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Marfan’s Syndrome and Other Microfibrillar Diseases

  • Harry C. Dietz
  • Francesco Ramirez
  • Lynn Y. Sakai
Part of the Advances in Human Genetics book series (AHUG, volume 22)

Abstract

During the past twenty years, the molecular causes of several heritable disorders of connective tissue have been firmly established. These advances have been facilitated by the development of new means of experimental analysis, and by the identification of new extracellular matrix (ECM) components. Most of the progress has increased our understanding of collagenopathies and the contribution of the fibrillar collagens to the structural integrity of bone, cartilage, skin, ligaments and internal organs (Lee et al., 1991a). We have also discovered causal associations between mutations in nonflbrillar collagens and the clinical manifestations of epidermolysis bullosa, Alport’s syndrome, and the Schmid form of metaphyseal chondrodysplasia (Uitto and Christiano, 1992; Hudson et al., 1993; Jacenko et al., 1994).

Keywords

Elastic Fiber Marfan Syndrome Aortic Dilatation Intrachain Disulfide Bond Fibrillin Gene 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Aoyama, T., Tynan, K., Dietz, H.C., Francke, U., and Furthmayer, H., 1993, Missense mutations impair intracellular processing of fibrillin and microfibril assembly in Marfan syndrome, Hum. Mol. Genet. 2:2135–2140.PubMedCrossRefGoogle Scholar
  2. Baccarani-Contri, M., Vincenzi, D., Cicchetti, F, Mori, G., and Pasquali-Ronchetti, I., 1990, Immunocytochemical localization of proteoglycans within normal elastin fibers, Eur. J. Cell Biol. 53:305–312.PubMedGoogle Scholar
  3. Beals, R.K., and Hecht, F, 1971, Congenital contractural arachnodactyly; a heritable disorder of connective tissue, J. Bone Joint Surg. 53-A:887–903.Google Scholar
  4. Bentall, H.H., and DeBono, A.A., 1987, A technique for complete replacement of the ascending aorta, Thorax 23:338–339.CrossRefGoogle Scholar
  5. Beighton, P, De Paepe, A., Danks, D., Finidori, G., Gedde-Dahl, T., Goodman, R., Hall, J., Hollister, D.W., Horton, W., McKusick, V.A., Opitz, J.M., Pope, J.M., Pyeritz, R.E., Rimoin, D.L., Sillence, D., Spranger, J.W., Thompson, E., Tsipouras, P., Viljoen, D., Winship, I., and Young, I., 1986, International nosology of heritable disorders of connective tissue, Berlin 1986, Am. J. Med. Genet. 29:581–594.CrossRefGoogle Scholar
  6. Boileau, C., Jondeau, G., Babron, M.-C., Coulon, M., Alexandre, J.A., Sakai, L., Melki, J., Delorme, G., Dubourg, O., Bonaiti-Pellie, C., Bouradarias, J.P., and Junien, C., 1993, Autosomal dominant Marfan-like connective tissue disorder with aortic dilatation and skeletal anomalies not linked to the fibrillin genes, Am. J. Hum. Genet. 53:46–54.PubMedGoogle Scholar
  7. Breathnach, S.M., Melrose, S.M., Bhogal, B., deBeer, EC., Dyck, R.F., Black, M.M., Tennent, G., and Pepys, M.B., 1991, Amyloid P component is located on elastic fibre microfibrils in normal human tissue, Nature 293:652–654.CrossRefGoogle Scholar
  8. Bressan, G.M., Daga-Gordini, D., Colombatti, A., Castellani, I., Marigo, V., and Volpin, D., 1993, Emilin, a component of elastic fibers preferentially located at the elastic-microfibrils interface, J. Cell Biol. 121:201–212.PubMedCrossRefGoogle Scholar
