The Biochemistry and Physiology of Metallic Fluoride: Action, Mechanism, and Implications

SAGE Publications - Tập 14 Số 2 - Trang 100-114 - 2003
Liang Li1
1Faculty of Dentistry, University of Manitoba, 780 Bannatyne Avenue, Winnipeg R3E 0W2 , MB, Canada;

Tóm tắt

Fluoride is a well-known G protein activator. Activation of heterotrimeric GTP-binding proteins by fluoride requires trace amounts of Al3+ or Be2+ ions. AlFx mimics a γ-phosphate at its transition state in a G α protein and is therefore able to inhibit its GTPase activity. AlFx also forms complexes with small GTP-binding proteins in the presence of their GTPase-activating proteins (GAP). As phosphate analogs, AlFx or BeFx affect the activity of a variety of phosphoryl transfer enzymes. Most of these enzymes are fundamentally important in cell signal transduction or energy metabolism. Al3+ and F- tend to form stable complexes in aqueous solution. The exact structure and concentration of AlFx depend on the pH and the amount of F- and Al3+ in the solution. Humans are exposed to both F and Al. It is possible that Al-F complexes may be formed in vivo, or formed in vitro prior to their intake by humans. Al-F complexes may play physiological or pathological roles in bone biology, fluorosis, neurotoxicity, and oral diseases such as dental caries and periodontal disease. The aim of this review is to discuss the basic chemical, biochemical, and toxicological properties of metallic fluoride, to explore its potential physiological and clinical implications.

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Tài liệu tham khảo

10.1016/S0014-5793(97)00422-5

10.1080/15287399409531849

10.1080/15287399509531963

Anderson NG, Kilgour E, Sturgill TW (1991). Activation of mitogen-activated protein kinase in BC3H1 myocytes by fluoroaluminate. J Biol Chem 266:10131–10135.

10.1177/154411130201300206

10.1007/BF02555250

10.1177/00220345890680070501

10.1021/bi00318a013

10.1177/00220345950740070501

Becker DE, Griffith JM, Hobbs CS, MacIntire WH (1950). The alleviation of fluorine toxicosis by means of certain aluminum compounds. J Animal Sci 9:647–655.

Berry M (1979). Advanced inorganic chemistry. 3rd ed. London: A. Holderness.

10.1016/0014-5793(85)80004-1

10.1002/j.1460-2075.1987.tb02594.x

10.1021/ic991248w

10.1126/science.163487

10.1177/10454411980090010401

10.1016/S0969-2126(00)00145-3

10.1016/0003-9969(72)90086-6

10.1073/pnas.74.8.3307

10.1073/pnas.75.9.4155

Caverzasio J, Imai T, Ammann P, Burgener D, Bonjour JP (1996). Aluminum potentiates the effect of fluoride on tyrosine phosphorylation and osteoblast replication in vitro and bone mass in vivo. J Bone Miner Res 11:46–55.

10.1359/jbmr.1997.12.12.1975

10.1016/S8756-3282(98)00058-1

10.1016/0968-0004(90)90117-T

10.1152/jn.2000.83.3.1273

10.1073/pnas.131213698

10.1006/jmbi.2000.3595

10.1016/S0076-6879(99)08006-4

10.1126/science.8073283

10.1042/bss0670163

10.1016/0003-9969(72)90137-9

Dawes C, Jenkins GN, Hardwick JL, Leach SA (1965). The relationship between fluoride concentrations in the dental plaque and in drinking water. Br Dent J 119:164–167.

10.1177/08959374890030022001

DenBesten PK, Mathews CH, Gao C, Li W (1998). Primary culture and characterization of enamel organ epithelial cells. Connect Tissue Res 38:3-8; discussion 35–41.

10.1046/j.0909-8836.1999.eos107407.x

Downs RW Jr, Spiegel AM, Singer M, Reen S, Aurbach GD (1980). Fluoride stimulation of adenylate cyclase is dependent on the guanine nucleotide regulatory protein. J Biol Chem 255:949–954.

10.1016/0003-9969(70)90076-2

10.1177/08959374940080021101

Emsley J, Hall D (1976). The chemistry of phosphorus: environmental, organic, inorganic, biochemical and spectroscopic aspects. New York: Harper & Row.

10.1126/science.6623079

Feuerstein J, Goody RS, Webb MR (1989). The mechanism of guanosine nucleotide hydrolysis by p21 c-Ha-Ras. The stereochemical course of the GTPase reaction. J Biol Chem 264:6188–6190.

