TY - JOUR
T1 - Isolation of the first piscine transforming growth factor β gene
T2 - Analysis reveals tissue specific expression and a potential regulatory sequence in rainbow trout (Oncorhynchus mykiss)
AU - Hardie, Laura J.
AU - Laing, Kerry J.
AU - Daniels, Garry D.
AU - Grabowski, Peter S.
AU - Cunningham, Charles
AU - Secombes, Christopher J.
PY - 1998/8/31
Y1 - 1998/8/31
N2 - The nucleotide sequence of a rainbow trout transforming growth factor β (TGF-β) peptide is presented, which translates into a 382 amino acid precursor molecule containing a 20 amino acid leader and a mature peptide of 112 amino acids. The mature peptide has nine conserved cysteines and a conserved proline (position 36) and glycine (position 46), all characteristic of TGF-β superfamily molecules. Within the precursor region are three glycosylation sites, two in common with known TGF-βs, an integrin binding site (RGD) and the tetrabasic peptide cleavage site (RKKR). The full 3' untranslated region (UTR) consists of 542 nucleotides with a polyadenylation signal 16 nucleotides upstream of the poly(A) tail. The 5' UTR contains an open reading frame with the potential to encode an eleven amino acid peptide, which may have significance for regulation of TGF-β translation. A wide tissue distribution of TGF-β message was detected by RT-PCR; in blood leukocytes, kidney macrophages, brain, gill, and spleen tissue but not liver. A phylogenetic tree reveals the trout TGF-β sequence is most related to xenopus TGF-β5, with these sequences and that of chicken TGF-β4 grouping with mammalian TGF-β1s. The impact of the trout sequence on current theories of TGF-β isotype evolution is discussed.
AB - The nucleotide sequence of a rainbow trout transforming growth factor β (TGF-β) peptide is presented, which translates into a 382 amino acid precursor molecule containing a 20 amino acid leader and a mature peptide of 112 amino acids. The mature peptide has nine conserved cysteines and a conserved proline (position 36) and glycine (position 46), all characteristic of TGF-β superfamily molecules. Within the precursor region are three glycosylation sites, two in common with known TGF-βs, an integrin binding site (RGD) and the tetrabasic peptide cleavage site (RKKR). The full 3' untranslated region (UTR) consists of 542 nucleotides with a polyadenylation signal 16 nucleotides upstream of the poly(A) tail. The 5' UTR contains an open reading frame with the potential to encode an eleven amino acid peptide, which may have significance for regulation of TGF-β translation. A wide tissue distribution of TGF-β message was detected by RT-PCR; in blood leukocytes, kidney macrophages, brain, gill, and spleen tissue but not liver. A phylogenetic tree reveals the trout TGF-β sequence is most related to xenopus TGF-β5, with these sequences and that of chicken TGF-β4 grouping with mammalian TGF-β1s. The impact of the trout sequence on current theories of TGF-β isotype evolution is discussed.
KW - cDNA sequence
KW - Cytokines
KW - Evolution
KW - Rainbow trout
KW - Transforming growth factor β
UR - http://www.scopus.com/inward/record.url?scp=0032145878&partnerID=8YFLogxK
U2 - 10.1006/cyto.1997.0334
DO - 10.1006/cyto.1997.0334
M3 - Article
C2 - 9722928
AN - SCOPUS:0032145878
SN - 1043-4666
VL - 10
SP - 555
EP - 563
JO - Cytokine
JF - Cytokine
IS - 8
ER -