Fetuin pp 75-102 | Cite as

Functions of Fetuin

  • Katarzyna M. Dziegielewska
  • William M. Brown
Part of the Molecular Biology Intelligence Unit book series (MBIU)

Abstract

No review of fetuin could possibly avoid listing the claimed, counterclaimed and reclaimed possible functions of fetuin. Since its discovery just 50 years ago,1 a whole plethora of papers claiming specific functions for fetuin has appeared in the literature. There have been several excellent reviews on fetuin, especially in tissue culture applications (see refs. 2 and 3 for most recent and comprehensive), so we will not dwell on this aspect of the field for too long.

Keywords

Cholesterol Tyrosine Leukemia Cortisol Trypsin 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Pedersen KO. Fetuin, a new globulin isolated from serum. Nature 1944; 154: 575.Google Scholar
  2. 2.
    Nie Z. Fetuin: its enigmatic property of growth promotion. Am J Physiol 1992; 263: C551–562.PubMedGoogle Scholar
  3. 3.
    Brown WM, Saunders NR, Mollgârd K et al. Fetuin–an old friend revisited. BioEssays 1992; 14: 749–755.PubMedGoogle Scholar
  4. 4.
    Galembeck F, Cann JR. Fetuin as a trypsin inhibitor. Arch Biochem Biophys 1974; 164: 326–331.PubMedGoogle Scholar
  5. 5.
    Westrom BR, Karlsson BW, Svelsen J. Levels of serum protease inhibitors during fetal and postnatal development of the pig. Biol Neonate 1981; 352: 1–10.Google Scholar
  6. 6.
    Yamamoto K, Sinohara H. Isolation and characterization of mouse countertrypsin, a new trypsin inhibitor belonging to the mammalian fetuin family. J Biol Chem 1993; 268: 17750–17753.PubMedGoogle Scholar
  7. 7.
    Dziegielewska KM, Brown WM, Casey SJ et al. The complete cDNA and amino acid sequence of bovine fetuin. Its homology with u2-HS glycoprotein and relation to other members of the cystatin superfamily. J Biol Chem 1990; 265: 4354–7.PubMedGoogle Scholar
  8. 8.
    Stubbs MT, Laber B, Bode W et al. The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction. EMBO J 1990; 9: 1939–47.PubMedGoogle Scholar
  9. 9.
    Johnson WV, Nagarajan M. Analysis of the trypsin inhibitory effect of fetuin. FASEB J 1994; 8: A1425 (abstract).Google Scholar
  10. 10.
    Yamakawa Y, Omori-Satoh T. Primary structure of the antihemorrhagic factor in serum of the Japanese Habu: a snake venom metalloproteinase inhibitor with a double-headed cystatin domain. J Biochem 1992; 112: 583–589.PubMedGoogle Scholar
  11. 11.
    Saitoh E, Isemura S. Molecular biology of human salivary cysteine proteinase inhibitors. Crit Rev Oral Biol Med 1993; 4: 487–493.PubMedGoogle Scholar
  12. 12.
    Saitoh E, Isemura S, Sanada K et al. The human cystatin gene family: cloning of three members and evolutionary relationship between cystatins and Bowman-Birk type proteinase inhibitors. Biomed Biochim Acta 1991; 50: 599–605.PubMedGoogle Scholar
  13. 13.
    Haasemann M, Nawratil P, Müller-Esterl W. Rat tyrosine kinase inhibitor shows sequence similarity to human a2-HS glycoprotein and bovine fetuin. Biochem J 1991; 274: 899–902.PubMedGoogle Scholar
  14. 14.
    Auberger P, Falquerho L, Contreres JO et al. Characterization of a natural inhibitor of the insulin receptor tyrosine kinase. cDNA cloning, purification, and anti-mitogenic activity. Cell 1989; 58: 631–640.PubMedGoogle Scholar
  15. 15.
    Le Cam A, Magnaldo I, Le Cam G et al. Secretion of a major phosphorylated glycoprotein by hepatocytes. Characterization of specific antibodies and investigations of the processing, excretion kinetics, and phosphorylation. J Biol Chem 1985; 260: 15965–15971.PubMedGoogle Scholar
  16. 16.
    Brown WM, Christie DL, Dziegielewska KM et al. The rat protein encoded by clone pp63 is a fetuin/a2-HS glycoprotein-like molecule, but is it the tyrosine kinase inhibitor pp63. Cell 1992; 68: 7–8.PubMedGoogle Scholar
  17. 17.
    Le Cam A, Auberger P, Falquerho L et al. pp63 is very likely the rat fetuin. Cell 1992; 67: 8.Google Scholar
  18. 18.
    Rauth G, Poschke O, Fink E et al. The nucleotide and partial amino acid sequences of rat fetuin. Identity with the natural tyrosine kinase inhibitor of the rat insulin receptor. Eur J Biochem 1992; 204: 523–9.PubMedGoogle Scholar
  19. 19.
    Mizuno M, Farach-Carson MC, Pinero GJ et al. Identification of the rat bone 60K acidic glycoprotein as a2-HS-glycoprotein. Bone and Mineral 1991; 13: 1–21.PubMedGoogle Scholar
  20. 20.
    Ohnishi T, Arakaki N, Nakamura O et al. Purification, characterization, and studies on biosynthesis of a 59-kDa bone sialic acid-containing protein (BSP) from rat mandible using a monoclonal antibody. Evidence that 59-kDa BSP may be the rat counterpart of human a2-HS glycoprotein and is synthesized by both hepatocytes and osteoblasts. J Biol Chem 1991; 266: 14636–14645.PubMedGoogle Scholar
  21. 21.
    Ohnishi T, Nakamura O, Ozawa M et al. Molecular cloning and sequence analysis of cDNA for a 59 kD bone sialoprotein of the rat: demonstration that it is a counterpart of human a2-HS glycoprotein and bovine fetuin. J Bone Mineral Res 1993; 8: 367–377.Google Scholar
  22. 22.
    Brown WM, Dziegielewska KM, Saunders NR et al. The nucleotide and deduced amino acid structures of sheep and pig fetuin. Common structural features of the mammalian fetuin family. Eur J Biochem 1992; 205: 321–331.PubMedGoogle Scholar
  23. 23.