10.1289/ehp.814043

10.1016/S0361-9230(01)00459-2

10.1006/jtbi.1994.1224

10.1016/S8756-3282(01)00625-1

10.1073/pnas.78.1.152

10.1034/j.1600-0722.2000.00735.x

10.1146/annurev.bi.56.070187.003151

10.1021/ac60207a074

10.1016/0005-2736(81)90071-7

10.1177/00220345900690S128

10.1111/j.1600-0528.1984.tb01402.x

10.1016/S0005-2736(98)00064-9

10.1159/000262381

Higashijima T, Ferguson KM, Sternweis PC, Ross EM, Smigel MD, Gilman AG (1987). The effect of activating ligands on the intrinsic fluorescence of guanine nucleotide-binding regulatory proteins. J Biol Chem 262:752–756.

Higashijima T, Graziano MP, Suga H, Kainosho M, Gilman AG (1991). 19F and 31P NMR spectroscopy of G protein alpha subunits. Mechanism of activation by Al3+ and F-. J Biol Chem 266:3396–3401.

Hildebrandt JD, Codina J, Risinger R, Birnbaumer L (1984). Identification of a gamma subunit associated with the adenylyl cyclase regulatory proteins Ns and Ni. J Biol Chem 259:2039–2042.

Howlett AC, Sternweis PC, Macik BA, Van Arsdale PM, Gilman AG (1979). Reconstitution of catecholamine-sensitive adenylate cyclase. Association of a regulatory component of the enzyme with membranes containing the catalytic protein and beta-adrenergic receptors. J Biol Chem 254:2287–2295.

Hubbard MJ (1998). Enamel cell biology. Towards a comprehensive biochemical understanding. Connect Tissue Res 38:17-32; discussion 35–41.

Imai T, Burgener D, Zhen X, Benjour JP, Caverzasio J (1996). Aluminum potentiates P(i) transport stimulation induced by fluoride in osteoblast-like cells. Am J Physiol 271(4 Pt 1):E694–701.

Inoue Y, Fishman PH, Rebois RV (1990). Differential activation of the stimulatory and inhibitory guanine nucleotide-binding proteins by fluoroaluminate in cells and in membranes. J Biol Chem 265:10645–10651.

10.1111/j.1749-6632.1997.tb48426.x

10.1074/jbc.273.18.11354

Kahn RA (1991). Fluoride is not an activator of the smaller (20-25 kDa) GTP-binding proteins. J Biol Chem 266:15595–15597.

Kanaho Y, Moss J, Vaughan M (1985). Mechanism of inhibition of transducin GTPase activity by fluoride and aluminum. J Biol Chem 260:11493–11497.

10.1016/0003-9969(89)90133-7

Kessabi M, Hamliri A, Braun JP (1986). Experimental fluorosis in sheep: alleviating effects of aluminum. Vet Hum Toxicol 28:300–304.

Kleber CJ, Putt MS (1984). Aluminum and dental caries. A review of the literature. Clin Prev Dent 6(6):14–25.

10.1159/000262011

10.1073/pnas.91.21.9828

10.1146/annurev.bi.49.070180.004305

Kraus AS, Forbes WF (1992). Aluminum, fluoride and the prevention of Alzheimer’s disease. Can J Public Health 83:97–100.

10.1016/S8756-3282(02)00671-3

10.1038/83053

10.1002/j.1460-2075.1992.tb05585.x

10.1016/S0014-5793(99)01414-3

10.1016/S0014-5793(99)01196-5

10.1111/j.1600-0528.1994.tb01831.x

Liptrot GF (1974). Modern inorganic chemistry. London: Mills and Boon Ltd.

10.1146/annurev.bi.59.070190.003121

10.1073/pnas.85.23.8958

10.1016/0968-0004(88)90012-6

10.1177/00220345900690S130

10.1093/clinchem/32.10.1797

10.1016/S0006-291X(88)81266-X

10.1021/ar00043a004

10.1016/S0010-8545(96)90008-9

Maruta S, Henry GD, Sykes BD, Ikebe M (1993). Formation of the stable myosin-ADP-aluminum fluoride and myosin-ADP-beryllium fluoride complexes and their analysis using 19F NMR. J Biol Chem 268:7093–7100.

10.1007/s002040050294

10.1007/s002040050576

May DC, Ross EM, Gilman AG, Smigel MD (1985). Reconstitution of catecholamine-stimulated adenylate cyclase activity using three purified proteins. J Biol Chem 260:15829–15833.

10.1016/0092-8674(87)90591-5

Misra UK, Gawdi G, Pizzo SV (2002). Beryllium fluoride-induced cell proliferation: a process requiring P21(ras)-dependent activated signal transduction and NF-kappaB-dependent gene regulation. J Leukoc Biol 71:487–494.

