Molecular Perspectives of Vascular Wall Structure and Disease: The Elastic Component

In 1974 more than 50 percent of all deaths in the United States were caused by the major cardiovascular diseases [I]. Thus the ancient dictum that "a man is as old as his arteries" is even more applicable to longevity in our modern Western society. With past analytical developments utilized in biomedical research, the primary site within the vascular wall of two of the three major degenerative processes has been identified as the elastic fiber. This has led to an extension of the above statement. "It is true that we have the age of our arteries. This means more or less that we have the age of their elastic fibers" [2]. More recently, composite elements of the elastic fiber have been described in molecular detail [3, 4]. These molecular descriptions provide an understanding of the mechanism of pathological calcification of the elastic fiber [5] and of deleterious lipid deposition in this essential dynamic component of vascular wall [6]; they provide an understanding of the importance of temperature in the formation and repair of elastic fiber [7]; and they may provide a molecular rationale for relating elevated sodium chloride levels to elevated blood pressures [7]. The molecular perspectives derive from physicochemical methods and concepts applied in studying the structure and disease of vascular wall elastic fiber.

[1]  W R Gray,et al.  Isolation and amino acid sequences of tropoelastin peptides. , 1973, The Journal of biological chemistry.

[2]  R. Canfield,et al.  Amino-terminal sequence of a large non-polar peptide from elastin. , 1976, Biochemical and biophysical research communications.

[3]  L. Sandberg,et al.  Molecular Model for Elastin Structure and Function , 1973, Nature.

[4]  S. O. Andersen,et al.  New Molecular Model for the Long-range Elasticity of Elastin , 1970, Nature.

[5]  D. Urry,et al.  Cross-linked polypentapeptide of tropoelastin: an insoluble, serum calcifiable matrix. , 1976, Biochemistry.

[6]  D. Urry,et al.  Communication: Coacervation of tropoelastin results in fiber formation. , 1974, The Journal of biological chemistry.

[7]  D. Urry On the Molecular Basis for Vascular Calcification , 2015, Perspectives in biology and medicine.

[8]  G. Martin,et al.  CHEMICAL AND MORPHOLOGICAL STUDIES ON THE IN VITRO CALCIFICATION OF AORTA , 1963, The Journal of cell biology.

[9]  L B Sandberg,et al.  Isolation and characterization of cross-linked peptides from elastin. , 1974, The Journal of biological chemistry.

[10]  D. Urry,et al.  Synthetic, cross-linked polypentapeptide fo tropoelastin: an anisotropic, fibrillar elastomer. , 1976, Biochemistry.

[11]  J G Llaurado,et al.  Collagen and Elastin Content in Canine Arteries Selected from Functionally Different Vascular Beds , 1966, Circulation research.

[12]  D. Kramsch,et al.  The protein and lipid composition of arterial elastin and its relationship to lipid accumulation in the atherosclerotic plaque. , 1971, The Journal of clinical investigation.

[13]  M. Giro,et al.  The ultrastructural organization of elastin. , 1974, Journal of ultrastructure research.

[14]  G. Weissmann,et al.  X-RAY DIFFRACTION STUDIES OF HUMAN AORTIC ELASTIN RESIDUES. , 1960, The Journal of clinical investigation.

[15]  L. Sandberg,et al.  Structural features of tropoelastin related to the sites of cross-links in aortic elastin. , 1971, Biochemistry.

[16]  W. Hornebeck,et al.  Conformational changes in fibrous elastin due to calcium ions. , 1975, European journal of biochemistry.

[17]  M M Long,et al.  Proton and carbon magnetic resonance studies of the synthetic polypentapeptide of elastin. , 1975, Journal of molecular biology.