Copper, lysyl oxidase, and extracellular matrix protein cross-linking

Robert B. Rucker, Taru Kosonen, Michael S. Clegg, Alyson E. Mitchell, Brian R. Rucker, Janet Y. Uriu-Hare, Carl L Keen

Research output: Contribution to journalArticle

215 Citations (Scopus)

Abstract

Protein-lysine 6-oxidase (lysyl oxidase) is a cuproenzyme that is essential for stabilization of extracellular matrixes, specifically the enzymatic cross-linking of collagen and elastin. A hypothesis is proposed that links dietary copper levels to dynamic and proportional changes in lysyl oxidase activity in connective tissue. Although nutritional copper status does not influence the accumulation of lysyl oxidase as protein or lysyl oxidase steady state messenger RNA concentrations, the direct influence of dietary copper on the functional activity of lysyl oxidase is clear. The hypothesis is based on the possibility that copper efflux and lysyl oxidase secretion from cells may share a common pathway. The change in functional activity is most likely the result of posttranslational processing of lysyl oxidase. Copper is essential for organic cofactor formation in amine oxidases such as lysyl oxidase. Copper-containing amine oxidases have peptidyl 2,4,5 tri(oxo)phenylalanine (TOPA) at their active centers. TOPA is formed by copper-catalyzed oxidation of tyrosine, which takes place as part of Golgi or trans-Golgi processing. For lysyl oxidase, recent evidence (Science 1996;273:1078-84) indicates that as an additional step, a lysyl group at the active center of lysyl oxidase reacts with TOPA or its precursor to form lysyl tyrosylquinone.

Original languageEnglish (US)
JournalAmerican Journal of Clinical Nutrition
Volume67
Issue number5 SUPPL.
StatePublished - 1998

Fingerprint

Protein-Lysine 6-Oxidase
Extracellular Matrix Proteins
crosslinking
extracellular matrix
copper
phenylalanine
Copper
proteins
Phenylalanine
amine oxidase (copper-containing)
elastin
messenger RNA
amines
connective tissues
tyrosine
copper oxidase
collagen
lysine
Amine Oxidase (Copper-Containing)
secretion

Keywords

  • Collagen
  • Copper
  • Elastin
  • Extracellular matrix
  • Golgi complex
  • Lysyl oxidase
  • Protein cross-linking
  • Protein-lysine 6-oxidase

ASJC Scopus subject areas

  • Medicine (miscellaneous)
  • Food Science

Cite this

Rucker, R. B., Kosonen, T., Clegg, M. S., Mitchell, A. E., Rucker, B. R., Uriu-Hare, J. Y., & Keen, C. L. (1998). Copper, lysyl oxidase, and extracellular matrix protein cross-linking. American Journal of Clinical Nutrition, 67(5 SUPPL.).

Copper, lysyl oxidase, and extracellular matrix protein cross-linking. / Rucker, Robert B.; Kosonen, Taru; Clegg, Michael S.; Mitchell, Alyson E.; Rucker, Brian R.; Uriu-Hare, Janet Y.; Keen, Carl L.

In: American Journal of Clinical Nutrition, Vol. 67, No. 5 SUPPL., 1998.

Research output: Contribution to journalArticle

Rucker, RB, Kosonen, T, Clegg, MS, Mitchell, AE, Rucker, BR, Uriu-Hare, JY & Keen, CL 1998, 'Copper, lysyl oxidase, and extracellular matrix protein cross-linking', American Journal of Clinical Nutrition, vol. 67, no. 5 SUPPL..
Rucker RB, Kosonen T, Clegg MS, Mitchell AE, Rucker BR, Uriu-Hare JY et al. Copper, lysyl oxidase, and extracellular matrix protein cross-linking. American Journal of Clinical Nutrition. 1998;67(5 SUPPL.).
Rucker, Robert B. ; Kosonen, Taru ; Clegg, Michael S. ; Mitchell, Alyson E. ; Rucker, Brian R. ; Uriu-Hare, Janet Y. ; Keen, Carl L. / Copper, lysyl oxidase, and extracellular matrix protein cross-linking. In: American Journal of Clinical Nutrition. 1998 ; Vol. 67, No. 5 SUPPL.
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