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© The Rockefeller University Press, 0021-9525/2000//779 $5.00
The Journal of Cell Biology, Volume 151, