The Structural and Functional Characteristics of the Motor End Plates of Dysferlin-Deficient Mice

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The Structural and Functional Characteristics of the Motor End Plates of Dysferlin-Deficient Mice. / Kravtsova, V. V.; Timonina, N. A.; Zakir'yanova, G. F.; Sokolova, A. V.; Mikhailov, V. M.; Zefirov, A. L.; Krivoi, I. I.

In: Neurochemical Journal, Vol. 12, No. 4, 305–310, 10.2018, p. 305-310.

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

Author

Kravtsova, V. V. ; Timonina, N. A. ; Zakir'yanova, G. F. ; Sokolova, A. V. ; Mikhailov, V. M. ; Zefirov, A. L. ; Krivoi, I. I. / The Structural and Functional Characteristics of the Motor End Plates of Dysferlin-Deficient Mice. In: Neurochemical Journal. 2018 ; Vol. 12, No. 4. pp. 305-310.

BibTeX

@article{b4dfb0c37c7046e8b0e617f38a47a2f9,

title = "The Structural and Functional Characteristics of the Motor End Plates of Dysferlin-Deficient Mice",

abstract = "The molecular mechanisms that underlie neuromuscular junction plasticity are complex and remain to be fully elucidated. Experimental models of various forms of impaired motor activity may be promising for their study. The dysferlin protein plays a key role in the multimolecular complex, which maintains sarcolemma integrity and the functioning of skeletal muscle cells. We studied the structural and functional characteristics of the diaphragm muscle motor end plates of dysferlin-deficient Bla/J mice (a model of dysferlinopathy), dystrophin-deficient mdx mice (a model of Duchenne muscular dystrophy), and control C57Bl/6 mice. Increased end plate fragmentation and a decrease in the area of individual fragments were observed in mdx mice and absent in Bla/J mice, which indicates a difference in these models of myodystrophy from these characteristics. However, end plates of both mice lines were characterized by a decrease in the density of distribution of nicotinic acetylcholine receptors, as well as by membrane depolarization, presumably, due to altered functional interaction between the 2 isoform of Na,K-ATPase and the nicotinic acetylcholine receptors.",

keywords = "skeletal muscle, motor endplate, nicotinic acetylcholine receptors, dysferlin, dysferlinopathy, SKELETAL-MUSCLE, NEUROMUSCULAR-JUNCTION, MUSCULAR-DYSTROPHY, SAFETY FACTOR, MECHANISMS, AUTOPHAGY, ELECTROGENESIS",

author = "Kravtsova, {V. V.} and Timonina, {N. A.} and Zakir'yanova, {G. F.} and Sokolova, {A. V.} and Mikhailov, {V. M.} and Zefirov, {A. L.} and Krivoi, {I. I.}",

year = "2018",

month = oct,

doi = "10.1134/S1819712418040049",

language = "Английский",

volume = "12",

pages = "305--310",

journal = "Neurochemical Journal",

issn = "1819-7124",

publisher = "МАИК {"}Наука/Интерпериодика{"}",

number = "4",

}

RIS

TY - JOUR

T1 - The Structural and Functional Characteristics of the Motor End Plates of Dysferlin-Deficient Mice

AU - Kravtsova, V. V.

AU - Timonina, N. A.

AU - Zakir'yanova, G. F.

AU - Sokolova, A. V.

AU - Mikhailov, V. M.

AU - Zefirov, A. L.

AU - Krivoi, I. I.

PY - 2018/10

Y1 - 2018/10

N2 - The molecular mechanisms that underlie neuromuscular junction plasticity are complex and remain to be fully elucidated. Experimental models of various forms of impaired motor activity may be promising for their study. The dysferlin protein plays a key role in the multimolecular complex, which maintains sarcolemma integrity and the functioning of skeletal muscle cells. We studied the structural and functional characteristics of the diaphragm muscle motor end plates of dysferlin-deficient Bla/J mice (a model of dysferlinopathy), dystrophin-deficient mdx mice (a model of Duchenne muscular dystrophy), and control C57Bl/6 mice. Increased end plate fragmentation and a decrease in the area of individual fragments were observed in mdx mice and absent in Bla/J mice, which indicates a difference in these models of myodystrophy from these characteristics. However, end plates of both mice lines were characterized by a decrease in the density of distribution of nicotinic acetylcholine receptors, as well as by membrane depolarization, presumably, due to altered functional interaction between the 2 isoform of Na,K-ATPase and the nicotinic acetylcholine receptors.

AB - The molecular mechanisms that underlie neuromuscular junction plasticity are complex and remain to be fully elucidated. Experimental models of various forms of impaired motor activity may be promising for their study. The dysferlin protein plays a key role in the multimolecular complex, which maintains sarcolemma integrity and the functioning of skeletal muscle cells. We studied the structural and functional characteristics of the diaphragm muscle motor end plates of dysferlin-deficient Bla/J mice (a model of dysferlinopathy), dystrophin-deficient mdx mice (a model of Duchenne muscular dystrophy), and control C57Bl/6 mice. Increased end plate fragmentation and a decrease in the area of individual fragments were observed in mdx mice and absent in Bla/J mice, which indicates a difference in these models of myodystrophy from these characteristics. However, end plates of both mice lines were characterized by a decrease in the density of distribution of nicotinic acetylcholine receptors, as well as by membrane depolarization, presumably, due to altered functional interaction between the 2 isoform of Na,K-ATPase and the nicotinic acetylcholine receptors.

KW - skeletal muscle

KW - motor endplate

KW - nicotinic acetylcholine receptors

KW - dysferlin

KW - dysferlinopathy

KW - SKELETAL-MUSCLE

KW - NEUROMUSCULAR-JUNCTION

KW - MUSCULAR-DYSTROPHY

KW - SAFETY FACTOR

KW - MECHANISMS

KW - AUTOPHAGY

KW - ELECTROGENESIS

U2 - 10.1134/S1819712418040049

DO - 10.1134/S1819712418040049

M3 - статья

VL - 12

SP - 305

EP - 310

JO - Neurochemical Journal

JF - Neurochemical Journal

SN - 1819-7124

IS - 4

M1 - 305–310

ER -

ID: 35109200