  9. Bruns, R.R., Press, W., and Ross, J., 1987, A large-scale, orthogonal network of microfibril bundles in the corneal stroma, J. Invest. Dermatol. 28:1939–1946.Google Scholar
  10. Cheng, J., Fogel-Petrovic, M., and Maquat, L.E., 1990, Translation to near the distal end of the penultimate exon is required for normal levels of spliced triosephosphate isomerase mRNA, Mol. Cell. Biol. 10:5215–5225.PubMedGoogle Scholar
  11. Geary, E.G., and Gibson, M. A., 1983, Elastin-associated microfibrils and microfibrillar proteins, Int. Rev. Connect. Tissue Res. 10:197–209.Google Scholar
  12. Cooke, R.M., Wilkinson, A.J., Baron, M., Pastore, A., Tappin, M.J., Campbell, I.D., Gregory, H., and Sheard, B., 1987, The solution structure of human epidermal growth factor, Nature 327:339–341.PubMedCrossRefGoogle Scholar
  13. Corson, G.M., Chalberg, S.C., Dietz, H.C., Charbonneau, N.L., and Sakai, L.Y., 1993, Fibrillin binds calcium and is coded by cDNAs that reveal a multidomain structure and alternatively spliced exons at the 5′end, Genomics 17:476–484.PubMedCrossRefGoogle Scholar
  14. Cotta-Pereira, G., Guerra Rodrigo, F., and Bittencourt-Sampaio, S., 1976, Oxytalan, elaunin, and elastic fibers in the human skin, J. Invest. Dermatol. 66:143–148.PubMedCrossRefGoogle Scholar
  15. Dahlback, B., Hildebrant, B., and Linse, S., 1990, Novel type of very high affinity calcium-binding sites in β-hydroxyasparagine-containing epidermal growth factor-like domains in vitamin K-dependent protein S, Cell 18481–18489.Google Scholar
  16. Dahlback, K., Lofberg, H.H., Alumes, J., and Dahlback, B., 1989, Immunochistochemical demonstration of age-related deposition of vitronectin (S-protein of complement) and terminal complement complex on dermal elastic fibers, Invest. Dermatol. 93:727–733.CrossRefGoogle Scholar
  17. Dahlback, K., Ljungquist, A., Lafberg, H., Dahlback, B., Engvall, E., and Sakai, L.Y., 1990, Fibrillin immunoreactive fibers constitute a unique network in the human dermis: Immuno-histochemical comparison of the distribution of fibrillin, vitronectin, amyloid P component, and orcein stainable structures in normal skin and elastosis, J. Invest. Dermatol. 94:284–291.PubMedCrossRefGoogle Scholar
  18. Dietz, H.C., Cutting, G.R., Pyeritz, R.E., Maslen, C.L., Sakai, L.Y., Corson, G.M., Puffenberger, E.G., Hamosh, A., Nanthakumar, E.J., Curristin, S.M., Stetten, G., Meyers, DA., and Francomano, C.A., 1991, Marfan syndrome caused by a recurrent de novo missense mutation in the fibrillin gene, Nature 352:337–339.PubMedCrossRefGoogle Scholar
  19. Dietz, H.C., Pyeritz, R.E., Puffenberger, E.G., Kendzior, R.J., Corson, G.M., Maslen, C.J., Sakai, L.Y., Francomano, C.A., and Cutting, G.R., 1992, Marfan phenotype variability in a family segregating a missense mutation in the EGF-like motif of the fibrillin gene, J. Clin. Invest. 89:1674–1680.PubMedCrossRefGoogle Scholar
  20. Dietz, H.C., Mcintosh, I., Sakai, L.Y., Corson, G.M., Chalberg, S.C., Pyeritz, R.E., and Francomano, C.A., 1993a, Four novel FBN1 mutations: Significance for mutant transcript level and EGF-like domain calcium binding in the pathogenesis of Marfan syndrome, Genomics 17:468–475.PubMedCrossRefGoogle Scholar
