Home LiteratureArticle Details
PMID: 3001704 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Identification of a novel receptor in Drosophila for both epidermal growth factor and insulin.

Thompson KL, Decker SJ, Rosner MR

Abstract

The notable amino acid homology among mammalian growth factor receptors with tyrosine-specific protein kinase activity has led to speculation that these receptors derived from a common evolutionary precursor. We report the identification of a novel growth factor receptor from Drosophila cell cultures that has dual binding specificity for both insulin and epidermal growth factor (EGF). This 100-kDa protein is also related antigenically to the mammalian receptors for EGF and possibly insulin but may not correspond to the mammalian counterpart of either receptor in Drosophila. The Drosophila protein is recognized by antisera directed against the mammalian receptor for EGF in immunoblot hybridizations. It can be affinity labeled with either 125I-labeled insulin or 125I-labeled EGF after immunoprecipitation with anti-EGF receptor antiserum. Excess unlabeled EGF or insulin will block the affinity labeling with either growth factor, suggesting that both EGF and insulin share a common binding site on the 100-kDa Drosophila receptor. This Drosophila protein, therefore, may be closely related to an evolutionary precursor of the mammalian receptors for insulin and EGF.

MeSH Terms
Affinity Labels Animals Biological Evolution Cell Line Cross Reactions Drosophila melanogaster/analysis,genetics ErbB Receptors Growth Substances/metabolism Immunologic Techniques Membrane Proteins/immunology,metabolism Molecular Weight Receptor, Insulin/immunology,metabolism Receptors, Cell Surface/immunology,metabolism
Chemicals
Affinity Labels Growth Substances Membrane Proteins Receptors, Cell Surface ErbB Receptors Receptor, Insulin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Thompson K L
Decker S J
Rosner M R
References (21)
21 references, click to expand
  1. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
    Nature. 1970 Aug 15;227(5259):680-5 PMID: 5432063
  2. Protein-tyrosine kinases.
    Annu Rev Biochem. 1985;54:897-930 PMID: 2992362
  3. Antibodies to purified insulin receptor have insulin-like activity.
    Science. 1978 Jun 16;200(4347):1283-4 PMID: 663609
  4. Insulin in insects and annelids.
    Diabetes. 1981 Jan;30(1):70-6 PMID: 6785127
  5. "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate--polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A.
    Anal Biochem. 1981 Apr;112(2):195-203 PMID: 6266278
  6. Three loci related to the src oncogene and tyrosine-specific protein kinase activity in Drosophila.
    Nature. 1983 Apr 28;302(5911):837-9 PMID: 6405280
  7. The insulin receptor protein kinase. Physicochemical requirements for activity.
    J Biol Chem. 1983 Dec 10;258(23):14450-5 PMID: 6557114
  8. Nucleotide sequences of the Drosophila src and abl homologs: conservation and variability in the src family oncogenes.
    Cell. 1983 Dec;35(2 Pt 1):393-401 PMID: 6317185
  9. Purification of denatured epidermal growth factor-receptor from A431 human epidermoid carcinoma cells.
    Arch Biochem Biophys. 1984 Feb 1;228(2):621-6 PMID: 6320745
  10. Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells.
    Nature. 1984 May 31-Jun 6;309(5967):418-25 PMID: 6328312
  11. A comparison of the insulin- and epidermal growth factor-stimulated protein kinases from human placenta.
    J Biol Chem. 1984 Aug 10;259(15):9913-21 PMID: 6378914
  12. The epidermal growth factor receptor gene and its product.
    Nature. 1984 Oct 4-10;311(5985):414-6 PMID: 6090939
  13. Antibodies to two defined regions of the transforming protein pp60src interact specifically with the epidermal growth factor receptor kinase system.
    Proc Natl Acad Sci U S A. 1984 Oct;81(19):5911-5 PMID: 6207534
  14. The neu oncogene: an erb-B-related gene encoding a 185,000-Mr tumour antigen.
    Nature. 1984 Dec 6-12;312(5994):513-6 PMID: 6095109
  15. Immunoprecipitation of insulin receptors from cultured human lymphocytes (IM-9 cells) by antibodies to pp60src.
    Science. 1985 Feb 15;227(4688):761-3 PMID: 3918346
  16. The Drosophila EGF receptor gene homolog: conservation of both hormone binding and kinase domains.
    Cell. 1985 Mar;40(3):599-607 PMID: 2982499
  17. Phosphorylation of the erbB gene product from an avian erythroblastosis virus-transformed chick fibroblast cell line.
    J Biol Chem. 1985 Feb 25;260(4):2003-6 PMID: 2982800
  18. A Drosophila genomic sequence with homology to human epidermal growth factor receptor.
    Nature. 1985 Mar 14-20;314(6007):178-80 PMID: 2983232
  19. The human insulin receptor cDNA: the structural basis for hormone-activated transmembrane signalling.
    Cell. 1985 Apr;40(4):747-58 PMID: 2859121
  20. Genes-in-pieces revisited.
    Science. 1985 May 17;228(4701):823-4 PMID: 4001923
  21. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.
    Anal Biochem. 1976 May 7;72:248-54 PMID: 942051
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1985-12-00
Pages
8443-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC390932
Subset
IM
Grants
NCI NIH HHS · CA35541 · United States
NCI NIH HHS · CA37754 · United States
NIEHS NIH HHS · T32-ES07020 · United States
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com