Localization of epidermal growth factor receptor in hepatocyte nuclei
Ulrich Marti
Cell Biology and Aging Section, Department of Veterans Affairs Medical Center, San Francisco, California 94121; and the Departments of Medicine and Anatomy, the Liver Center and Hooper Foundation, University of California, San Francisco, California 94143
Search for more papers by this authorCorresponding Author
Dr. Susan Jo Burwen
Cell Biology and Aging Section, Department of Veterans Affairs Medical Center, San Francisco, California 94121; and the Departments of Medicine and Anatomy, the Liver Center and Hooper Foundation, University of California, San Francisco, California 94143
Cell Biology Section 151E, Department of Veterans Affairs Medical Center, 4150 Clement Street, San Francisco, CA 94121===Search for more papers by this authorAlan Wells
Cell Biology and Aging Section, Department of Veterans Affairs Medical Center, San Francisco, California 94121; and the Departments of Medicine and Anatomy, the Liver Center and Hooper Foundation, University of California, San Francisco, California 94143
Search for more papers by this authorMary E. Barker
Cell Biology and Aging Section, Department of Veterans Affairs Medical Center, San Francisco, California 94121; and the Departments of Medicine and Anatomy, the Liver Center and Hooper Foundation, University of California, San Francisco, California 94143
Search for more papers by this authorSandra Huling
Cell Biology and Aging Section, Department of Veterans Affairs Medical Center, San Francisco, California 94121; and the Departments of Medicine and Anatomy, the Liver Center and Hooper Foundation, University of California, San Francisco, California 94143
Search for more papers by this authorAnna M. Feren
Cell Biology and Aging Section, Department of Veterans Affairs Medical Center, San Francisco, California 94121; and the Departments of Medicine and Anatomy, the Liver Center and Hooper Foundation, University of California, San Francisco, California 94143
Search for more papers by this authorAlbert L. Jones
Cell Biology and Aging Section, Department of Veterans Affairs Medical Center, San Francisco, California 94121; and the Departments of Medicine and Anatomy, the Liver Center and Hooper Foundation, University of California, San Francisco, California 94143
Search for more papers by this authorUlrich Marti
Cell Biology and Aging Section, Department of Veterans Affairs Medical Center, San Francisco, California 94121; and the Departments of Medicine and Anatomy, the Liver Center and Hooper Foundation, University of California, San Francisco, California 94143
Search for more papers by this authorCorresponding Author
Dr. Susan Jo Burwen
Cell Biology and Aging Section, Department of Veterans Affairs Medical Center, San Francisco, California 94121; and the Departments of Medicine and Anatomy, the Liver Center and Hooper Foundation, University of California, San Francisco, California 94143
Cell Biology Section 151E, Department of Veterans Affairs Medical Center, 4150 Clement Street, San Francisco, CA 94121===Search for more papers by this authorAlan Wells
Cell Biology and Aging Section, Department of Veterans Affairs Medical Center, San Francisco, California 94121; and the Departments of Medicine and Anatomy, the Liver Center and Hooper Foundation, University of California, San Francisco, California 94143
Search for more papers by this authorMary E. Barker
Cell Biology and Aging Section, Department of Veterans Affairs Medical Center, San Francisco, California 94121; and the Departments of Medicine and Anatomy, the Liver Center and Hooper Foundation, University of California, San Francisco, California 94143
Search for more papers by this authorSandra Huling
Cell Biology and Aging Section, Department of Veterans Affairs Medical Center, San Francisco, California 94121; and the Departments of Medicine and Anatomy, the Liver Center and Hooper Foundation, University of California, San Francisco, California 94143
Search for more papers by this authorAnna M. Feren
Cell Biology and Aging Section, Department of Veterans Affairs Medical Center, San Francisco, California 94121; and the Departments of Medicine and Anatomy, the Liver Center and Hooper Foundation, University of California, San Francisco, California 94143
Search for more papers by this authorAlbert L. Jones
Cell Biology and Aging Section, Department of Veterans Affairs Medical Center, San Francisco, California 94121; and the Departments of Medicine and Anatomy, the Liver Center and Hooper Foundation, University of California, San Francisco, California 94143
Search for more papers by this authorAbstract
Experiments undertaken to investigate the binding of epidermal growth factor by hepatocyte nuclei showed that: (a) isolated nuclei from both normal and regenerating rat liver are capable of binding 125I-epidermal growth factor, (b) the nuclear epidermal growth factor-binding protein is similar in molecular weight to the plasma membrane epidermal growth factor receptor, (c) monoclonal antibodies produced against the plasma membrane epidermal growth factor receptor recognize the nuclear epidermal growth factor receptor and (d) the nuclear receptor has an affinity for epidermal growth factor comparable to that of the plasma membrane receptor, but fewer (∼ 10%) nuclear receptors are available per protein unit compared with the plasma membrane. (HEPATOLOGY 1991;13:15–20).
