzenhauser MJ, Reiken S, Meli AC, Umanskaya A, et al. (2011) Ryanodine receptor oxidation causes intracellular calcium leak and muscle weakness in aging. Cell Metab 14: 196–207. doi: 10.1016/j.cmet.2011.05.014 21803290

20. Aydin J, Shabalina IG, Place N, Reiken S, Zhang SJ, et al. (2008) Nonshivering thermogenesis protects against defective calcium handling in muscle. FASEB J 22: 3919–3924. doi: 10.1096/fj.08-113712 18687806

Štítky
Genetika Reprodukčná medicína

Článok vyšiel v časopise

PLOS Genetics


2015 Číslo 1
Najčítanejšie tento týždeň
Najčítanejšie v tomto čísle
Kurzy

Zvýšte si kvalifikáciu online z pohodlia domova

Aktuální možnosti diagnostiky a léčby litiáz
nový kurz
Autori: MUDr. Tomáš Ürge, PhD.

Všetky kurzy
Prihlásenie
Zabudnuté heslo

Zadajte e-mailovú adresu, s ktorou ste vytvárali účet. Budú Vám na ňu zasielané informácie k nastaveniu nového hesla.

Prihlásenie

Nemáte účet?  Registrujte sa

#ADS_BOTTOM_SCRIPTS#