Chicken synucleins: cloning and expression in the developing embryo.
Synucleins comprise a family of small intracellular proteins that have recently attracted considerable attention because of their involvement in human diseases. Mutations of alpha-synuclein has been found in several families with hereditary early-onset Parkinson's disease and accumulation of this protein in characteristic cytoplasmic inclusions is a pathohistological hallmark of several neurodegenerative diseases that have been recently classified as 'alpha;-synucleinopathies' (reviewed in Brain Res. Bull. 50 (1999) 465; J. Neurosci. Res. 58 (1999) 120; Philos. Trans. R. Soc. Lond. Biol. Sci. 354 (1999) 1101; Brain Pathol. 9 (1999) 733). Aggregates of beta-synuclein and persyn (gamma-synuclein) also have been found in dystrophic neurites associated with Parkinson's and other neurodegenerative diseases (Proc. Natl. Acad. Sci. USA 96 (1999) 13450; and our unpublished observations). Moreover, persyn has been implicated in malignization of breast tumours (Cancer Res. 57 (1997) 759; Cancer Res. 59 (1999) 742; Hum. Mol. Genet. 7 (1998) 1417). All synucleins have distinct, although overlapping, patterns of expression in the embryonic, postnatal and adult mammalian nervous systems, suggesting important, although still not clear, biological functions in neuronal developing. Chicken embryo is a unique object for developmental studies that allows in vivo manipulations not always possible for mammalian embryos. Studies of synucleins expression in this model system could shed light on their functions in the developing nervous system. We cloned three chicken synucleins from the embryonic neural cDNA libraries and studied their expression in normal chicken embryonic tissues by Northern and in situ hybridization with specific probes. Our results demonstrate that primary structures and expression patterns of synucleins are similar in birds and mammals, suggesting that conserved function of synucleins is important for embryonic development of vertebrates.
Tiunova
A A
AA
P.K. Anokhin Institute of Normal Physiology, Baltyiskaya Street, Moscow, Russia.
Anokhin
K V
KV
Saha
A R
AR
Schmidt
O
O
Hanger
D P
DP
Anderton
B H
BH
Davies
A M
AM
Ninkina
N N
NN
Buchman
V L
VL
D000595:Amino Acid Sequence; D000818:Animals; D015152:Blotting, Northern; D001921:Brain / Q000196:embryology; D002642:Chick Embryo; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000378:metabolism; D004625:Embryo, Nonmammalian / Q000378:metabolism*; D017403:In Situ Hybridization; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins / Q000096:biosynthesis* / Q000235:genetics* / Q000378:metabolism; D009474:Neurons / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D051843:Synucleins; D014018:Tissue Distribution; D051844:alpha-Synuclein; D051846:beta-Synuclein; D051845:gamma-Synuclein
D018076:DNA, Complementary; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins; C104249:SNCG protein, human; D051843:Synucleins; D051844:alpha-Synuclein; D051846:beta-Synuclein; D051845:gamma-Synuclein