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Molecular Cloning of Synucleins in River Lamprey Lampetra fluviatilis. / Vorontsova, O. V.; Akkuratov, E. E.; Korenkova, O. M.; Shupliakov, O.

In: Biochemistry (Moscow) Supplement Series A: Membrane and Cell Biology, Vol. 12, No. 3, 01.07.2018, p. 278-286.

Research output: Contribution to journalArticlepeer-review

Harvard

Vorontsova, OV, Akkuratov, EE, Korenkova, OM & Shupliakov, O 2018, 'Molecular Cloning of Synucleins in River Lamprey Lampetra fluviatilis', Biochemistry (Moscow) Supplement Series A: Membrane and Cell Biology, vol. 12, no. 3, pp. 278-286. https://doi.org/10.1134/S1990747818030108

APA

Vorontsova, O. V., Akkuratov, E. E., Korenkova, O. M., & Shupliakov, O. (2018). Molecular Cloning of Synucleins in River Lamprey Lampetra fluviatilis. Biochemistry (Moscow) Supplement Series A: Membrane and Cell Biology, 12(3), 278-286. https://doi.org/10.1134/S1990747818030108

Vancouver

Vorontsova OV, Akkuratov EE, Korenkova OM, Shupliakov O. Molecular Cloning of Synucleins in River Lamprey Lampetra fluviatilis. Biochemistry (Moscow) Supplement Series A: Membrane and Cell Biology. 2018 Jul 1;12(3):278-286. https://doi.org/10.1134/S1990747818030108

Author

Vorontsova, O. V. ; Akkuratov, E. E. ; Korenkova, O. M. ; Shupliakov, O. / Molecular Cloning of Synucleins in River Lamprey Lampetra fluviatilis. In: Biochemistry (Moscow) Supplement Series A: Membrane and Cell Biology. 2018 ; Vol. 12, No. 3. pp. 278-286.

BibTeX

@article{1fffc4ce2f41481c83b525f492184897,
title = "Molecular Cloning of Synucleins in River Lamprey Lampetra fluviatilis",
abstract = "Synaptic proteins synucleins are found in pathologic aggregates in human brain during neurodegenerative diseases and in some tumors. Normal functions of these proteins in synapses are still unclear. In the present study, we used cDNA cloning to determine amino acid sequences of synucleins in the central nervous system of river lamprey (Lampetra fluviatilis), which is used as a model organism to study molecular mechanisms of synaptic transmission. Three genes are identified. High similarity in amino acid sequences as compared to other vertebrate species is revealed. The bioinformatic analysis predicts that the river lamprey synucleins relate to the group of gamma-synucleins. High homology with human alpha-synuclein is reported. The hydrophobic region required for the formation of alpha-synuclein amyloid fibers is also present in the river lamprey synucleins. The latter suggests that this region appeared at early stages of evolution. The obtained amino acid sequences of synucleins in the river lamprey brain will allow generating novel molecular tools for dissecting physiological functions of these proteins.",
keywords = "evolution, lamprey, molecular cloning, synapse, synuclein, synucleinopathies",
author = "Vorontsova, {O. V.} and Akkuratov, {E. E.} and Korenkova, {O. M.} and O. Shupliakov",
year = "2018",
month = jul,
day = "1",
doi = "10.1134/S1990747818030108",
language = "English",
volume = "12",
pages = "278--286",
journal = "Biochemistry (Moscow) Supplement Series A: Membrane and Cell Biology",
issn = "1990-7478",
publisher = "МАИК {"}Наука/Интерпериодика{"}",
number = "3",

}

RIS

TY - JOUR

T1 - Molecular Cloning of Synucleins in River Lamprey Lampetra fluviatilis

AU - Vorontsova, O. V.

AU - Akkuratov, E. E.

AU - Korenkova, O. M.

AU - Shupliakov, O.

PY - 2018/7/1

Y1 - 2018/7/1

N2 - Synaptic proteins synucleins are found in pathologic aggregates in human brain during neurodegenerative diseases and in some tumors. Normal functions of these proteins in synapses are still unclear. In the present study, we used cDNA cloning to determine amino acid sequences of synucleins in the central nervous system of river lamprey (Lampetra fluviatilis), which is used as a model organism to study molecular mechanisms of synaptic transmission. Three genes are identified. High similarity in amino acid sequences as compared to other vertebrate species is revealed. The bioinformatic analysis predicts that the river lamprey synucleins relate to the group of gamma-synucleins. High homology with human alpha-synuclein is reported. The hydrophobic region required for the formation of alpha-synuclein amyloid fibers is also present in the river lamprey synucleins. The latter suggests that this region appeared at early stages of evolution. The obtained amino acid sequences of synucleins in the river lamprey brain will allow generating novel molecular tools for dissecting physiological functions of these proteins.

AB - Synaptic proteins synucleins are found in pathologic aggregates in human brain during neurodegenerative diseases and in some tumors. Normal functions of these proteins in synapses are still unclear. In the present study, we used cDNA cloning to determine amino acid sequences of synucleins in the central nervous system of river lamprey (Lampetra fluviatilis), which is used as a model organism to study molecular mechanisms of synaptic transmission. Three genes are identified. High similarity in amino acid sequences as compared to other vertebrate species is revealed. The bioinformatic analysis predicts that the river lamprey synucleins relate to the group of gamma-synucleins. High homology with human alpha-synuclein is reported. The hydrophobic region required for the formation of alpha-synuclein amyloid fibers is also present in the river lamprey synucleins. The latter suggests that this region appeared at early stages of evolution. The obtained amino acid sequences of synucleins in the river lamprey brain will allow generating novel molecular tools for dissecting physiological functions of these proteins.

KW - evolution

KW - lamprey

KW - molecular cloning

KW - synapse

KW - synuclein

KW - synucleinopathies

UR - http://www.scopus.com/inward/record.url?scp=85051468881&partnerID=8YFLogxK

U2 - 10.1134/S1990747818030108

DO - 10.1134/S1990747818030108

M3 - Article

AN - SCOPUS:85051468881

VL - 12

SP - 278

EP - 286

JO - Biochemistry (Moscow) Supplement Series A: Membrane and Cell Biology

JF - Biochemistry (Moscow) Supplement Series A: Membrane and Cell Biology

SN - 1990-7478

IS - 3

ER -

ID: 40826768