Summary
Several physiological parameters were examined for inducing acinar cell proliferation and corresponding increased expression of β1–4 galactosyltransferase. In this study, dietary changes causing acinar cell proliferation included the following: the introduction of animals to a liquid diet (causing gland atrophy) followed by reintroduction of solid chow, gustatory stimulation provided by the introduction of 0.5% citric acid to animal drinking water, and removal of the submandibular gland with subsequent reliance on the parotid gland for salivary protein. Alterations in growth factor levels were produced by injecting animals with a chronic (3 day) regimen of either nerve growth factor or epidermal growth factor. Parotid gland proliferation could be blocked in all cases except EGF by the injection of propranolol, a β-adrenoceptor antagonist, or the galactosyltransferase specific modifier protein, α-lactalbumin. EGF-induced proliferation could, however, be prevented by treating the animals with monoclonal antibody to EGF receptor or galactosyltransferase modifier protein a-lactalbumin. These results for normal acinar cell proliferation suggest a direct role for cell surface β1–4 galactosyltransferase in signalling and maintaining active cell growth.
Similar content being viewed by others
References
Kornfeld R, Kornfeld S: Assembly of asparagine-linked oligosaccharides. Ann Rev Biochem 54: 631–664, 1985
Roth J, Lentze MJ, Berger EG: Immunocytochemical demonstration of ecto-galactosyltransferase in absorptive intestinal cells. J Cell Biol 100: 118–125, 1985
Roseman S: The synthesis of complex carbohydrates by multiglycosyltransferase systems and their potential function in intercellular adhesion. Chem Phys Lipids 5: 270–274,1970
Shur BD: The receptor function of galactosyltransferase during cellular interactions. Molec Cell Biochem 61: 143–156,1984
Humphreys-Beher MG, Schneyer CA, Kidd VJ, Marchase RB: Isoproterenol-mediated parotid gland hypertrophy is inhibited by effectors of 4β-galactosyltransferase. J Biol Chem 262: 11706–11713, 1987
Roth S, White D: Intercellular contact and cell-surface galactosyltransferase activity. Proc Natl Acad Sci USA 69: 485–489,1972
Patt LM, Grimes WJ: Cell surface glycolipid and glycoprotein glycosyltransferases of normal and transformed cells. J Biol Chem 249: 4157–4165, 1974
Roth S, Roelke M, Dorsey J: Cell surface glycosyltransferase on malignant and nonmalignant cells. In: Growth, Kinetics and Biochemical Regulation of Normal and Malignant Cells (B Drewinko and RM Humphrey eds.), Williams and Wilkins, Baltimore, MD, 1977, pp 245–259
Podolsky DK, Weiser MM, Westwood JC, Gammon M: Cancer-associated serum galactosyltransferase activity. Demonstration of an animal model system. J Biol Chem 252:1807–1813,1977
Ip C, Dao TL: Increase in serum and tissue glycosyltransferases and glycosidases in tumor-bearing rats. Cancer Res 37:3442–3447,1977
Podolsky DK, Weiser MM: Galactosyltransferase activities in human sera: detection of a cancer-associated isoenzyme. Biochem Biophys Res Commun 65: 545–551, 1975
Roth S, McGuire EJ, Roseman S: Evidence for cell surface glycosyltransferase, J Cell Biol 51: 536–547, 1971
Pierce M, Turley EA, Roth S: Cell surface galactosyltransferase activities. International Review of Cytology 65: 244,1980
Mobs WD, Wilson JR, Weiser MM: UDP-galactose inhibition of BALB13 T12 cell growth. Exper Cell Res 141: 365–374,1982
Schneyer CA: Salivary gland and changes after isoproterenol-induced enlargement. Am J Physiol 203: 232–236, 1962
Schneyer CA: Regulation of salivary gland size. In: Regulation of Organ and Tissue Growth (RJ Goss, ed) pp 211–232, Academic Press, New York, NY, 1972
Selye H, Cantin M, Veilleux R: Abnormal growth and sclerosis of the salivary glands induced by chronic treatment with isoproterenol. Growth 25: 243–248, 1961
Barka T: Induced cell proliferation: the effect of isoproterenol. Cell Tissue Res 37: 662–667, 1965
Marchase RB, Kidd VJ, Rivera AA, Humphreys-Beher MG: Cell-surface expression of 4β-galactosyltransferase accompanies rat parotid acinar cell transition to growth. J Cell Biochem 36: 453–465, 1988
Humphreys-Beher MG, Imell M, Jentoft N, Gleason M, Carlson DM: Isolation and characterization of UDP-galactose: N-acetylglucosamine 4β-galactosyltransferase activity induced in rat parotid glands treated with isoproterenol. J Biol Chem 259: 5,799–5,802, 1984
