TY - JOUR
T1 - Primary structure of ovine fibroblast growth factor-1 deduced by protein and cDNA analysis
AU - Grieb, Teri Wangler
AU - Ring, Mary
AU - Brown, Ernest
AU - Palmer, Carol
AU - Belle, Natalie
AU - Donjerkovic, Dubravka
AU - Chang, Helena
AU - Yun, June
AU - Subramanian, Ramiah
AU - Forozan, Farahnaz
AU - Guo, Yan
AU - Vertes, Akos
AU - Winkles, Jeffrey A.
AU - Burgess, Wilson H.
PY - 1998/5/8
Y1 - 1998/5/8
N2 - The amino acid sequence of full-length ovine fibroblast growth factor-1 (FGF-1) was determined by a combination of protein and cDNA sequencing. FGF-1 cDNA analysis indicated that ovine kidney cells express mRNAs encoding both full length FGF-1 and a truncated FGF-1 variant. An overall comparison of the ovine FGF-1 primary sequence to the eight species studied to date revealed a high degree of conservation, with ovine FGF-1 sharing 90 and 95% sequence identity with human FGF-1 and bovine FGF-1, respectively. Additionally, the FGF-1 proteins from the various species have conserved cysteine residues at positions 30 and 97 and contain acetylated amino-terminal alanine residues. Mass spectrometry analysis confirmed that the blocking group of ovine FGF-1 is also consistent with that of an acetyl-moiety. In contrast to the other FGF-1 proteins, the 154 residue primary sequence of ovine FGF-1 contains three unique amino acid differences: Arg9, Arg44, and Ile123. Ovine FGF-1, unlike human FGF-1, is a potent mitogenic factor for NIH 3T3 fibroblasts in the absence of heparin. In the presence of exogenous heparin, the mitogenic activity of ovine FGF-1 is potentiated slightly.
AB - The amino acid sequence of full-length ovine fibroblast growth factor-1 (FGF-1) was determined by a combination of protein and cDNA sequencing. FGF-1 cDNA analysis indicated that ovine kidney cells express mRNAs encoding both full length FGF-1 and a truncated FGF-1 variant. An overall comparison of the ovine FGF-1 primary sequence to the eight species studied to date revealed a high degree of conservation, with ovine FGF-1 sharing 90 and 95% sequence identity with human FGF-1 and bovine FGF-1, respectively. Additionally, the FGF-1 proteins from the various species have conserved cysteine residues at positions 30 and 97 and contain acetylated amino-terminal alanine residues. Mass spectrometry analysis confirmed that the blocking group of ovine FGF-1 is also consistent with that of an acetyl-moiety. In contrast to the other FGF-1 proteins, the 154 residue primary sequence of ovine FGF-1 contains three unique amino acid differences: Arg9, Arg44, and Ile123. Ovine FGF-1, unlike human FGF-1, is a potent mitogenic factor for NIH 3T3 fibroblasts in the absence of heparin. In the presence of exogenous heparin, the mitogenic activity of ovine FGF-1 is potentiated slightly.
UR - http://www.scopus.com/inward/record.url?scp=0032495986&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032495986&partnerID=8YFLogxK
U2 - 10.1006/bbrc.1998.8597
DO - 10.1006/bbrc.1998.8597
M3 - Article
C2 - 9600090
AN - SCOPUS:0032495986
SN - 0006-291X
VL - 246
SP - 182
EP - 191
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -