TY - JOUR
T1 - Identification of receptor tyrosine kinases in the embryonic chicken Lens
AU - Potts, Jay D.
AU - Harocopos, George J.
AU - Beebe, David C.
N1 - Funding Information:
ACKNOWLEDGMENTS We would like to thank Dr. Steven Bassnett for his helpful discussions and critical review of the manuscript. We would also like to thank Mike Flora for the synthesis of the oligodeoxynucleotides. This study was supported by NIH grant EY 04853.
PY - 1993
Y1 - 1993
N2 - Protein phosphorylation plays a critical role in the control of growth and regulation of many eukaryotic cells. Members of the protein tyrosine kinase (PTK) family of peptides function as growth factor receptors and oncoproteins. A common feature of members of the PTK family is a highly conserved intracellular catalytic domain. We analyzed the chicken lens epithelium, which responds to several known growth factors, for the presence of receptor PTK's. Using reverse transcription polymerase chain reaction (rtPCR) and degenerate primers made to conserved regions within kinase domains, we amplified RNA from embryonic day 6 (E6) lens epithleium and sequenced 135 cDNA clones. Sixteen distinct kinase sequences were obtained. Eight of these sequences represented kinase domains of known mammalian growth factor receptors, and six represented intercellular kinases. Two sequences appeared to code for new kinases. The amino acid identity of the chicken homologs ranged from 80-100% when compared to their mammalian counterparts.
AB - Protein phosphorylation plays a critical role in the control of growth and regulation of many eukaryotic cells. Members of the protein tyrosine kinase (PTK) family of peptides function as growth factor receptors and oncoproteins. A common feature of members of the PTK family is a highly conserved intracellular catalytic domain. We analyzed the chicken lens epithelium, which responds to several known growth factors, for the presence of receptor PTK's. Using reverse transcription polymerase chain reaction (rtPCR) and degenerate primers made to conserved regions within kinase domains, we amplified RNA from embryonic day 6 (E6) lens epithleium and sequenced 135 cDNA clones. Sixteen distinct kinase sequences were obtained. Eight of these sequences represented kinase domains of known mammalian growth factor receptors, and six represented intercellular kinases. Two sequences appeared to code for new kinases. The amino acid identity of the chicken homologs ranged from 80-100% when compared to their mammalian counterparts.
UR - http://www.scopus.com/inward/record.url?scp=0027199802&partnerID=8YFLogxK
U2 - 10.3109/02713689308995772
DO - 10.3109/02713689308995772
M3 - Article
C2 - 8222737
AN - SCOPUS:0027199802
SN - 0271-3683
VL - 12
SP - 759
EP - 763
JO - Current Eye Research
JF - Current Eye Research
IS - 8
ER -