Y. Zhan et K. Jimmy, Molecular isolation and characterisation of carp transforming growth factor beta 1 from activated leucocytes, FISH SHELLF, 10(4), 2000, pp. 309-318
The transforming growth factor (TGF beta) family of proteins are a set of p
leiotropic secreted signalling molecules with unique and potent immunoregul
atory properties. In this study the molecular cloning of carp TGF beta(1),
is reported. A partial cDNA of the TGF beta protein was initially identifie
d from a cDNA pool, obtained by subtracting the cDNAs from Con A-induced ca
rp head kidney leucocytes from uninduced carp head kidney leucocyte cDNA. T
he entire coding sequence was assembled by sequencing both ends of the cDNA
clone by using an anchored PCR reaction. Sequence analysis revealed an ORF
encoding a protein of 376 amino acids, containing the similar unique patte
rn of conserved cysteines (seven out of nine) in the cysteine knot structur
e which exists in all known TCTF beta proteins. Compared with other animal
TCT beta s, the cDNA clone shows approximately 59-42, 40-38 and 37-36% amin
o acid identity with TGF beta(1), TGF beta(3), and TGF beta(2) respectively
. Carp TGF beta(1) is expressed at low levels in carp head kidney, spleen,
egg and liver, whereas its messenger RNA level is increased after activatio
n of the head kidney leucocytes with Con A. Sequence analysis and pattern o
f expression suggests that this is the carp TGF beta(1). (C) 2000 Academic
Press.