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J Cell Biol. 1998 Jun 1;141(5):1277-86.

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

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  • 1Department of Medicine and Genetics, Case Western Reserve University and University Hospitals of Cleveland, Cleveland, Ohio 44106-4952, USA. sxc76@po.cwru.edu

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.

PMID:
9606218
[PubMed - indexed for MEDLINE]
PMCID:
PMC2137175
Free PMC Article
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