References
- 1 Burwen SJ, Jones AL. The association of polypeptide hormones and growth factors with the nucleus of target cells. Trends Biochem Sci 1987; 12: 159–162.
- 2 Johnson LK, Vlodavsky I, Baxter JD, Gospodarowicz D. Nuclear accumulation of epidermal growth factor in cultured rat pituitary cells. Nature 1980; 287: 340–343.
- 3 Savion N, Vlodavsky I, Gospodarowicz D. Nuclear accumulation of epidermal growth factor in cultured bovine corneal endothelial and granulosa cells. J Biol Chem 1981; 256: 1149–1154.
- 4 Green MR, Phil D, Mycock C, Smith CG, Couchman JR. Biochemical and structural processing of [125I] epidermal growth factor in rat epidermis and hair follicles: accumulation of nuclear label. J Invest Dermatol 1987; 88: 259–265.
- 5 Rakowicz-Szulczynska EM, Rodeck U, Herlyn M, Koprowski H. Chromatin binding of epidermal growth factor, nerve growth factor, and platelet-derived growth factor in cells bearing the appropriate surface receptors. Proc Natl Acad Sci USA 1986; 83: 3728–3732.
- 6 Rakowicz-Szulczynska EM, Otwiaska D, Rodeck U, Koprowski H. Epidermal growth factor (EGF) and monoclonal antibody to cell surface EGF receptor bind to the same chromatin receptor. Arch Biochem Biophys 1989; 268(2): 456–464.
- 7 Raper SE, Burwen SJ, Barker ME, Jones AL. Translocation of epidermal growth factor to the hepatocyte nucleus during rat liver regeneration. Gastroenterology 1987; 92: 1243–1250.
- 8 Burwen SJ, Barker ME, Goldman IS, Hradek GT, Raper SE, Jones AL. Transport of epidermal growth factor by rat liver: evidence for nonlysosomal pathway. J Cell Biol 1984; 99: 1259–1265.
- 9 Marti U, Burwen SJ, Barker ME, Huling S, Feren AM, Jones AL. The effect of oxidative iodination of epidermal growth factor on its binding and secretion by hepatocytes. J Cell Biochem 1989; 40: 109–119.
- 10 Ichii S, Yoshida A, Hoshikawa Y. Binding sites for epidermal growth factor in nuclear fraction from rat liver. Endocrinol Jpn 1988; 35: 567–575.
- 11 Vlodavsky I, Brown KD, Gospodarowicz D. A comparison of the binding of epidermal growth factor to cultured granulosa and luteal cells. J Biol Chem 1978; 253: 3744–3750.
- 12 Blobel G, Potter VR. Nuclei from rat liver: isolation method that combines purity with high yield. Science 1966; 154: 1662–1665.
- 13 Aronson NN, Touster O. Isolation of rat liver plasma membrane fragments in isotonic sucrose. Methods Enzymol 1974; 31: 90–102.
- 14 Hilaire St. RJ, Hradek GT, Jones AL. Hepatic sequestration and biliary secretion of epidermal growth factor: evidence for a high-capacity uptake system. Proc Natl Acad Sci USA 1983; 80: 3797–3801.
- 15 Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680–685.
- 16
McIntosh JEA,
McIntosh RP.