    Ohnishi T, Nakamura O, Arakaki N et al. Effects of cytokines and growth factors on phosphorylated fetuin biosynthesis by adult rat hepatocytes in primary culture. Biochem Biophys Res Comm 1994; 200: 598–605.PubMedGoogle Scholar
  24. 24.
    Spiro RG. Studies on fetuin, a glycoprotein of fetal serum. I. isolation, chemical composition, and physicochemical properties. J Biol Chem 1960; 235: 2860–2869.Google Scholar
  25. 25.
    Schmid K, Bürgi W. Preparation and properties of the human Ba-a2glycoproteins. Biochim Biophys Acta 1961; 47: 440–453.PubMedGoogle Scholar
  26. 26.
    Sbraccia P, Goodman PA, Maddux BA et al. Production of inhibitor of insulin-receptor tyrosine kinase in fibroblasts from patients with insulin resistance and NIDDM. Diabetes 1991; 40: 295–299.PubMedGoogle Scholar
  27. 27.
    Maddux BA, Sbraccia P, Reaven GM et al. Inhibitors of insulin receptor tyrosine kinase in fibroblasts from diverse patients with impaired insulin action: evidence for a novel mechanism of postreceptor insulin resistance. J Clin Endocrinol Metab 1993; 77: 73–79.PubMedGoogle Scholar
  28. 28.
    Srinivas PR, Wagner AS, Reddy LV et al. Serum a2-HS-glycoprotein is an inhibitor of the human insulin receptor at the tyrosine kinase level. Mol Endocrinol 1993; 7: 1445–1455.PubMedGoogle Scholar
  29. 29.
    Salomon DS, Bano M, Smith KB et al. Isolation and characterization of a growth factor (embryonin) from bovine fetuin which resembles a2-macroglobulin. J Biol Chem 1982; 257: 14093–14101.PubMedGoogle Scholar
  30. 30.
    Salomon DS, Smith KB, Losonczy I et al. a2-macroglobulin, a contaminant of commercially prepared Pedersen fetuin: isolation, characterization, and biological activity. In: Cell Culture Methods for Molecular Biology. DW Barnes, DA Sirbasku, and GH Sato, eds. New York: Alan R. Liss, Inc.; 1984.Google Scholar
  31. 31.
    Libby P, Raines EW, Cullinane PM et al. Analysis of the mitogenic effect of fetuin preparations on arterial smooth muscle cells: the role of contaminant platelet-derived growth factor. J Cell Physiol 1985; 125: 357–366.PubMedGoogle Scholar
  32. 32.
    Subbiah MT. Newly recognized lipid carrier proteins in fetal life. Proc Soc Exptl Biol Med 1991; 198: 495–499.Google Scholar
  33. 33.
    Kumbla L, Bhadra S, Subbiah MT. Multifunctional role for fetuin (fetal protein) in lipid transport. FASEB J 1991; 5: 2971–2975.PubMedGoogle Scholar
  34. 34.
    Kumbla L, Cayatte AJ, Subbiah MT. Association of a lipoprotein-like particle with bovine fetuin. FASEB J 1989; 3: 2075–2080.PubMedGoogle Scholar
  35. 35.
    Brown WM. The plasma protein fetuin: common structural features of the mammalian fetuin family. PhD thesis, University of Southampton, UK; 1991.Google Scholar
  36. 36.
    Cayatte AJ, Kumbla L, Subbiah MT. Marked acceleration of exogenous fatty acid incorporation into cellular triglycerides by fetuin. J Biol Chem 1990; 265: 5883–5888.PubMedGoogle Scholar
  37. 37.
    Stein O, Haratz D, Scwartz R et al. Modification of cellular fatty acid composition of Hep-G2 cells: effect of antioxidants on cholesterol esterification and secretion. Biochim Biophys Acta 1989; 1003: 115–120.PubMedGoogle Scholar
  38. 38.
    Gaillard D, Ailhaud G, Negrel R. Fetuin modulates growth and differentiation of Ob17 preadipose cells in serum-free hormone-supplemented medium. Biochim Biophys Acta 1985; 846: 185–191.PubMedGoogle Scholar
  39. 39.
    Zaitsu H, Serrero G. Pedersen fetuin contains three adipogenic factors with distinct Biochemical characteristics. J Cell Physiol 1990; 144: 485–491.PubMedGoogle Scholar
  40. 40.
    Bachmeier M, Loftier G. Adipogenic activities in commercial preparations of fetuin. Horm Metab Res 1994; 26: 92–96.PubMedGoogle Scholar
  41. 41.
    Fisher DA, Lam RW. Thyroid hormone binding by bovine and ovine fetuin. Endocrinology 1974; 94: 49–54.PubMedGoogle Scholar
  42. 42.
    Lewis JG, André C. A serum DNA-binding protein absent in malignant disease. FEBS Letts 1978; 92: 211–213.Google Scholar
  43. 43.
    Wilson JM, Ashton B, Triffitt JT. The interaction of a component of bone organic matrix with the mineral phase. Calcif Tiss Res 1977; 22: 458–460.Google Scholar
  44. 44.
    Yang F, Schwartz Z, Swain LD et al. a2-HS-glycoprotein: expression in chondrocytes and augmentation of alkaline phosphatase and phospholipase A2 activity. Bone 1991; 12: 7–15.PubMedGoogle Scholar
  45. 45.
    Ishiguro H, Higashiyama S, Namikawa C et al. Interaction of human calpains I and II with high molecular weight and low molecular weight kininogens and their heavy chain: mechanism of interaction and the role of divalent cations. Biochemistry 1987; 26: 2863–2870.PubMedGoogle Scholar
  46. 46.
    Higashiyama S, Ohkubo I, Ishiguro H et al. Heavy chain of human high molecular weight and low molecular weight kininogens binds calcium ion. Biochemistry 1987; 26: 7450–7458.PubMedGoogle Scholar
  47. 47.
    Kretsinger RH. Calcium coordination and the calmodulin fold: divergent versus convergent evolution. Cold Spring Harbor Symp Quant Biol 1987; 52: 499–510.PubMedGoogle Scholar
  48. 48.
    Bairoch A, Cox JA. EF-hand motifs in inositol phospholipid-specific phospholipase C. FEBS Letts 1990; 269: 454–456.Google Scholar
  49. 49.
    Ozawa M, Muramatsu T. Reticulocalbin, a novel endoplasmic reticulum resident Cat`-binding protein with multiple EF-hand motifs and a carboxyl-terminal HDEL sequence. J Biol Chem 1993; 268: 699–705.PubMedGoogle Scholar
  50. 50.
    Tuckwell DS, Brass A, Humphries MJ. Homology modelling of integrin EF-hands. Evidence for widespread use of a conserved cation binding site. Biochem J 1992; 285: 325–331.PubMedGoogle Scholar
  51. 51.
    Weinman S. Calcium-binding proteins: an overview. J Biol Chem 1991; 19: 90–98.Google Scholar
  52. 52.
    Kretsinger RH, Nakayama S. Evolution of EF-hand calcium-modulated proteins. IV. Exon shuffling did not determine the domain composition of EF-hand proteins. J Mol Evol 1993; 36: 477–488.PubMedGoogle Scholar
  53. 53.
    Nakayama S, Kretsinger RH. Evolution of EF-hand calcium-modulated proteins. III. Exon sequences confirm most dendrograms based on protein sequence: calmodulin dendrograms show significant lack of parallelism. J Mol Evol 1993; 36: 458–476.PubMedGoogle Scholar
  54. 54.
    Kawasaki H, Kretsinger RH. Calcium-binding proteins, 1. EF-hands. Protein Profile 1994; 1: 343.PubMedGoogle Scholar
  55. 55.
    Sakane F, Yamada K, Kanoh H et al. Porcine diacylglycerol kinase sequence has zinc finger and EF hand motifs. Nature 1990; 344: 345–348.PubMedGoogle Scholar
  56. 56.
    Putkey JA, Ts’ui KF, Tanaka T et al. Chicken calmodulin genes. A comparison of cDNA sequences and isolation of a genomic clone. J Biol Chem 1983; 258: 11864–11870.PubMedGoogle Scholar
  57. 57.
    Wilkinson JM. Troponin C from rabbit slow skeletal and cardiac muscle is the product of a single gene. Eur J Biochem 1980; 103: 179–188.PubMedGoogle Scholar
  58. 58.
    Tufty RM, Kretsinger RH. Troponin and parvalbumin calcium binding regions predicted in myosin light chain and T4 lysozyme. Science 1975; 187: 167–169.PubMedGoogle Scholar
  59. 59.
    Kuwano R, Maeda T, Usui H et al. Molecular cloning of cDNA of S100-alpha subunit mRNA. FEBS Letts 1986; 202: 97–101.Google Scholar
  60. 60.
    Emori Y, Kawasaki H, Sugihara H et al. Isolation and sequence analyses of cDNA clones for the large subunits of two isozymes of rabbit calcium-dependent protease. J Biol Chem 1986; 261: 9465–9471.PubMedGoogle Scholar
  61. 61.
    von Bulow FA, Janas MS, Terkelsen OB et al. Human fetuin/a2-HS glycoprotein in colloid and parenchymal cells in human fetal pituitary gland. Histochem 1993; 99: 13–22.Google Scholar
  62. 62.
    Yachnin S. Fetuin, an inhibitor of lymphocyte transformation. The interaction of fetuin with phytomitogens and a possible role for fetuin in fetal development. J Exp Med 1975; 141: 242–256.Google Scholar
  63. 63.
    Splitter GA, Everlith KM. Suppression of bovine T- and B-lymphocyte responses by fetuin, a bovine glycoprotein. Cell Immunol 1982; 70: 205–218.PubMedGoogle Scholar
  64. 64.
    Lewis JG, Andre CM. Effect of human a2-HS glycoprotein on mouse macrophage function. Immunol 1980; 39: 317–322.Google Scholar
  65. 65.
    Jakab L, Jakab L, Kalabay L et al. The effect of the a2-HS-glycoprotein on the mitogen-induced lymphoblastic transformation and IL-2 production. Acta Physiol [Hung] 1991; 77: 25–31.Google Scholar
  66. 66.
    Hsu CCS, Floyd M. Lymphocyte stimulating and immunochemical properties of fetuin preparation. Protides Biol Fluids 1976; 24: 295–302.Google Scholar
  67. 67.
    van Oss CJ, Gillman CF, Bronson PM et al. Opsonic properties of human serum a2-HS glycoprotein. Immunol Commun 1974; 3: 329–335.PubMedGoogle Scholar
  68. 68.
    van Oss CJ, Bronson PM. Isolation of human serum a2-HS glycoprotein. Prep Biochem 1974; 4: 127–139.PubMedGoogle Scholar
  69. 69.
    Colclasure GG, Lloyd WS, Lamkin M et al. Human serum a2-HS glycoprotein modulates in vitro bone resorption. J Clin Endocrin Metab 1988; 66: 187–192.Google Scholar
  70. 70.
    Ishikawa Y, Wu LN, Valhmu WB et al. Fetuin and a2-HS glycoprotein induce alkaline phosphatase in epiphyseal growth plate chondrocytes. J Cell Physiol 1991; 149: 222–234.PubMedGoogle Scholar
  71. 71.
    Mollgord K, Reynolds ML, Jacobsen M et al. Differential immunocytochemical staining for fetuin and transferrin in the developing cortical plate. J Neurocytol 1984; 13: 497–502.Google Scholar
  72. 72.
    Reynolds ML, Sarantis ME, Lorscheider FL et al. Fetuin as a marker of cortical plate cells in the fetal cow neocortex: a comparison of the distribution of fetuin, a2-HS-glycoprotein, a-fetoprotein and albumin during early development. Anat Embryol 1987; 175: 355–363.PubMedGoogle Scholar
  73. 73.
    Dziegielewska KM, Mollg$rd K, Reynolds ML et al. A fetuin-related glycoprotein (a2-HS) in human embryonic and fetal development. Cell Tiss Res 1987; 248: 33–41.Google Scholar
  74. 74.
    Dziegielewska KM, Reader M, Matthews N et al. Synthesis of the foetal protein fetuin by early developing neurons in the immature neocortex. J Neurocytol 1993; 22: 266–272.PubMedGoogle Scholar
  75. 75.
    Lewis JG, André CM. Enhancement of human monocyte function by a2-HS glycoprotein. Immunol 1981; 42: 481–487.Google Scholar
  76. 76.
    Lewis JG, André CM. The a2-HS glycoprotein receptor on lymphocytes transformed by Epstein-Barr virus. FEBS Letts 1982; 143: 332–336.Google Scholar
  77. 77.
    Lewis JG, Crosier PS, André CM. a2-HS glycoprotein binds to lymphocytes transformed by Epstein-Barr virus. FEBS Letts 1982; 138: 37–39.Google Scholar
  78. 78.
    Malone JD, Teitelbaum SL, Griffin GL et al. Recruitment of osteoclast precursors by purified bone matrix constituents. J Cell Biol 1982; 92: 227–230.PubMedGoogle Scholar
  79. 79.
    Lewis JG, André CM. The effect of a2-HS glycoprotein on lymphocyte reactivity to phytohemagglutinin. Immunol Comm 1984; 13: 35–47.Google Scholar
  80. 80.
    White H, Totty N, Panayotou G. Haemonectin, a granulocytic-cell-binding protein, is related to the plasma glycoprotein fetuin. Eur J Biochem 1993; 213: 523–528.PubMedGoogle Scholar
  81. 81.
    Dziegielewska KM, Deal A, Foster K et al. Expression of fetuin in the developing and adult tissues of the lymphoid system. J Biol Chem 1994; submitted.Google Scholar
  82. 82.
    Ashton BA, Hohling H, Triffitt JT. Plasma proteins present in human cortical bone:enrichment of the a2-HS glycoprotein. Calcif Tiss Res 1976; 22: 27–33.Google Scholar
  83. 83.
    Triffitt JT, Gebauer U, Ashton BA et al. Origin of plasma a2-HS glycoprotein and its accumulation in bone. Nature 1976; 262: 226–227.PubMedGoogle Scholar
  84. 84.
    Smith AJ, Matthews JB, Wilson C et al. Plasma proteins in human cortical bone: in vitro binding studies. Calcif Tiss Res 1985; 37: 208–210.Google Scholar
  85. 85.
    Quelch KJ, Cole WG, Melick RA. Noncollagenous proteins in normal and pathological human bone. Calcif Tiss Int 1984; 36: 545–549.Google Scholar
  86. 86.
    Cavanagh ME, M0llgàrd K. An immunocytochemical study of the distribution of some plasma proteins within the developing forebrain of the pig with special reference to the neocortex. Brain Res 1985; 349: 183–194.PubMedGoogle Scholar
  87. 87.
    Jones SE. Developmental profile of a fetuin-like glycoprotein in neocortex, cerebrospinal fluid and plasma of postnatal tammar wallaby (Macropus eugenii). PhD thesis, University of Southampton, UK; 1990.Google Scholar
  88. 88.
    Jones SE, Christie DL, Dziegielewska KM et al. Developmental profile of a fetuin-like glycoprotein in neocortex, cerebrospinal fluid and plasma of post-natal tammar wallaby (Macropus eugenii). Anat Embryol 1991; 183: 313–320.PubMedGoogle Scholar
  89. 89.
    Saunders NR, Sheardown S, Deal A et al. Expression and distribution of fetuin in the developing sheep fetus. Histochem 1994; 102: 457–475.Google Scholar
  90. 90.
    Freyd G, Kim SK, Horvitz HR. Novel cysteine-rich motif and homeodomain in the product of the Caenorhabditis elegans lineage gene lin-11. Nature 1990; 344: 876–879.PubMedGoogle Scholar
  91. 91.
    Huber R, Carrell RW. Implications of the three-dimensional structure of a,-antitrypsin for structure and function of serpins. Biochemistry 1989; 28: 8951–8966.PubMedGoogle Scholar
  92. 92.
    Pemberton PA, Stein PE, Pepys MB et al. Hormone binding globulins undergo serpin conformational change in inflammation. Nature 1988; 336: 257–258.PubMedGoogle Scholar
  93. 93.
    Way JC, Chalfie M. mec-3, a homeobox-containing gene that specifies differentiation of the touch receptor neurons in C. elegans. Cell 1988; 54: 5–16.PubMedGoogle Scholar
  94. 94.
    Way JC, Chalfie M. The mec-3 gene of Caenorhabditis elegans requires its own product for maintained expression and is expressed in three neuronal cell types. Genes Dev 1989; 3: 1823–1833.PubMedGoogle Scholar
  95. 95.
    Way JC, Wang L, Run JQ et al. The mec-3 gene contains cis-acting elements mediating positive and negative regulation in cells produced by asymmetric cell division in Caenorhabditis elegans. Genes Dev 1991; 5: 2199–2211.PubMedGoogle Scholar
  96. 96.
    Way JC, Run JQ, Wang AY. Regulation of anterior cell-specific mec-3 expression during asymmetric cell division in C. elegans. Dev Dynamics 1992; 194: 289–302.Google Scholar
  97. 97.
    Karlsson O, Thor S, Norberg T et al. Insulin gene enhancer binding protein Isl-1 is a member of a novel class of proteins containing both a homeoand a cys-his domain. Nature 1990; 344: 879–882.PubMedGoogle Scholar
  98. 98.
    Wilks AF, Harpur AG. Cytokine signal transduction and the JAK family of protein tyrosine kinases. BioEssays 1994; 16: 313–320.PubMedGoogle Scholar
  99. 99.
    Rose-John S, Heinrich PC. Soluble receptors for cytokines and growth factors: generation and biological function. Biochem J 1994; 300: 281–290.PubMedGoogle Scholar
  100. 100.
    Dynan WS, Tjian R. Control of eukaryotic messenger RNA synthesis by sequence specific DNA binding proteins. Nature 1985; 316: 774–778.PubMedGoogle Scholar
  101. 101.
    Maniatis T, Goodbourn S, Fischer JA. Regulation of inducible and tissue-specific gene expression. Science 1987; 236: 1237–1245.PubMedGoogle Scholar
  102. 102.