Humphreys-Beher MG, Bunnell B, Ledbetter DH, Van Tuinen P, Kidd VJ: Molecular cloning and chromosomal localization of human 4β-galactosyltransferase. Proc Natl Acad Sci USA 83: 8918–8923, 1986
Humphreys-Beher MG: Restoration of α-lactalbumin-inhibited rat parotid gland hypertrophy and hyperplasia by agents specific for membrane glycoprotein N-acetylglucosamine. Archs Oral Biol 34: 811–819, 1989
Hall HD, Schneyer CA: Functional mediation of compensatory enlargement of parotid. Cell Tiss Res 184: 249–254, 1977
Hall HD, Schneyer CA: Neural regulation of compensatory enlargement of the parotid gland of the rat. Cell Tiss Res 187:147–151,1978
Humphreys-Beher MG, Schneyer CA: Cell surface expression of 4β-galactosyltransferase accompanies rat parotid gland hypertrophy induced by changes in diet. Biochem J 246:387–391,1987
Hall HD, Schneyer CA: Role of autonomic pathways in disuse atrophy of rat parotid. Proc Soc Exp Biol Med 143: 19–22,1973
Zelles T, Blazsek J, Kóbor A, Gelencser F: A glandula parotis gusztatórikus ingerrel létrehozott megnagyobbadása. Fogovosi Szemle 77: 315–318, 1984
Schneyer CA, Humphreys-Beher MG: Effects of epidermal growth factor and nerve growth factor on isoproterenol-induced DNA synthesis in rat parotid and pancreas following removal of submandibular-sublingual glands. J Oral Pathol 17: 250–256, 1988
Schneyer CA, Humphreys-Beher MG: Inhibition of isoproterenol-induced DNA and RNA synthesis in rat parotid and pancreas following removal of the submandibular-sublingual glands. Cell Tiss Res 256: 361–363, 1989
Oliver C, Water JF, Tolbert CL, Kleinman HK: Growth of exocrine acinar cells on a reconstituted basement membrane gel. In Vitro Cell and Developmental Biology 23: 465–473,1987
Schaterle GE, Pollack RL: A simplified method for the quantified assay of small amounts of protein in biologic material. Anal Biochem 51: 654–655, 1973
Loken MR, Stall AM: Flow cytometry as an analytical and preparative tool in immunology. J Immunol Methods 50: R85-R112,1982
Krstulovic AM: Investigations of catecholamine metabolism using high performance liquid chromatography. Analytical methodology and clinical applications. J Chromatogr 229:1–34,1982
Muenzer J, Bildstein C, Gleason M, Carlson DM: Purification of proline-rich proteins from parotid glands of isoproterenol-treated rats. J Biol Chem 254: 5623–5628, 1979
Pugsley AP, Schnaitman CA: Factors affecting the electrophoretic mobility of the major outer membrane proteins of Escherichia coli in polyacrylamide gels. Biochem Biophys Acta 581: 163–178, 1979
Fairbanks G, Steck TL, Wallach DE: Electrophoretic analysis of major polypeptides of the erythrocyte membrane. Biochemistry 10: 2606–2617, 1971
Humphreys-Beher MG, Wells DJ: Metachromatic staining patterns of basic proline-rich proteins from human and rat saliva in sodium dodecyl sulfate-polyacrylamide gels. J Appl Biochem 6: 353–360, 1984
Towbin H, Staehelin T, Gordon J: Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc Natl Acad Sci USA 76: 4350–4354, 1979
Carlin CR, Tollefson AE, Brady HA, Hoffman BL, Wold WSM: Epidermal growth factor receptor is down-regulated by a 10,400 MW protein encoded by the E3 region of adenovirus. Cell 57: 135–144, 1989
Inoue H, Kikuchi K, Nishino M: Effects of epidermal growth factor on the synthesis of DNA and polyamine in isoproterenol-stimulated murine parotid gland. J Biochem 100: 605–613, 1986
Chen WS, Lazar CS, Poene M, Tsien RY, Gill GN, Rosenfeld MG: Requirement for intrinsic protein tyrosine kinase in the immediate and late actions of EGF receptor. Nature 328:820–823,1987
Fujii M, Shalloway D, Verma I: Gene regulation by tyrosine kinases: scr protein activates various poromotors, including c-fos. Molec Cell Biol 9: 2493–2499, 1989
Greene LA, Shooter EM: The nerve growth factor: biochemistry, synthesis and mechanism of action. Annu Rev Neuroscience 3: 353–402, 1980
Banya EM, Runyan RB, Scully NF, Reichner J, Lopez LC, Shur BD: Cell surface galactosyltransferase as a recognition molecule during development. Molec Cell Biochem 72:141–151,1986
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Humphreys-Beher, M.G., Zelles, T., Maeda, N. et al. Cell surface galactosyltransferase acts as a general modulator of rat acinar cell proliferation. Mol Cell Biochem 95, 1–11 (1990). https://doi.org/10.1007/BF00219524
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00219524