Lumican regulates collagen fibril assembly: Skin fragility and corneal opacity in the absence of lumican

Shukti Chakravarti, Terry Magnuson, Jonathan H. Lass, Karl J. Jepsen, Christian LaMantia, Heidi Carroll

Research output: Contribution to journalArticlepeer-review

Abstract

Lumican, a prototypic leucine-rich proteoglycan with keratan sulfate side chains, is a major component of the cornea, dermal, and muscle connective tissues. Mice homozygous for a null mutation in lumican display skin laxity and fragility resembling certain types of Ehlers-Danlos syndrome. In addition, the mutant mice develop bilateral corneal opacification. The underlying connective tissue defect in the homozygous mutants is deregulated growth of collagen fibrils with a significant proportion of abnormally thick collagen fibrils in the skin and cornea as indicated by transmission electron microscopy. A highly organized and regularly spaced collagen fibril matrix typical of the normal cornea is also missing in these mutant mice. This study establishes a crucial role for lumican in the regulation of collagen assembly into fibrils in various connective tissues. Most importantly, these results provide a definitive link between a necessity for lumican in the development of a highly organized collagenous matrix and corneal transparency.

Original languageEnglish (US)
Pages (from-to)1277-1286
Number of pages10
JournalJournal of Cell Biology
Volume141
Issue number5
DOIs
StatePublished - Jun 1 1998
Externally publishedYes

ASJC Scopus subject areas

  • Cell Biology

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