10.1126/science.273.5271.115

10.1177/00220345000790111401

10.1038/366654a0

10.1073/pnas.77.11.6516

Northup JK, Sternweis PC, Gilman AG (1983a). The subunits of the stimulatory regulatory component of adenylate cyclase. Resolution, activity, and properties of the 35,000-dalton β subunit. J Biol Chem 258:11361–11368.

Northup JK, Smigel MD, Sternweis PC, Gilman AG (1983b). The subunits of the stimulatory regulatory component of adenylate cyclase. Resolution of the activated 45,000-dalton α subunit. J Biol Chem 258:11369–11376.

10.1093/clinchem/40.4.598

10.1073/pnas.97.2.538

Pfeuffer T (1977). GTP-binding proteins in membranes and the control of adenylate cyclase activity. J Biol Chem 252:7224–7234.

10.1079/PNS19930056

10.1079/PNS19930055

10.1073/pnas.89.8.3649

10.1016/S0048-9697(96)05347-8

Rall TW, Sutherland EW (1958). Formation of a cyclic adenine ribonucleotide by tissue particles. J Biol Chem 232:1065–1076.

Rall TW, Sutherland EW, Berthet J (1957). The relationship of epinephrine and glucagon to liver phosphorylase. IV. Effect of epinephrine and glucagons on the reactivation of phosphorylase in liver homogenates. J Biol Chem 224:463–475.

10.1191/096032799678839572

10.1038/191184a0

10.1007/s00223-001-1050-x

10.1016/S0065-2571(96)00020-9

Rodbell M, Bimbaumer L, Pohl SL, Krans HM (1971). The glucagon-sensitive adenyl cyclase system in plasma membranes of rat liver. V. An obligatory role of guanylnucleotides in glucagon action. J Biol Chem 246:1877–1882.

Ross EM, Gilman AG (1977). Resolution of some components of adenylate cyclase necessary for catalytic activity. J Biol Chem 252:6966–6969.

Ross EM, Howlett AC, Ferguson KM, Gilman AG (1978). Reconstitution of hormone-sensitive adenylate cyclase activity with resolved components of the enzyme. J Biol Chem 253:6401–6412.

10.1126/science.277.5324.333

10.1016/S0968-0004(98)01224-9

Schindelin H, Kisker C, Schlessman JL, Howard JB, Rees DC (1997). Structure of ADP.AlF; stabilized nitrogenase complex and its implications for signal transduction. Science 387:370–376.

10.1038/11485

10.1016/0014-4835(77)90128-2

10.5694/j.1326-5377.1985.tb123008.x

10.1038/372276a0

10.1111/j.1749-6632.1980.tb21337.x

10.1080/07315724.1985.10720071

Spencer H, Kramer L, Osis D, Wiatrowski E (1985b). Effects of aluminum hydroxide on fluoride and calcium metabolism. J Environ Pathol Toxicol Oncol 6:33–41.

10.1146/annurev.biochem.66.1.639

Stein PJ, Halliday KR, Rasenick MM (1985). Photoreceptor GTP binding protein mediates fluoride activation of phosphodiesterase. J Biol Chem 260:9081–9084.

Sternweis PC, Gilman AG (1979). Reconstitution of catecholamine-sensitive adenylate cyclase. Reconstitution of the uncoupled variant of the S40 lymphoma cell. J Biol Chem 254:3333–3340.

10.1073/pnas.79.16.4888

Sternweis PC, Northup JK, Smigel MD, Gilman AG (1981). The regulatory component of adenylate cyclase. Purification and properties. J Biol Chem 256:11517–11526.

Still CN, Kelley P (1980). On the incidence of primary degenerative dementia vs. water fluoride content in South Carolina. Neurotoxicology 1:125–131.

10.1007/BF00291269

Susa M (1999). Heterotrimeric G proteins as fluoride targets in bone. Int J Mol Med 3:115–126.

10.1006/bbrc.1997.6864

Sutherland EW, Rall TW, Menon T (1962). Adenylate cyclase I. Distribution, preparation and properties. J Biol Chem 237:1220–1227.

10.1128/IAI.55.11.2597-2603.1987

Swift P (1967). A method for the trace elemental analysis of dental tissues. Br Dent J 123:326–327.

10.1073/pnas.161273998

10.1016/S0031-6865(99)00046-1

10.1016/S0006-8993(97)01336-X

10.1159/000016615

Warren JJ, Levy SM (1999). A review of fluoride dentifrice related to dental fluorosis. Pediatr Dent 21:265–271.

10.1177/00220345870660051501

10.1177/00220345900690S108

10.1016/S0960-9822(06)00295-8

Wittinghofer A (1998). Signal transduction via Ras. Biol Chem 379:933–937.

10.1016/S0014-5793(97)00321-9

10.1177/08959374970110042701

10.1073/pnas.96.26.14789

10.1021/ic010245s

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