Altered x-ray diffraction pattern is accompanied by a change in the mode of cross-link formation in lipodermatosclerosis

Jürgen Brinckmann*, Yahya Açil, Michael Tronnier, Holger Notbohm, Boris Bätge, Wilfried Schmeller, Michel H.J. Koch, Peter K. Müller, Helmut H. Wolff

*Corresponding author for this work
17 Citations (Scopus)


We studied the molecular packing of collagen fibrils by x-ray diffraction in skin specimens of patients with lipodermatosclerosis and in controls. A difference in the tilt angles of the collagen molecules relative to the fiber axis is suggested by a D-stagger that is 1 nm larger in sclerotic skin than in normal skin. In parallel, the collagen cross-links in the skin specimens were analyzed, and a marked increase of both hydroxylysylpyridinoline and lysylpyridinoline, the trivalent mature cross-links characteristic of skeletal tissues, was found. The content of hydroxylysylpyridinoline and lysylpyridinoline was higher in the deep layer of the affected dermis than in the superficial dermis. This increase was always accompanied by an increase in the hydroxylysylpyridinoline/lysylpyridinoline ratio, suggesting that hydroxylysylpyridinoline is a sclerosis-associated cross-link. In addition, lysyl hydroxylation was increased in affected skin, and this increase was apparently restricted to the collagen telopeptides, which are crucial anchoring structures for lysyl dependent cross-links.

Original languageEnglish
JournalJournal of Investigative Dermatology
Issue number4
Pages (from-to)589-592
Number of pages4
Publication statusPublished - 01.01.1996

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)


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