Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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.
в: Bulletin of Experimental Biology and Medicine, Том 166, № 5, 2019, стр. 593-597.Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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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