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Mitogen-activated protein kinase-activated protein kinase 2 (MK2) in skeletal muscle atrophy and hypertrophy
Linnéuniversitetet, Fakultetsnämnden för naturvetenskap och teknik, Institutionen för naturvetenskap, NV.
Linnéuniversitetet, Fakultetsnämnden för naturvetenskap och teknik, Institutionen för naturvetenskap, NV.
2010 (engelsk)Inngår i: Journal of Cellular Physiology, ISSN 0021-9541, E-ISSN 1097-4652, Vol. 223, nr 1, s. 194-201Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Skeletal muscle is a highly plastic tissue. Overall muscle growth (hypertrophy) or muscle wasting (atrophy) results from alterations in intracellular signaling pathways with important regulatory steps occurring in the nucleus as well as in the cytoplasm. Previous studies have identified components of the Akt/mTor pathway as well as the p38 MAPK pathway as important for skeletal muscle hypertrophy and/or atrophy. The present study tests the hypothesis that MK2, a substrate of p38 which following phosphorylation, can be exported from the nucleus in a complex with p38, may be important for skeletal muscle growth. The expression of MK2 was examined in denervated mouse hind-limb (atrophic) and hemidiaphragm (transiently hypertrophic) muscles. MK2 mRNA expression decreased after denervation in both atrophic (48% of innervated controls, P < 0.001) and hypertrophic muscle (34% of innervated controls, P < 0.01) but MK2 protein expression decreased only in atrophic muscle (32% of innervated controls, P < 0.01). The level of T205 phosphorylated MK2 increased after denervation in both atrophic (fourfold increase, P < 0.01) and hypertrophic muscles (almost sevenfold increase, P < 0.001) whereas the level of T317 phosphorylated MK2 (necessary for nuclear export) increased after denervation in hypertrophic muscle (nearly threefold increase, P < 0.001) but not in atrophic muscle. Logarithmically transformed relative changes in MK2 phosphorylated at T317 correlated well (r2 = 0.7737) with relative changes in muscle weight. The results suggest a role for MK2 in the regulation of muscle mass, a role which, at least in part, may be related to determining the subcellular localization of p38 in muscle fibers. J. Cell. Physiol. 223: 194–201,

sted, utgiver, år, opplag, sider
Wiley-Liss, Inc. , 2010. Vol. 223, nr 1, s. 194-201
HSV kategori
Forskningsprogram
Biomedicinsk vetenskap, Farmakologi; Naturvetenskap, Biomedicinsk vetenskap
Identifikatorer
URN: urn:nbn:se:lnu:diva-2134DOI: 10.1002/jcp.22023OAI: oai:DiVA.org:lnu-2134DiVA, id: diva2:309184
Tilgjengelig fra: 2010-04-06 Laget: 2010-04-06 Sist oppdatert: 2018-01-12bibliografisk kontrollert
Inngår i avhandling
1. Gene and protein expression in denervated atrophic and hypertrophic skeletal muscle
Åpne denne publikasjonen i ny fane eller vindu >>Gene and protein expression in denervated atrophic and hypertrophic skeletal muscle
2011 (engelsk)Doktoravhandling, med artikler (Annet vitenskapelig)
Abstract [en]

Following denervation skeletal muscles change their functional and structural properties. Some changes resemble conditions in developing muscles and may be important for reinnervation. Due to inactivity following denervation most skeletal muscles loose muscle mass and become atrophic. The hemidiaphragm muscle, however, undergoes a phase of transient hypertrophy following denervation, gaining weight during the first 6-10 days followed by a decrease in weight. In this thesis the expression (mRNA, protein and protein phosphorylations) of potential factors involved in the regulation of muscle mass were examined in denervated hind-limb and hemidiaphragm muscles.

NIFK is a protein that associates with Ki67, a protein expressed predominantly in proliferating cells. The mRNA expression of NIFK was upregulated in denervated atrophic muscles but unaltered in denervated hypertrophic muscles, suggesting a potential role in the regulation of skeletal muscle mass (Paper I). p38 MAPK has previously been implicated in both anabolic and catabolic processes. Its substrate MK2 becomes phosphorylated at two sites, one of which is suggested to be important for nuclear export. MK2 phosphorylation at this site correlated with muscle weight in both atrophic and hypertrophic denervated muscles and may thus have a role in atrophy and hypertrophy (Paper III). Factors regulating protein synthesis are likely to play a role in atrophy and hypertrophy and many signaling pathways appear to converge on the formation of the translation initiation complex. The protein expression and phosphorylation status of several components in both Wnt and Akt signaling pathways indicate increased protein synthesis in denervated atrophic muscles as well as in denervated hypertrophic muscles (Papers II, IV and V). This suggests that increased protein degradation is more important than decreased protein synthesis for the loss of muscle mass in denervated atrophic muscles.

sted, utgiver, år, opplag, sider
Växjö, Kalmar: Linnaeus University Press, 2011
Serie
Linnaeus University Dissertations ; 34/2011
Emneord
Skeletal muscle, Denervation, Hypertrophy, Atrophy, Gene expression, Protein expression, Protein phosphorylation, NIFK, Wnt, MK2, Akt signaling
HSV kategori
Identifikatorer
urn:nbn:se:lnu:diva-10411 (URN)978-91-86491-61-1 (ISBN)
Disputas
2011-03-11, N2007, Smålandsgatan 24, Kalmar, 09:00 (svensk)
Veileder
Tilgjengelig fra: 2011-01-31 Laget: 2011-01-28 Sist oppdatert: 2014-05-09bibliografisk kontrollert

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