Cloning and sequencing of an equine insulin-like growth factor I cDNA and its expression in fetal and adult tissues.
A cDNA for equine insulin-like growth factor I (IGF I) has been isolated by reverse transcriptase-polymerase chain reaction and subsequently sequenced. The sequenced fragment contained 465 bp including the coding regions for the signal peptide, the entire mature protein, and 4 amino acids into the E-peptide. Like its human counterpart, the mature equine IGF I peptide contains 70 amino acids and was 100% homologous between horse and man. The 49-amino-acid signal peptide had the threonine in position 26 of the human signal peptide substituted by isoleucine. The nucleotide homology across the entire clone was 96.3% between horse and man and 91.6% between horse and rat. The isolated cDNA hybridized to the same transcripts in fetal and adult tissues.
Otte
K
K
Department of Pathology, Faculty of Veterinary Medicine, Swedish University of Agricultural Sciences, Uppsala, Sweden.
Rozell
B
B
Gessbo
A
A
Engström
W
W
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D005075:Biological Evolution; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics* / Q000302:isolation & purification; D018507:Gene Expression Regulation, Developmental / Q000502:physiology*; D006736:Horses / Q000235:genetics*; D006801:Humans; D007334:Insulin-Like Growth Factor I / Q000235:genetics*; D008969:Molecular Sequence Data; D051381:Rats / Q000235:genetics*; D017386:Sequence Homology, Amino Acid; D012689:Sequence Homology, Nucleic Acid; D012756:Sheep / Q000235:genetics*
D018076:DNA, Complementary; D007334:Insulin-Like Growth Factor I