    Ptashne M. How eukaryotic transcriptional activators work. Nature 1988; 335: 683–689.PubMedGoogle Scholar
  103. 103.
    Wasylyk B. Enhancers and transcription factors in the control of gene expression. Biochim Biophys Acta 1988; 951: 17–35.PubMedGoogle Scholar
  104. 104.
    Johnson PF, McKnight SL. Eukaryotic transcriptional regulatory proteins. Ann Rev Biochem 1989; 58: 799–839.PubMedGoogle Scholar
  105. 105.
    Latchman DS. Eukaryotic transcription factors. Biochem J 1990; 270: 281–189.PubMedGoogle Scholar
  106. 106.
    Latchman DS. Transcription factors: an overview. Int J Exp Pathol 1993; 74: 417–422.PubMedGoogle Scholar
  107. 107.
    Drapkin R, Merino A, Reinberg D. Regulation of RNA polymerase II transcription. Current Opinion in Cell Biology 1993; 5: 469–476.PubMedGoogle Scholar
  108. 108.
    Buratowski S. The basics of basal transcription by RNA polymerase II. Cell 1994; 77: 1–3.PubMedGoogle Scholar
  109. 109.
    Tjian R, Maniatis T. Transcriptional activation: a complex puzzle with few easy pieces. Cell 1994; 77: 5–8.PubMedGoogle Scholar
  110. 110.
    Drapkin R, Sancar A, Reinberg D. Where transcription meets repair. Cell 1994; 77: 9–12.PubMedGoogle Scholar
  111. 111.
    Wolfe AP. Transcription: in tune with the histones. Cell 1994; 77: 13–16.Google Scholar
  112. 112.
    Borgmeyer U, Nowock J, Sippel AE. The TGGCA-binding protein: a eukaryotic nuclear protein recognizing a symmetrical sequence on double-stranded linear DNA. Nucleic Acids Res 1984; 12: 4295–4311.PubMedGoogle Scholar
  113. 113.
    Lichtsteiner S, Wuarin J, Schibler U. The interplay of DNA-binding proteins on the promoter of the mouse albumin gene. Cell 1987; 51: 963–973.PubMedGoogle Scholar
  114. 114.
    Jones KA, Kadonaga JT, Rosenfeld PJ et al. A cellular DNA-binding protein that activates eukaryotic transcription and DNA replication. Cell 1987; 48: 79–89.PubMedGoogle Scholar
  115. 115.
    Raymondjean M, Cereghini S, Yaniv M. Several distinct “CCAAT” box binding proteins coexist in eukaryotic cells. Proc Natl Acad Sci USA 1988; 85: 757–761.PubMedGoogle Scholar
  116. 116.
    Gerster T, Matthias P, Thali M et al. Cell type-specificity elements of the immunoglobulin heavy chain gene enhancer. EMBO J 1987; 6: 1323–1330.PubMedGoogle Scholar
  117. 117.
    Rosales R, Vigneron M, Macchi M et al. In vitro binding of cell-specific and ubiquitous nuclear proteins to the octamer motif of the SV40 enhancer and related motifs present in other promoters and enhancers. EMBO J 1987; 6: 3015–3025.PubMedGoogle Scholar
  118. 118.
    Bohmann D, Keller W, Dale T et al. A transcription factor which binds to the enhancers of SV40, immunoglobulin heavy chain and U2 snRNA genes. Nature 1987; 325: 268–272.PubMedGoogle Scholar
  119. 119.
    Fletcher C, Heintz N, Roeder RG. Purification and characterization of OTF-1, a transcription factor regulating cell cycle expression of a human histone H2b gene. Cell 1987; 51: 773–781.PubMedGoogle Scholar
  120. 120.
    Sturm R, Herr W. The POU domain is a bipartite DNA-binding structure. Nature 1988; 336: 601–604.PubMedGoogle Scholar
  121. 121.
    Schorpp M, Kugler W, Wagner U et al. Hepatocyte-specific promoter element HP1 of the Xenopus albumin gene interacts with transcription factors of mammalian hepatocytes. J Mol Biol 1988; 202: 307–320.PubMedGoogle Scholar
  122. 122.
    Courtois G, Morgan JG, Campbell LA et al. Interaction of a liver-specific nuclear factor with fibrinogen and a-1-antitrypsin promoters. Science 1987; 238: 688–692.PubMedGoogle Scholar
  123. 123.
    Courtois G, Baumhueter S, Crabtree GR. Purified hepatocyte nuclear factor 1 interacts with a family of hepatocyte-specific promoters. Proc Natl Acad Sci USA 1988; 85: 7937–7941.PubMedGoogle Scholar
  124. 124.
    Hardon EM, Frain M, Paonessa G et al. Two distinct factors interact with the promoter region of several liver-specific genes. EMBO J 1988; 7: 1711–1719.PubMedGoogle Scholar
  125. 125.
    Frain M, Swart G, Monaci P et al. The liver-specific transcription factor LF-B1 contains a highly diverged homeobox DNA binding domain. Cell 1989; 59: 145–157.PubMedGoogle Scholar
  126. 126.
    Baumhueter S, Mendel DB, Conley PB et al. HNF-1 shares three sequence motifs with the POU domain proteins and is identical to LF-B1 and APF. Genes Dev 1990; 4: 372–379.PubMedGoogle Scholar
  127. 127.
    Landschulz WH, Johnson PF, Adashi EY et al. Isolation of a recombinant copy of a gene encoding C/EBP. Genes Dev 1988; 2: 786–800.PubMedGoogle Scholar
  128. 128.
    Landschulz WH, Johnson PF, McKnight SL. The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins. Science 1988; 240: 1759–1764.PubMedGoogle Scholar
  129. 129.
    Landschulz WH, Johnson PF, McKnight SL. The DNA binding domain of the rat liver protein C/EBP is bipartite. Science 1989; 243: 1681–1688.PubMedGoogle Scholar
  130. 130.
    Hurst HC. Transcription factors 1: bZIP proteins. Protein Profile 1994.Google Scholar
  131. 131.
    Angel P, Imagawa M, Chiu R et al. Phorbol ester-inducible genes contain a common cis element recognized by a TPA-modulated trans-acting factor. Cell 1987; 49: 729–739.PubMedGoogle Scholar
  132. 132.