  21. Dietz, H.C., Valle, D., Francomano, C.A., Kendzior, F.J., Pieritz, R.E., and Cutting, G.R., 1993b, The skipping of constitutive exons in vivo induced by nonsense mutations, Science 254:680–683.CrossRefGoogle Scholar
  22. Fehon, R.G., Kooh, P.J., Rebay, I., Regan, C.L., xu, T., Muskavich, M.A.T., and Artavanis-Tsakonas, S., 1990, Molecular interactions between the protein products of the neurogenic loci notch and delta, two EGF-homologus genes in Drosophila, Cell 61:523–534.PubMedCrossRefGoogle Scholar
  23. Gibson, M.A., Sandburg, L.B., Grosso, L.E., and Cleary, E.G., 1991, Complementary DNA cloning establishes microfibril-associated glycoprotein (MAGP) to be a discrete component of the elastin-associated microfibrils, J. Biol. Chem. 266:7596–7601.PubMedGoogle Scholar
  24. Godfrey, M., Vandemark, N., Wang, M., Velinov, M., Wargowski, D., Tsipouras, P., Haw, J., Becker, X, Robertson, W, Droste, S., and Rao, V.H., 1993, Prenatal diagnosis and a donor splice mutation in fibrillin in a family with Marfan syndrome, Am. J. Hum. Genet. 53:472–480.PubMedGoogle Scholar
  25. Gott, V.L., Pyeritz, R.E., Cameron, D.E., Green, P.S., and McKusick, V.A., 1991, Composite graft repair of Marfan aneurysm of the ascending aorta: results in 100 patients, Ann. Thorac. Surg. 52:38–45.PubMedCrossRefGoogle Scholar
  26. Greenlee, Jr., T.K., Ross, R., and Hartman, J.L., 1966, The fine structure of elastic fibers, J. Cell Biol. 30:59–71.PubMedCrossRefGoogle Scholar
  27. Handford, P.A., Baron, M., Mayhew, M., Willis, A., Beesley, T., Brownlee, G.G., and Campbell, I.D., 1990, The first EGF-like domain from human factor IX contains a high affinity calcium binding site, EMBO J. 9:475–480.PubMedGoogle Scholar
  28. Handford, P.A., Mayhew, M., Baron, M., Winship, RR., Campbell, I.D., and Brownlee, G.G., 1991, Key residues involved in calcium-binding motifs in EGF-like domains, Nature 351:164–167.PubMedCrossRefGoogle Scholar
  29. Herskowitz, I., 1993, Functional inactivation of genes by dominant negative mutations, Nature 329:219–222.CrossRefGoogle Scholar
  30. Hewett, D.R., Lynch, J.R., Smith, R., and Sykes, B., 1993, Fibrillin mutation in the Marfan syndrome may disrupt calcium binding of the epidermal growth factor module, Hum. Mol. Genet. 2:475–477.PubMedCrossRefGoogle Scholar
  31. Hollister, D.W., Godfrey, M., Sakai, L.Y., and Pyeritz, R.E., 1990, Marfan syndrome: immunohistologic abnormalities of the elastin-associated microfibrillar fiber system, N. Engl. J. Med. 323:152–159.PubMedCrossRefGoogle Scholar
  32. Horrigan, S.K., Rich, C.B., Streeten, B.W., Li, Z.Y., and Foster, J.A., 1992, Characterization of an associated microfibril protein through recombinant DNA techniques, J. Biol. Chem. 267:10087–10095.PubMedGoogle Scholar
  33. Hudson, B.G., Reeders, S.T., and Tryggvason, K., 1993, Type IV collagen: structure, gene organization, and role in human diseases, J. Biol. Chem. 268:26033–26036.PubMedGoogle Scholar
  34. Indik, A., Yah, H., Ornstein-Goldstein, N., Sheppard, P., Anderson, N., Rosenbloom, J.C., Peltonen, L., and Rosenbloom, J., 1987, Alternative splicing of human elastic mRNA indicated by sequence analysis of cloned genomic and complimentary DNA, Proc. Natl. Acad. Sci. USA 84:5680–5684.PubMedCrossRefGoogle Scholar
