Abnormal Membrane Localization of α2 Isoform of Na,K-ATPase in m. soleus of Dysferlin-Deficient Mice

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Abnormal Membrane Localization of α2 Isoform of Na,K-ATPase in m. soleus of Dysferlin-Deficient Mice. / Kravtsova, V.V.; Bouzinova, E.V.; Matchkov , V.V.; Timonina, N.A.; Zakyrjanova, G.F.; Zefirov, A.L.; Krivoi, I.I.

In: Bulletin of Experimental Biology and Medicine, Vol. 166, No. 5, 2019, p. 593-597.

Research output: Contribution to journal › Article › peer-review

Author

Kravtsova, V.V. ; Bouzinova, E.V. ; Matchkov , V.V. ; Timonina, N.A. ; Zakyrjanova, G.F. ; Zefirov, A.L. ; Krivoi, I.I. / Abnormal Membrane Localization of α2 Isoform of Na,K-ATPase in m. soleus of Dysferlin-Deficient Mice. In: Bulletin of Experimental Biology and Medicine. 2019 ; Vol. 166, No. 5. pp. 593-597.

BibTeX

@article{2654d2a58cb44d85b20634faf77fdf87,

title = "Abnormal Membrane Localization of α2 Isoform of Na,K-ATPase in m. soleus of Dysferlin-Deficient Mice",

abstract = "Dysferlin protein plays a key role in the multimolecular complex responsible for the maintenance of sarcolemma integrity and skeletal muscle cell functioning. We studied the membrane distribution of nicotinic acetylcholine receptors and α2 isoform of Na,K-ATPase in motor endplates of m. soleus in dysferlin-deficient Bla/J mice (a dysferlinopathy model). Endplates of Bla/J mice were characterized by increased area (without changes in fragmentation degree) and reduced density of the membrane distribution of nicotinic acetylcholine receptors in comparison with the corresponding parameters in control С57Bl/6 mice. The density of the membrane distribution of α2 isoform of Na,K-ATPase was also reduced, but the level of the corresponding mRNA remained unchanged. It can be hypothesized that abnormal membrane localization of α2 isoform of Na,K-ATPase results from adaptive skeletal muscle remodeling under conditions of chronic motor dysfunction.",

keywords = "Na,K-ATPase isoforms, acetylcholine receptors, dysferlin, dysferlinopathy, nicotinic, skeletal muscle",

author = "V.V. Kravtsova and E.V. Bouzinova and V.V. Matchkov and N.A. Timonina and G.F. Zakyrjanova and A.L. Zefirov and I.I. Krivoi",

note = "Kravtsova, V.V., Bouzinova, E.V., Machkov, V.V. et al. Bull Exp Biol Med (2019) 166: 593. https://doi.org/10.1007/s10517-019-04398-z",

year = "2019",

doi = "10.1007/s10517-019-04398-z",

language = "English",

volume = "166",

pages = "593--597",

journal = "Bulletin of Experimental Biology and Medicine",

issn = "0007-4888",

publisher = "Springer Nature",

number = "5",

}

RIS

TY - JOUR

T1 - Abnormal Membrane Localization of α2 Isoform of Na,K-ATPase in m. soleus of Dysferlin-Deficient Mice

AU - Kravtsova, V.V.

AU - Bouzinova, E.V.

AU - Matchkov , V.V.

AU - Timonina, N.A.

AU - Zakyrjanova, G.F.

AU - Zefirov, A.L.

AU - Krivoi, I.I.

N1 - Kravtsova, V.V., Bouzinova, E.V., Machkov, V.V. et al. Bull Exp Biol Med (2019) 166: 593. https://doi.org/10.1007/s10517-019-04398-z

PY - 2019

Y1 - 2019

N2 - Dysferlin protein plays a key role in the multimolecular complex responsible for the maintenance of sarcolemma integrity and skeletal muscle cell functioning. We studied the membrane distribution of nicotinic acetylcholine receptors and α2 isoform of Na,K-ATPase in motor endplates of m. soleus in dysferlin-deficient Bla/J mice (a dysferlinopathy model). Endplates of Bla/J mice were characterized by increased area (without changes in fragmentation degree) and reduced density of the membrane distribution of nicotinic acetylcholine receptors in comparison with the corresponding parameters in control С57Bl/6 mice. The density of the membrane distribution of α2 isoform of Na,K-ATPase was also reduced, but the level of the corresponding mRNA remained unchanged. It can be hypothesized that abnormal membrane localization of α2 isoform of Na,K-ATPase results from adaptive skeletal muscle remodeling under conditions of chronic motor dysfunction.

AB - Dysferlin protein plays a key role in the multimolecular complex responsible for the maintenance of sarcolemma integrity and skeletal muscle cell functioning. We studied the membrane distribution of nicotinic acetylcholine receptors and α2 isoform of Na,K-ATPase in motor endplates of m. soleus in dysferlin-deficient Bla/J mice (a dysferlinopathy model). Endplates of Bla/J mice were characterized by increased area (without changes in fragmentation degree) and reduced density of the membrane distribution of nicotinic acetylcholine receptors in comparison with the corresponding parameters in control С57Bl/6 mice. The density of the membrane distribution of α2 isoform of Na,K-ATPase was also reduced, but the level of the corresponding mRNA remained unchanged. It can be hypothesized that abnormal membrane localization of α2 isoform of Na,K-ATPase results from adaptive skeletal muscle remodeling under conditions of chronic motor dysfunction.

KW - Na,K-ATPase isoforms

KW - acetylcholine receptors

KW - dysferlin

KW - dysferlinopathy

KW - nicotinic

KW - skeletal muscle

UR - http://www.scopus.com/inward/record.url?scp=85063717331&partnerID=8YFLogxK

UR - http://www.mendeley.com/research/abnormal-membrane-localization-%CE%B12-isoform-nakatpase-m-soleus-dysferlindeficient-mice

U2 - 10.1007/s10517-019-04398-z

DO - 10.1007/s10517-019-04398-z

M3 - Article

VL - 166

SP - 593

EP - 597

JO - Bulletin of Experimental Biology and Medicine

JF - Bulletin of Experimental Biology and Medicine

SN - 0007-4888

IS - 5

ER -

ID: 45289906