Mathematical modelling and computers in endocrinology.
New York:
Springer-Verlag,
1980.
10.1007/978-3-642-81401-3 Google Scholar
- 17 McCarley DJ, Wells A, Bishop JM, Schatzman RC. Activation of the EGF receptor by monoclonal antibody directed against the carboxy-terminus of the receptor [Abstract]. J Cell Biochem 1988; 12A: 109.
- 18 Wells A, Bishop JM, Helmeste D. Amplified gene for the epidermal growth factor receptor in a human glioblastoma cell line encodes an enzymatically inactive protein. Mol Cell Biol 1988; 8: 4561–4565.
- 19 Hauri HP, Roth J, Sterchi E, Lentze M. Transport to cell surface of intestinal sucrase-isomaltase is blocked in the Golgi apparatus in a patient with congenital sucrase-isomaltase deficiency. Proc Natl Acad Sci USA 1985; 82: 4423–4427.
- 20 Linsley PS, Fox CF. Direct linkage of EGF to its receptor: characterization and biological relevance. J Cell Biochem 1980; 14: 441–459.
- 21 Vessey DA, Zakim D. Are glucuronidation reactions compartmented? In: A Aito, ed. Conjugation reaction in drug biotransformation. Amsterdam: Elsevier/North-Holland Biomedical Press, 1978; 247–255.
- 22 Capitani S, Girard PR, Mazzei GJ, Kuo JF, Berezney R, Manzoli FA. Immunochemical characterization of protein kinase C in rat liver nuclei and subnuclear fractions. Biochem Biophys Res Commun 1987; 142: 367–375.
- 23 Buckley AR, Crowe PD, Russell DH. Rapid activation of protein kinase C in isolated rat liver nuclei by prolactin, a known hepatic mitogen. Proc Natl Acad Sci USA 1988; 85: 8649–8653.
- 24 Vigneri R, Goldfine ID, Wong KY, Smith GJ, Pezzino V. The nuclear envelope: the major site of insulin binding in rat liver nuclei. J Biol Chem 1978; 253: 2098–2103.
- 25 Re RN, Vizard DL, Brown J, Bryan SE. Angiotensin II receptors in chromatin fragments generated by micrococcal nuclease. Biochem Biophys Res Commun 1984; 119: 220–227.
- 26 Re RN, Vizard DL, Brown J, LeGros L, Bryan SE. Angiotensin II receptors in chromatin. J Hypertension (Suppl) 1984; 2: S271–S273.
- 27 Rao Ch V, Mitra S. Gonadotropin and prostaglandin binding sites in nuclei of bovine corpora lutea. Biochim Biophys Acta 1979; 584: 454–466.
- 28 Rajendran KG, Menon KMJ. Evidence for the existence of gonadotropin receptors in the nuclei isolated from rat ovary. Biochem Biophys Res Commun 1983; 111: 127–134.
- 29 Zolman JC, Theodoropoulos TJ. Localization of putative gonadotropin releasing hormone receptor protein in the anterior pituitary. Cell Biochem Funct 1984; 2: 208–212.
- 30 Millar RP, Rosen H, Badminton M, Pasqualini C, Kerdelhue B. Luteinizing hormone-releasing hormone (LH-RH) binding to purified rat pituitary nuclei. FEBS Lett 1983; 153: 382–386.
- 31 Andres RY, Jeng I, Bradshaw RA. Nerve growth factor receptors: Identification of distinct classes in plasma membranes and nuclei of embryonic dorsal root neurons. Proc Natl Acad Sci USA 1977; 74: 2785–2789.
- 32 Yankner BA, Shooter EM. Nerve growth factor in the nucleus: Interaction with receptors on the nuclear membrane. Proc Natl Acad Sci USA 1979; 76: 1269–1273.
- 33 Cornell RP. Gut-derived endotoxin elicits hepatotrophic factor secretion for liver regeneration. Am J Physiol 1985; 249: R551–R562.
- 34 Earp HS, O'Keefe EJ. Epidermal growth factor receptor numbers decrease during rat liver regeneration. J Clin Invest 1981; 67: 1580–1583.