    Lee W, Mitchell ‘P, Tjian R. Purified transcription factor AP-1 interacts with TPA-inducible enhancer elements. Cell 1987; 49: 741–752.PubMedGoogle Scholar
  133. 133.
    Angel P, Karin M. The role of jun, fos and the AP-1 comlex in cell-proliferation and transformation. Biochim Biophys Acta 1991; 1072: 129–157.PubMedGoogle Scholar
  134. 134.
    Lin A, Smeal T, Binetruy B et al. Control of AP-1 activity by signal transduction cascades. Advances in Second Messenger and Phosphoprotein Research 1993; 28: 255–260.PubMedGoogle Scholar
  135. 135.
    Radler-Pohl A, Gebel S, Sachsenmaier C et al. The activation and activity control of Ap-1 (fos/jun). Ann NY Acad Sci 1993; 684: 127–148.PubMedGoogle Scholar
  136. 136.
    Woodgett JR, Pulverer BJ, Nikolakaki E et al. Regulation of jun/AP-1 oncoproteins by protein phosphorylation. Advances in Second Messenger and Phosphoprotein Research 1993; 28: 261–269.PubMedGoogle Scholar
  137. 137.
    Morgan WD, Williams GT, Morimoto RI et al. Two transcriptional activators, CCAAT-box binding transcription factor and heat shock transcription factor, interact with a human hsp70 gene promoter. Mol Cell Biol 1987; 7: 1129–1138.PubMedGoogle Scholar
  138. 138.
    Wu C, Wilson S, Walker B et al. Purification and properties of Drosophila heat shock activator protein. Science 1987; 238: 1247–1253.PubMedGoogle Scholar
  139. 139.
    Sorger PK, Pelham HRB. Purification and characterization of a heat-shock element binding protein from yeast. EMBO J 1987; 6: 3035–3041.PubMedGoogle Scholar
  140. 140.
    Sorger PK, Pelham HRB. Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation. Cell 1988; 54: 855–864.PubMedGoogle Scholar
  141. 141.
    Gilman MZ, Wilson RN, Weinberg RA. Multiple protein-binding sites in the 5’-flanking region regulate c-fos expression. Mol Cell Biol 1986; 6: 4305–4316.PubMedGoogle Scholar
  142. 142.
    Prywes R, Roeder RG. Inducible binding of a factor to the c-fos enhancer. Cell 1986; 47: 777–784.PubMedGoogle Scholar
  143. 143.
    Treisman R. Transient accumulation of c-fos RNA following serum stimulation requires a conserved 5’ element and c-fos 3’ sequences. Cell 1985; 42: 889–902.PubMedGoogle Scholar
  144. 144.
    Treisman R. Identification of a protein-binding site that mediates transcriptional response of the c-fos gene to serum factors. Cell 1986; 46.Google Scholar
  145. 145.
    Treisman R. Identification and purification of a polypeptide that binds to the c-fos serum response element. EMBO J 1987; 6: 2711–2717.PubMedGoogle Scholar
  146. 146.
    Treisman R. The SRE: a growth factor responsive transcriptional regulator. Seminars in Cancer Biology 1990; 1: 47–58.PubMedGoogle Scholar
  147. 147.
    Treisman R. The serum response element. Trends. Biochem Sci 1992; 17: 423–426.PubMedGoogle Scholar
  148. 148.
    Pollock R, Treisman R. Human SRF-related proteins: DNA-binding properties and potential regulatory targets. Genes Dev 1991; 5: 2327–2341.PubMedGoogle Scholar
  149. 149.
    Dalton S, Treisman R. Characterization of SAP-1, a protein recruited by serum response factor to the c-fos serum response element. Cell 1992; 68: 597–612.PubMedGoogle Scholar
  150. 150.
    Treisman R, Ammerer G. The SRF and MCM1 transcription factors. Current Opinion in Genetics and Development 1.ï92; 2: 221–226.Google Scholar
  151. 151.
    Wynne J, Treisman R. SRF and MCM1 have related but distinct DNA binding specificities. Nucleic Acids Res 1992; 20: 3297–3303.PubMedGoogle Scholar
  152. 152.
    Marais R, Wynne J, Treisman R. The SRF accessory protein Elk-1 contains a growth factor-regulated transcriptional activation domain. Cell 1993; 73: 381–393.PubMedGoogle Scholar
  153. 153.
    Dalton S, Marais R, Wynne J et al. Isolation and characterization of SRF accessory proteins. Phil Trans R Soc, London, B, Biol Sci 1993; 340: 325–332.Google Scholar
  154. 154.
    Hill CS, Marais R, John S et al. Functional analysis of a growth factor-responsive transcription factor. Cell 1993; 73: 395–406.PubMedGoogle Scholar
  155. 155.
    Falquerho L, Patey G, Paquereau L et al. Primary structure of the rat gene encoding an inhibitor of the insulin receptor tyrosine kinase. Gene 1991; 98: 209–216.PubMedGoogle Scholar
  156. 156.
    Genetics Computer Group. Program manual for the GCG package. Version 7, April 1991.Google Scholar
  157. 157.
    Ghosh D. A relational database of transcription factors. Nucleic Acids Res 1990; 18: 1749–1756.PubMedGoogle Scholar
  158. 158.
    Ghosh D. Status of the transcription factor database (TFD). Nucleic Acids Res 1993; 21: 3117–3118.PubMedGoogle Scholar
  159. 159.
    Falquerho L, Paquereau L, Vilarem MJ et al. Functional characterization of the promoter of pp63, a gene encoding a natural inhibitor of the insulin receptor tyrosine kinase. Nucleic Acids Res 1992; 20: 1983–1990.PubMedGoogle Scholar
  160. 160.
    Akhoundi C, Amiot M, Auberger P et al. Insulin and interleukin-1 differentially regulate pp63, an acute phase phosphoprotein in hepatoma cell line. J Biol Chem 1994; 269: 15925–15930.PubMedGoogle Scholar
  161. 161.
    Yang F, Chen ZL, Bergeron JM et al. Human a2-HS-glycoprotein/bovine fetuin homologue in mice: identification and developmental regulation of the gene. Biochim Biophys Acta 1992; 1130: 149–156.PubMedGoogle Scholar
  162. 162.
    van Oss CJ, Bronson PM, Border JR. Changes in serum alpha glycoprotein distribution in trauma patients. J Trauma 1975; 15: 451–455.PubMedGoogle Scholar
  163. 163.
    Lebreton JP, Joisel F, Raoult JP et al. Serum concentration of human a 2-HS glycoprotein during the inflammatory process: evidence that a2-HS glycoprotein is a negative acute-phase reactant. J Clin Invest 1979; 64: 1118–1129.PubMedGoogle Scholar
  164. 164.
    Baskies AM, Chretien PB, Weiss JF et al. Serum glycoproteins in cancer patients: first report of correlations with in vitro and in vivo parameters of cellular immunity. Cancer 1980; 45: 3050–60.PubMedGoogle Scholar
  165. 165.
    Daveau M, Christian-Davrinche, Julen N et al. The synthesis of human a2-HS glycoprotein is down-regulated by cytokines in hepatoma HepG2 cells. FEBS Letts 1988; 241: 191–194.Google Scholar
  166. 166.
    Dziegielewska KM, Brown WM, Gould CC et al. Fetuin: an acute phase protein in cattle. J Comp Physiol [B] 1992; 162: 168–171.Google Scholar
  167. 167.
    Daveau M, Davrinche C, Djelassi N et al. Partial hepatectomy and mediators of inflammation decrease the expression of liver a2-HS glycoprotein gene in rats. FEBS Letts 1990; 273: 79–81.Google Scholar
  168. 168.
    Kalabay L, Jakab L, Cseh K et al. Correlations between serum a2-HSglycoprotein concentration and conventional laboratory parameters in systemic lupus erythematosus. Acta Med [Hung] 1990; 47: 53–64.Google Scholar
  169. 169.
    Kalabay L, Cseh K, Benedek S et al. Serum a2-HS glycoprotein concentration in patients with hematological malignancies. A follow-up study. Ann Hematol 1991; 63: 264–269.PubMedGoogle Scholar
  170. 170.
    Kalabay L, Cseh K, Jakab L et al. Diagnostic value of the determination of serum a2-HS-glycoprotein. [Hung] Ory Hetil 1992; 133: 1553–4; 1559–60.Google Scholar
  171. 171.
    Ashton BA, Smith R. Plasma a2-HS glycoprotein concentration in Paget’s disease of bone: its possible significance. Clin Sci 1980; 58: 435–438.PubMedGoogle Scholar
  172. 172.
    Schelp FP, Thanangkul O, Supawan V et al. a2-HS glycoprotein serum levels in protein-energy malnutrition. Br J Nutr 1980; 43: 381–383.PubMedGoogle Scholar
  173. 173.
    Abiodun PO, Ihongbe JC, Dati F. Decreased levels of a2-HS glycoprotein in children with protein-energy-malnutrition. Eur J Pediatr 1985; 144: 368–369.PubMedGoogle Scholar
  174. 174.
    Abiodun PO, Olomu IN. a2-HS-glycoprotein levels in children with protein-energy malnutrition and infections. J Pediatr Gastroenterol Nutr 1987; 6: 271–275.PubMedGoogle Scholar
  175. 175.
    Crawford SM. a2-HS glycoprotein in the hypercalcaemia of multiple myeloma. Br J Cancer 1984; 49:813–815.Google Scholar
  176. 176.
    Dickson IR, Bagga M, Paterson CR. Variations in the serum concentration and urine excretion of a2-HS glycoprotein, a bone-related protein, in normal individuals and in patients with osteogenesis imperfecta. Calcif Tiss Int 1983; 35: 16–20.Google Scholar
  177. 177.
    Won K, Baumann H. The cytokine response element of the rat at-acid glycoprotein gene is a complex of several interacting regulatory sequences. Mol Cell Biol 1990; 10: 3965–3978.PubMedGoogle Scholar
  178. 178.
    Goyal N, Knox J, Gronostajski RM. Analysis of multiple forms of nuclear factor I in human and murine cell lines. Mol Cell Biol 1990; 10: 1041–1048.PubMedGoogle Scholar
  179. 179.
    Jackson DA, Rowader KE, Stevens K et al. Modulation of liver-specific transcription by interactions between hepatocyte nuclear factor 3 and nuclear factor 1 binding in close apposition. Mol Cell Biol 1993; 13: 2401–2410.PubMedGoogle Scholar
  180. 180.
    Gil G, Smith JR, Goldstein JL et al. Multiple genes encode nuclear factor 1-like proteins that bind to the promoter for 3-hydroxy-3-methyl-glutarylcoenzyme A reductase. Proc Natl Acad Sci USA 1988; 85: 8963–8967.PubMedGoogle Scholar
  181. 181.
    Paonessa G, Gounari F, Frank R et al. Purification of a NF 1-like DNA-binding protein from rat liver and cloning of the corresponding cDNA. EMBO J 1988; 7: 3115–3123.PubMedGoogle Scholar
  182. 182.
    Santoro C, Mermod N, Andrews PC et al. A family of human CCAATbox binding proteins active in transcription and DNA replication: cloning and expression of multiple cDNAs. Nature 1988; 334: 218–224.PubMedGoogle Scholar
  183. 183.
    Meisterernst M, Rogge L, Foeckler R et al. Structural and functional organization of a porcine gene coding for nuclear factor I. Biochemistry 1989; 28: 8191–8200.PubMedGoogle Scholar
  184. 184.
    Rupp RAW, Kruse U, Multhaup G et al. Chicken NF 1 /TGGCA proteins are encoded by at least three independent genes: NF 1/A, NF1-B and NF1-C with homologues in mammalian genomes. Nucleic Acids Res 1990; 18: 2607–2616.PubMedGoogle Scholar
  185. 185.
    Weinstein IB, Lee L, Fisher PB et al. Action of phorbol esters in cell culture: mimicry of transformation, altered differentiation, and effects on cell membranes. J Supramol Struct 1979; 12: 195–208.PubMedGoogle Scholar
  186. 186.
