Nutritional Copper Deficiency and Penicillamine Administration: Some Effects on Bone Collagen and Arterial Elastin Crosslinking

  • R. B. Rucker
  • JoAnn Murray
  • R. S. Riggins
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 86)


Nutritional copper deficiency effects marked changes in the crosslinking of collagen and elastin, presumably in relationship to copper’s role as a cofactor for lysyl oxidase. Lysyl oxidase controls one of the initial steps in the crosslinking of elastin and collagen, i.e., the conversion of peptidyl lysine or hydroxylysine residues to peptidyl α-aminoadipic-δ-semialdehyde derivatives. Once lysine-derived aldehydic functions in collagen and elastin are formed, crosslinks occur via aldol and Schiff-base type condensations. A decrease in the degree of crosslinking results in changes in the biomechanical properties of both collagen- and elastin-rich tissues. Some of these changes are described with respect to chick bone and aorta. Likewise, penicillamine blocks crosslinking reactions. In this case, however, it is probably because of the formation of thiazolidine complexes between penicillamine aldehydic functions. The administration of penicillamine at different levels to young growing chicks allows the isolation of fibrous insoluble elastin varying in aldehyde content.


Cellulose Formaldehyde Urea Mold Fluoride 
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Copyright information

© Springer Science+Business Media New York 1977

Authors and Affiliations

  • R. B. Rucker
    • 1
  • JoAnn Murray
    • 1
  • R. S. Riggins
    • 2
  1. 1.Departments of Nutrition, College of Agriculture and Environmental ScienceUniversity of CaliforniaDavisUSA
  2. 2.Orthopaedic Surgery, School of MedicineUniversity of CaliforniaDavisUSA

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