  35. Jacenko, O., Olsen, B.R., and Warman, M.L., 1994, Ofmice and men: heritable skeletal disorders, Am. J. Hum. Genet. 54:163–168.PubMedGoogle Scholar
  36. Kagan, H.M., Vaccaro, C.A., Bronxon, R.E., Tang, S.S., and Brody, J.S., 1986, Ultrastructural immunolocalization of lysyl oxidase in vascular connective tissue, J. Cell Bio. 103:1121–1128.CrossRefGoogle Scholar
  37. Kainulainen, K., Pulkkinen, L., Savolainen, A., Kaitila, I., and Peltonen, L., 1990, Location of chromosome 15 of the gene defect causing Marfan syndrome, N. Engl. J. Med. 323:935–939.PubMedCrossRefGoogle Scholar
  38. Kainulainen, K., Sakai, L.Y., Child, A., Pope, M.F., Puhakka, L., Ryhanen, L., Palotie, A., Kaitila, I., and Peltonen, L., 1992, Two unique mutations in Marfan syndrome resulting in truncated polypeptide chains of fibrillin, Proc. Natl. Acad. Sci. USA 88:5917–5921.CrossRefGoogle Scholar
  39. Kainulainen, K., Karttunen, L., Puhakka, L., Sakai, L.Y, and Peltonen, L., 1994, Mutations in the fibrillin gene responsible for dominant ectopia lentis and neonatal Marfan syndrome, Nature Genet. 6:64–69.PubMedCrossRefGoogle Scholar
  40. Kanzaki, T., Olofsson, A., Moren, A., Wernstedt, C., Hellman, U., Miyazono, K., Claesson-Welsh, L., and Heldin, C-H., 1990, TGF-β1 binding protein: a component of the large latent complex of TGF-β1 with multiple repeat sequences, Cell 61:1051–1061.PubMedCrossRefGoogle Scholar
  41. Keene, D.R., Maddox, K.B., Kuo, H.S., Sakai, L.Y, and Glanville, R.W., 1991, Extraction of extendable beaded structures and their identification as fibrillin-containing extracellular matrix microfibrils, J. Histochem. Cytochem. 39:441–449.PubMedCrossRefGoogle Scholar
  42. Kielty, C.M., and Shuttleworth, C.A., 1993, The role of calcium in the organization of fibrillin microfibrils, FEBS Lett. 336:323–326.PubMedCrossRefGoogle Scholar
  43. Kobayashi, R., Tashima, Y., Masuda, H., Shozawa, S., Numata, Y., Miyauchi, K., and Hayakawa, T., 1989, Isolation and characterization of a new 36-kDA microfibril-associated glycoprotein from porcine aorta, J. Biol. Chem. 264:17437–17444.PubMedGoogle Scholar
  44. Lee, B., D’Alessio, M., and Ramirez, F., 1991a, Modifications in the organization and expression of collagen genes associated with skeletal disorders, Crit. Rev. Euk. Gene. Exp. 1:173–187.Google Scholar
  45. Lee, B., Godfrey, M., Vitale, E., Hori, H., Mattei, M.G., Sarfarazi, M., Tsipouras, P., Ramirez, E, and Hollister, D.W., 1991b, Linkage of Marfan syndrome and a phenotypically related disorder to two fibrillin genes, Nature 352:330–334.PubMedCrossRefGoogle Scholar
  46. Maddox, B.K., Sakai, L.Y., Keene, D.R., and Glanville, R.W., 1989, Connective tissue microfibrils; isolation and characterization of three large pepsin-resistant domains of fibrillin, J. Biol. Chem. 264:21381–21385.PubMedGoogle Scholar
  47. Magid, D., Pyeritz, R.E., and Fishman, E.K., 1990, Musculoskeletal manifestations of the Marfan syndrome: radiologic features, Am. J. Roentgenol. 155:99–104.CrossRefGoogle Scholar
  48. Maslen, C.L., Corson, G.M., Maddox, B.K., Glanville, R.W., and Sakai, L.Y., 1991, Partial sequence of a candidate gene for the Marfan syndrome, Nature 352:334–337.PubMedCrossRefGoogle Scholar
  49. Maumenee, I.H., 1981, The eye in the Marfan syndrome, Trans. Am. Ophthal. Soc. 79:684–733.PubMedGoogle Scholar
  50. Mayhew, M., Handford, P.A., Baron, M., Tse, A.G.D., Campbell, I.D., and Brownlee, G.G., 1992, Ligand requirements for calcium binding to EGF-like domains, Prot. Engineering 15:489–494.CrossRefGoogle Scholar
  51. McGookey-Milewicz, D., Pyeritz, R.E., Crawford, E.S., and Byers, P.H., 1992, Marfan syndrome: defective synthesis, secretion and extracellular matrix formation of fibrillin by cultured dermal fibroblasts, J. Clin. Invest. 89:79–86.CrossRefGoogle Scholar
  52. Milewicz, D.M., and Duvic, M., 1994, Severe neonatal Marfan syndrome resulting from a de novo 3-bp insertion into the fibrillin gene on chromosome 15, Am. J. Hum. Genet. 54:447–453.PubMedGoogle Scholar
  53. Morse, R.P., Rockenmacher, S., Pyeritz, R.E., Sanders, S.P., Bieber, ER., Lin, A., MacLeod, P, Hall, B., and Graham, Jr., J.M., 1990, Diagnosis and management of infantile Marfan syndrome, Pediatrics 86:888–895.PubMedGoogle Scholar
  54. Murdoch, J.L., Walker, B.A., Halpern, B.I., Kuzma, J.W., and McKusick, V.A., 1972, Life expectancy and causes of death in the Marfan syndrome, N. Engl. J. Med. 286:804–808.PubMedCrossRefGoogle Scholar
  55. Pereira, L., D’Alessio, M., Ramirez, F., Lynch, J.R., Sykes, B., Pangilinan, T., and Bonadio, J., 1993, Genomic organization of the sequence coding for fibrillin, the defective gene product in Marfan syndrome, Hum. Mol. Genet. 2:961–968.PubMedCrossRefGoogle Scholar
  56. Pereira, L., Levran, O., Ramirez, F., Lynch, J.R., Sykes, B., Pyeritz, R.E., and Dietz, H.C., 1994, Diagnosis of Marfan syndrome: a molecular approach for stratification of cardiovascular risk within families, N. Engl. J. Med. (in press).Google Scholar
  57. Pyeritz, R.E., and McKusick, VA., 1979, The Marfan syndrome: diagnosis and management, N. Engl. J. Med. 300:772–777.PubMedCrossRefGoogle Scholar
  58. Ramirez, F., Pereira, L., Zhang, H., and Lee, B., 1993, The fibrillin-Marfan syndrome connection, BioEssays 15:589–594.PubMedCrossRefGoogle Scholar
  59. Raju, K., and Anwar, R.A., 1987, Primary structures of bovine elastin a,b, and c deduced from sequences of cDNA clones, J. Biol. Chem. 262:5755–5762.PubMedGoogle Scholar
  60. Raviola, G., 1971, The fine structure of the ciliary zonule and ciliary epithelium, J. Invest. Opthal. 10:851–869.Google Scholar
  61. Roberts, W.C., and Honig, H.S., 1982, The spectrum of cardiovascular disease in the Marfan syndrome: A clinico-morphologic study of 18 necropsy patients and comparison to 151 previously reported necropsy patients, Am. Heart J. 104:115–135.PubMedCrossRefGoogle Scholar
  62. Rosenbloom, J., Abrams, W.R., and Mecham, R., 1993, Extracellular matrix 4: the elastic fiber, EASEB J. 7:1208–1218.Google Scholar
  63. Ross, R., and Bornstein, P., 1966, The elastic fiber, J. Cell Biol. 40:336–381.Google Scholar
  64. Sakai, L.Y., 1990, Disulfide bonds crosslink molecules of fibrillin in the connective tissue space, in Elastin: Chemical and Biological Aspects (A. Tamburro and J.M. Davidson, eds.), pp. 213–227, Congedo Editore, Galatina, Italy.Google Scholar
  65. Sakai, L. Y., Keene, D.R., and Engvall, E., 1986, Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils, J. Cell Biol. 103:2499–2509.PubMedCrossRefGoogle Scholar
  66. Sakai, L.Y., Keene, D.R., Glanville, R.W., and Bachinger, H.P., 1991, Purification and partial characterization of fibrillin, a cysteine-rich structural component of connective tissue micro-fibrils, J. Biol. Chem. 266:14763–16770.PubMedGoogle Scholar
  67. Savage, Jr., R.C., Wilkinson, A.J., Baron, B., Pastore, A., Tappin, M.J., Campbell, I.D., Gregory, G., and Sheard, B., 1987, The solution structure of human epidermal growth factor, Nature 327:339–341.CrossRefGoogle Scholar
  68. Shores, J., Berger, K.R., Murphy, E.A., and Pyeritz, R.E., 1994, Progression of aortic dilatation and the benefit of long-term β-adrenergic blockade in the Marfan syndrome, N. Engl. J. Med. (in press).Google Scholar
  69. Tsipouras, P., Del Mastro, R., Sarfarazi, M., Lee, B., Vitale, E., Child, A., Godfrey, M., Devereux, R., Hewett, D., Steinmann, B., Viljoen, D., Sykes, B.C., Kilkpatrick, M., and Ramirez, F., 1992, Linkage of Marfan syndrome, dominant ectopia lentis and congenital contractural arachnodactyly to the fibrillin genes on chromosomes 15 and 5, N. Engl. J. Med. 326:905–909.PubMedCrossRefGoogle Scholar
  70. Tynan, K., Comeau, K., Pearson, M., Wilgenbus, P., Levitt, D., Gasner, C., Berg, M.A., Miller, DC, and Francke, U., 1993, Mutation screening of complete fibrillin-1 coding sequence: Report of five new mutations, including two in 8-cysteine domains, Hum. Mol. Genet. 2:1813–1821.PubMedCrossRefGoogle Scholar
  71. Uitto, J., and Christiano, A.M., 1992, Molecular genetics of the cutaneous basement membrane zone, J. Clin. Invest. 90:687–692.PubMedCrossRefGoogle Scholar
  72. Urlaub, G., Mitchell, P.J., Ciudad, C.J., and Chasin, L.A., 1989, Nonsense mutations in the dihydrofolate reductase gene affect RNA processing, Mol. Cell. Biol. 1989; 9:2868–2880.PubMedGoogle Scholar
  73. Wright, D.W., and Mayne, R., 1988, Vitreous humor of chicken contains two fibrillar systems: an analysis of their structure, J. Ultrastruct. Mol. Res. 100:234–244.Google Scholar
  74. Zhang, H., Apfelroth, S.D., Hu, W, Davis, E.C., Sanguineti, C., Bonadio, J., Mecham, R.P., and Ramirez, F., 1994, Structure and expression of fibrillin-2, a novel microfibrillar component preferentially located in elastic matrices, J. Cell Biol. 124:855–863.PubMedCrossRefGoogle Scholar
  75. Zimmermann, D.R., Dours-Zimmermann, M.T., Schubert, M., and Bruchner-Tuderman, L., 1994, Versican is expressed in the proliferating zone in the epidermis and in association with the elastic network of the dermis, J. Cell Biol. 124:817–825.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1994

Authors and Affiliations

  • Harry C. Dietz
    • 1
  • Francesco Ramirez
    • 2
  • Lynn Y. Sakai
    • 3
  1. 1.Departments of Pediatrics, Medicine, and Molecular Biology and GeneticsJohns Hopkins University School of MedicineBaltimoreUSA
  2. 2.Brookdale Center for Molecular BiologyMount Sinai School of MedicineNew YorkUSA
  3. 3.Shriners Hospital for Crippled Children and Department of Biochemistry and Molecular BiologyOregon Health Sciences UniversityPortlandUSA

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