    Slaga TJ. Cellular and molecular mechanisms of tumour promotion. Cancer Surveys 1983; 2: 595–612.Google Scholar
  187. 187.
    Greenberg ME, Ziff EB. Stimulation of 3T3 cells induces transcription of the c-fos proto-oncogene. Nature 1984; 311: 433–438.PubMedGoogle Scholar
  188. 188.
    Kruijer W, Cooper JA, Hunter T et al. Platelet-derived growth factor induces rapid but transient expression of the c-fos gene. Nature 1984; 312: 711–716.PubMedGoogle Scholar
  189. 189.
    Kelly K, Cochran BH, Stiles CD et al. Cell-specific regulation ofthe cmyc gene by lymphocyte mitogens and platelet-derived growth factor. CellGoogle Scholar
  190. 1983;.
    :603–610.Google Scholar
  191. 190.
    Colamonici OR, Trepel JB, Vidal CA et al. Phorbol ester induces c-sis gene transcription in stem cell line K-562. Mol Cell Biol 1986; 6: 1847–1850.PubMedGoogle Scholar
  192. 191.
    Lerman MI, Colburn NH. Pro genes: a novel class of genes that specify sensitivity to induction of neoplastic transformation by tumor promoters. In: Tumor promotion: biological approaches for mechanistic studies and assay systems. Langenbach R, Barrett JC, Elmore E, eds. New York: Raven Press 1987.Google Scholar
  193. 192.
    Whitham SE, Murphy G, Angel P et al. Comparison of human stromelysin and collagenase by cloning and sequence analysis. Biochem J 1986; 240: 913–916.PubMedGoogle Scholar
  194. 193.
    Matrisian LM, Leroy P, Ruhlmann C et al. Isolation of the oncogene and epidermal growth factor-induced transin gene: complex control in rat fibroblasts. Mol Cell Biol 1986; 6: 1679–1686.PubMedGoogle Scholar
  195. 194.
    Lee W, Haslinger A, Karin M et al. Activation of transcription by two factors that bind promoter and enhancer sequences of the human metallothionein gene and SV40. Nature 1987; 325: 368–372.PubMedGoogle Scholar
  196. 195.
    Pfahl M. Nuclear receptor/AP-1 interaction. Endocrine Reviews 1993; 14: 651–658.PubMedGoogle Scholar
  197. 196.
    Karin M, Richards RI. Human metallothionein genes–primary structure of the metallothionein-II gene and a related processed gene. Nature 1982; 299: 797–802.PubMedGoogle Scholar
  198. 197.
    Buchman AR, Burnett L, Berg P. The SV40 nucleotide sequence. In: Molecular biology of tumor viruses, part II. Tooze J, ed. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press 1980: 799–829.Google Scholar
  199. 198.
    Griffin BE, Soeda E, Barrell BG et al. Sequence and analysis of polyoma virus DNA. In: Molecular biology of tumor viruses, part II. Tooze J, ed. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press 1980: 831–896.Google Scholar
  200. 199.
    Zenke M, Grundstrom T, Matthes H et al. Multiple sequence motifs are involved in SV40 enhancer function. EMBO J 1986; 5: 387–397.PubMedGoogle Scholar
  201. 200.
    Fujita T, Shibuya H, Ohashi T et al. Regulation of human interleukin-2 gene: functional DNA sequences in the 5’ flanking region for the gene expression in activated T lymphocytes. Cell 1986; 46: 401–407.PubMedGoogle Scholar
  202. 201.
    Elder PK, Schmidt LJ, Ono T et al. Specific stimulation of actin transcription by epidermal growth factor and cycloheximide. Proc Natl Acad Sci USA 1984; 81: 7476–7480.PubMedGoogle Scholar
  203. 202.
    Muller R, Bravo R, Burckhardt J et al. Induction of c-fos gene and protein by growth factors precedes activation of c-myc. Nature 1984; 312: 716–720.PubMedGoogle Scholar
  204. 203.
    Cochran BH, Zullo J, Verma IM et al. Expression of the c-fos related gene and of a fos-related gene is stimulated by platelet-derived growth factor. Science 1984; 226: 1080–1082.PubMedGoogle Scholar
  205. 204.
    Lau LF, Nathan D. Identification of a set of genes expressed during the GO/G1 transition of cultured mouse cells. EMBO J 1985; 4: 3145–3151.PubMedGoogle Scholar
  206. 205.
    Imbra RJ, Karin M. Metallothionein gene expression is regulated by serum factors and activators of protein kinase C. Mol Cell Biol 1987; 7: 1358–1363.PubMedGoogle Scholar
  207. 206.
    Subramaniam M, Schmidt LJ, Crutchfield CEI et al. Negative regulation of serum-responsive enhancer elements. Nature 1989; 340: 64–66.PubMedGoogle Scholar
  208. 207.
    Herrera RE, Shaw PE, Nordheim A. Occupation of the c-fos serum response element in vivo my a multi protein complex is unaltered by grwoth factor induction. Nature 1989; 340: 68–70.PubMedGoogle Scholar
  209. 208.
    Mohun TJ, Garrett N, Treisman RH. Xenopus cytoskeletal actin and human c-fos gene promoters share a conserved protein binding site. EMBO J 1987; 6: 667–673.PubMedGoogle Scholar
  210. 209.
    van Delft S, Coffer P, Kruijer W et al. c-fos induction by stress can be mediated by the SRE. Biochem Biophys Res Comm 1993; 197: 542–548.PubMedGoogle Scholar
  211. 210.
    Bowman BH. Hepatic plasma proteins. Mechanisms of function and regulation. Academic Press Inc; 1993.Google Scholar
  212. 211.
    Kunz D, Zimmermann R, Heisig M et al. Identification of the promoter sequence involved in the interleukin-6 dependent expression of the rat a macroglobulin gene. Nucleic Acid Res 1989; 1121–1138.Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1995

Authors and Affiliations

  • Katarzyna M. Dziegielewska
    • 1
  • William M. Brown
    • 2
  1. 1.University of TasmaniaHobartAustralia
  2. 2.Law Firm: Sills, Cummis, Zuckerman, Radin, Tischman, Epstein and GrossNewarkUSA

Personalised recommendations