Covalent linkage between nucleotides and platelet-derived endothelial cell growth factor
- PMID: 1939103
Covalent linkage between nucleotides and platelet-derived endothelial cell growth factor
Abstract
Platelet-derived endothelial cell growth factor (PD-ECGF) is a 45-kDa peptide mitogen which is present in platelets and placenta and produced by certain cultured cell lines. Immunoprecipitation of A431 cells metabolically labeled with [32P]orthophosphate revealed the incorporation of 32P radioactivity into PD-ECGF. Phosphoamino acid analysis showed that serine residues of PD-ECGF were phosphorylated in vivo. Forskolin, 12-O-tetradecanoylphorbol-13-acetate, and epidermal growth factor had no effect on the in vivo phosphorylation of PD-ECGF. Moreover, incubation of pure PD-ECGF with [gamma-32P]ATP led to labeling of PD-ECGF. Optimal labeling was achieved by incubation at 95 degrees C for 5 min in the presence of sodium dodecyl sulfate, dithiothreitol, and Mg2+ or Mn2+. PD-ECGF was also labeled with [2,8-3H]ATP, [2,5',8-3H]ATP, or [alpha-32P]ATP. ATP and GTP were the preferred nucleotide substrates by comparison with other nucleotides and related components. Partial amino acid hydrolysis liberated a significant amount of O-[32P]phosphoserine from PD-ECGF labeled in vitro with [gamma-32P] ATP. Furthermore, 32P-radiolabeled nucleotides were released after snake venom phosphodiesterase or piperidine treatment from PD-ECGF labeled in vitro with [alpha-32P]ATP or [gamma-32P]ATP, as well as from PD-ECGF labeled in vivo with [32P]orthophosphate. These data indicate that serine residues of PD-ECGF can be covalently linked to phosphate groups of nucleotides, resulting in a nucleotidylated protein. The functional significance of this post-translational modification remains to be determined.
Similar articles
-
Thymidine phosphorylase activity associated with platelet-derived endothelial cell growth factor.J Biochem. 1993 Jul;114(1):9-14. doi: 10.1093/oxfordjournals.jbchem.a124146. J Biochem. 1993. PMID: 8407883
-
Expression of platelet-derived endothelial cell growth factor in Escherichia coli and confirmation of its thymidine phosphorylase activity.Biochemistry. 1992 Dec 8;31(48):12141-6. doi: 10.1021/bi00163a024. Biochemistry. 1992. PMID: 1457409
-
Platelet-derived endothelial cell growth factor has thymidine phosphorylase activity.Biochem Biophys Res Commun. 1992 May 15;184(3):1311-6. doi: 10.1016/s0006-291x(05)80025-7. Biochem Biophys Res Commun. 1992. PMID: 1590793
-
Platelet-derived endothelial cell growth factor.Prog Growth Factor Res. 1991;3(3):207-17. doi: 10.1016/0955-2235(91)90007-q. Prog Growth Factor Res. 1991. PMID: 1811791 Review.
-
Platelet-derived endothelial cell growth factor.J Cell Biochem. 1991 Nov;47(3):208-10. doi: 10.1002/jcb.240470304. J Cell Biochem. 1991. PMID: 1724243 Review.
Cited by
-
Platelet-derived endothelial cell growth factor thymidine phosphorylase in tumour growth and response to therapy.Br J Cancer. 1997;76(6):689-93. doi: 10.1038/bjc.1997.447. Br J Cancer. 1997. PMID: 9310231 Free PMC article. Review.
-
Thymidine phosphorylase promotes malignant progression in hepatocellular carcinoma through pentose Warburg effect.Cell Death Dis. 2019 Jan 17;10(2):43. doi: 10.1038/s41419-018-1282-6. Cell Death Dis. 2019. PMID: 30674871 Free PMC article.
-
Thymidine phosphorylase: A potential new target for treating cardiovascular disease.Trends Cardiovasc Med. 2018 Apr;28(3):157-171. doi: 10.1016/j.tcm.2017.10.003. Epub 2017 Oct 20. Trends Cardiovasc Med. 2018. PMID: 29108898 Free PMC article. Review.
-
Human platelet-derived endothelial cell growth factor is homologous to Escherichia coli thymidine phosphorylase.Protein Sci. 1992 May;1(5):688-90. doi: 10.1002/pro.5560010514. Protein Sci. 1992. PMID: 1304367 Free PMC article. No abstract available.
-
The biology of radioresistance: similarities, differences and interactions with drug resistance.Cytotechnology. 1993;12(1-3):325-45. doi: 10.1007/BF00744671. Cytotechnology. 1993. PMID: 7764455 Review.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources