Lathyrism and the Biochemistry of Elastin

  • Judith Ann Foster
  • Celeste B. Rich
  • Rogers M. FredIII


Elastic recoil is of paramount importance in the structural integrity and function of large blood vessels and key connective tissue elements of pulmonary tissue. The elasticity of these tissues is due primarily to the presence of elastic fibers. These fibers can be shown both morphologically and chemically to be composed of at least two major proteins. One of the components, elastin, possesses an amorphous appearance in electron micrographs and has a unique amino acid composition consisting of approximately 95% nonpolar amino acids (Ross and Bornstein 1969; Partridge and David 1955). The other major component, the microfibril, displays a fibrillar structure in electron micrographs and possesses an amino acid composition characterized by a high content of polar amino acids and a significant amount of cysteine residues (Ross and Bornstein 1969). Although the microfibrillar component has not yet been chemically well defined, it is possible that this component may represent a single or a family of related glycoproteins (Serafini-Fracassini et al. 1975). The relationship between the two components of elastic fibers is not chemically well understood; however, ultrastructural studies have provided strong evidence that during development of the elastic fibers the microfibril appears !irst in the extracellular matrix. The insolubilized microfibril is thought to act as a framework upon which soluble elastin is aligned and subsequently insolubilized (Ross 1971).


Amino Acid Composition Elastic Fiber Aortic Tissue Lysyl Oxidase Nonpolar Amino Acid 
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.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Abraham PA, Smith DW, Carnes WH, (1974) Synthesis of soluble elastin by aortic medial cells in culture. Biochem Biophys Res Commun 58: 597–000PubMedCrossRefGoogle Scholar
  2. Bachhuber TE, Lalich JJ, Angevine DM, Schilling ED, Strong FM, (1955) Lathyrus factor activity of beta-aminopropionitrile and related compounds. Proc Soc Exp BioI Med 89: 294–294Google Scholar
  3. Burnett W, Rosenbloom J, (1979) Isolation and translation of elastin mRN A from chick aorta. Biochem Biophys Res Commun 86: 478–478PubMedCrossRefGoogle Scholar
  4. Foster JA, Bruenger E, Gray WR, Sandberg SB, (1972) Isolation and amino acid sequences of tropoelastin peptides. J BioI Chern 248: 2876–2876Google Scholar
  5. Foster JA, Gray WR, Franzblau C, (1973) Isolation and characterization of crosslinked peptides from elastin. Biochim Biophys Acta 303: 363–369PubMedGoogle Scholar
  6. Foster JA, Mecham RP, Franzblau C, (1976) A high molecular weight species of soluble elastin. Biochem Biophys Res Commun 72: 1399PubMedCrossRefGoogle Scholar
  7. Foster JA, Mecham RP, Rich CB, Cronin MF, Levine A, Imberman M, Salcedo LL, (1978) Proelastin. J BioI Chern 253: 2797Google Scholar
  8. Foster J A, Rich CB, Berglund N, Huber S, Mecham RP, Lange G, (1979) The anti-proteolytic behavior or lathyrogens. Biochim Biophys Acta 587: 477PubMedGoogle Scholar
  9. Foster JA, Rich CB, DeSa MD, Jackson AS, Fletcher S, , (1980a) Improved methodologies for the isolation and purification of tropoelastin. Anal Biochem (in press)Google Scholar
  10. Foster JA, Rich CB, DeSa MD, (1980b) Comparison of aortic and ear cartilage tropoelastins isolated from lathyritic pigs. Biochim Biophys Acta (in press)Google Scholar
  11. Foster J A, Rubin L, Kagan H, Franzblau CB, Luenger E, Sandberg LB, (1974) Isolation and characterization of elastin crosslinked peptides. J BioI Chern 249: 6191Google Scholar
  12. Foster JA, Shapiro R, Voynow P, Faris B, Crombie G, Franzblau C, (1975) Isolation of soluble elastin from lathyritic chicks. Comparison to tropoelastin from copper-deficient pigs. Biochemistry 14: 5343PubMedCrossRefGoogle Scholar
  13. Franzblau C, Faris B, Papaioannoy R, (1969) Lysinonorleucine. A new amino acid from hydrolysates of elastin. Biochemistry 8: 2833-2837PubMedCrossRefGoogle Scholar
  14. Franzblau C, Lent RW, (1969) Studies on the chemistry of elastin structure, function and evolution in proteins. Brookhaven Sympos BioI 21: 358–377Google Scholar
  15. Franzblau C, Sinex FM, Faris B, Lampidis R, (1965) Identification of a new crosslinking amino acid in elastin. Biochem Biophys Res Commun 21: 575-581PubMedCrossRefGoogle Scholar
  16. Geiger BJ, Steenback H, Persons H, (1933) Lathyrism in the rat. J Nutr 6: 427Google Scholar
  17. Gerber GE, Anwar RA, (1975) Comparative studies of the crosslinked regions of elastin from bovine ligamentum nuchae and bovine, porcine and human aorta. Biochem J 149: 685–695PubMedGoogle Scholar
  18. Gray WR, Sandberg SB, Foster JA, (1973) Molecular model for elastin structure and function. Nature 246: 461PubMedCrossRefGoogle Scholar
  19. Hall DA, (1970) Coordinately bound calcium as a crosslinking agent in elastin and as an activator of elastolysis. Gerontologia 16: 326CrossRefGoogle Scholar
  20. Hall DA, Reed R, Tunbridge RE, (1952) Structure of elastic tissue. Nature 170: 264PubMedCrossRefGoogle Scholar
  21. Harris ED, Gonnerman WA, Savage JE, O’Dell BL, (1974) Amine oxidases in aorta. II Purification and partial characterization of lysyl oxidase in chick aorta. Biochim Biophys Acta 341: 322–344Google Scholar
  22. John R, Thomas J, (1972) Chemical compositions of elastins isolated from aortas and pulmonary tissues of humans of different ages. Biochem J 127: 261PubMedGoogle Scholar
  23. Kadar A, (1979) The elastic fiber. Normal and pathological conditions in the arteries. In: Experimental Pathology Suppl 5.Google Scholar
  24. Foster J. A.,et al., Kagan HM, Crombie GD, Jordan RE, Lewis W, Franzblau C, (1972) Proteolysis of elastin-ligand complexes. Stimulation of elastase digestion of insoluble elastin by sodium dodecyl sulfate. Biochemistry 11: 3412Google Scholar
  25. Kramsch DM, Franzblau C, Hollander W, (1971) The protein and lipid composition of arterial elastin and its relationship to lipid accumulation in the atherosclerotic plaque. J Clin Invest 50: 1666PubMedCrossRefGoogle Scholar
  26. Kramsch DM, Franzblau C, Hollander W, (1974) Components of the protein-lipid complex of arterial elastin: their role in the retention of lipid in atherosclerotic lesions. Adv Exp Med BioI 43: 193Google Scholar
  27. Lansing AI, Rosenthal TB, Alex M, Dempsey EW, (1952) The structure and chemical characterization of elastic fibers as revealed by elastase and by electron microscopy. Anat Rec 114: 555–575PubMedCrossRefGoogle Scholar
  28. Lent RW, Smith B, Salcedo LL, Faris B, Franzblau C, (1969) Studies on the reduction of elastin. II Evidence for the presence of α-aminoadipic acid δ-semialdehyde and its aldol condensation product. Biochemistry 8: 2837–2845PubMedCrossRefGoogle Scholar
  29. Miller EJ, Fullmer HM, (1966) Elastin: diminished reactivity with aldehyde reagents in copper deficiency and lathyrism. J Exp Med 123: 1097–1106PubMedCrossRefGoogle Scholar
  30. Miller EJ, Martin GR, Piez KA, (1964) The utilization of lysine in the biosynthesis of elastin cross-links. Biochem Biophys Res Commun 17: 248–253PubMedCrossRefGoogle Scholar
  31. Murphy S, Harsch M, Mori T, Rosenbloom J, (1972) Identification of a soluble intermediate during synthesis of elastin by embryonic chick aortae. FEBS Lett 21: 113PubMedCrossRefGoogle Scholar
  32. Narayanan AS, Sandberg SB, Ross R, Layman DL, (1976) The smooth muscle cell. Elastin synthesis in arterial smooth muscle cell culture. J Cell BioI 68: 411CrossRefGoogle Scholar
  33. Narayanan AS, Siegel RC, Martin GR, (1972) On the inhibition of lysyl oxidase by B-aminopropionitrile. Biochem Biophys Res Commun 46: 745PubMedCrossRefGoogle Scholar
  34. Partridge SM, (1962) Elastin. Advanc Protein Chern 17: 227–302CrossRefGoogle Scholar
  35. Partridge SM, David HF, Adair GS, (1955) The chemistry of connective tissues. Two soluble proteins derived from partial hydrolysis of elastin. Biochem J 61: 21PubMedGoogle Scholar
  36. Partridge SM, Elsden DF, Thomas J, (1963) Constitution of the cross-linkages in elastin. Nature 197: 1297–1298.PubMedCrossRefGoogle Scholar
  37. Partridge SM, Elsden DF, Thomas J, Dorfman A, Telser A, Ho PL, (1966) Incorporation of labelled lysine into the desmosine cross-bridges in elastin. Nature 209: 399–400PubMedCrossRefGoogle Scholar
  38. Partridge SM, Keeley FM, (1974) Age related and atherosclerotic changes in aortic elastin. Adv Exp Med BioI 43: 173Google Scholar
  39. Pinnell SR, Martin GR, (1968) The crosslinking of collagen and elastin: enzymatic conversion of lysine in peptide linkage to a-aminoadipic-8-semialdehyde. Proc Natl Acad Sci 61: 708PubMedCrossRefGoogle Scholar
  40. Rosenbloom J, Cywinski A, (1976) Biosynthesis and secretion of tropoelastin by chick aorta cells. Biochem Biophys Res Commun 69: 613PubMedCrossRefGoogle Scholar
  41. Ross R, (1971) The smooth muscle cell. II Growth of smooth muscle in culture and formation of elastic fibers. J Cell BioI 50: 172–186CrossRefGoogle Scholar
  42. Ross R, Bornstein P, (1969) The elastic fiber. I The separation and partial characterization of its macromolecular components. J Cell BioI 40: 366–381CrossRefGoogle Scholar
  43. Rucker RB, Murray J, Lefevre M, Lee J, (1977) Putative forms of soluble elastin and their relationship to the synthesis of fibrous elastin. Biochem Biophys Res Commun 75: 358PubMedCrossRefGoogle Scholar
  44. Rucker RB, Tom K, Tanaka M, Haniu M, Yasunobu KT, (1975) Chick tropoelastin isolation and partial chemical characterization. Biochem Biophys Res Commun 66: 287PubMedCrossRefGoogle Scholar
  45. Ryhanen L, Graves PN, Bressan GM, Prockop DJ, (1978) Synthesis of an elastin component of molecular weight about 70,000 by polysomes from chick embryo aortas. Arch Biochem Biophys 185: 344PubMedCrossRefGoogle Scholar
  46. Foster J. A. et a1, Saboria JL, Segura M, Flores M, Garcia R, Palmer E, (1979) Differential expression of gizzard actin genes during chick embryogenesis. J BioI Chern 254: 1119Google Scholar
  47. Sandberg LB, Weissman N, Gray WR, (1971) Structural features of tropoelastin related to the sites of crosslinks in aortic elastin. Biochemistry 10: 52PubMedCrossRefGoogle Scholar
  48. Sandberg LB, Weissman N, Smith DW, (1969) The purification and partial characterization of a soluble elastin-like protein from copper-deficient porcine aorta. Biochemistry 8: 2940PubMedCrossRefGoogle Scholar
  49. Serafini-Fracassini A, Field JM, Armitt C, (1975) Characterization of the microfibrillar component of bovine ligamentum nuchae. Biochem Biophys Res Commun 65: 1146–1152PubMedCrossRefGoogle Scholar
  50. Shibahara S, Davidson J, Smith K, Boyd C, Tolstoshev P, Crystal R, (1980) Modulation of elastin mRN A levels in developing sheep lung and nuchal ligament. Fed Proc 36: 989Google Scholar
  51. Siegel RC, Pinnell SR, Martin GR, (1970) Crosslinking of collagen and elastin. Properties of lysyl oxidase. Biochemistry 9: 4486PubMedCrossRefGoogle Scholar
  52. Sykes BC, Partridge SM, (1974) Salt-soluble elastin from lathyritic chicks. Biochem J 141: 567Google Scholar
  53. Tanzer ML, Housley T, Berube L, Fairweather R, Franzblau C, Gallop PM, (1973) Structure of two histidine-containing crosslinks from collagen. J BioI Chern 248: 393Google Scholar
  54. Thomas J, Elsden DF, Partridge SM, (1963) Degradation products from elastin. Nature 200: 651–652PubMedCrossRefGoogle Scholar
  55. Uitto J, Hoffmann H, Prockop DJ, (1976) Synthesis of elastin and procollagen by cells from embryonic aorta. Arch Biochem Biophys 173: 187PubMedCrossRefGoogle Scholar
  56. Urry DW, (1974) Arterial mesenchyma and arteriosclerosis interaction of elastin. Adv Exp Med BioI 43: 211Google Scholar

Copyright information

© Springer-Verlag New York, Inc. 1981

Authors and Affiliations

  • Judith Ann Foster
  • Celeste B. Rich
  • Rogers M. FredIII

There are no affiliations available

Personalised recommendations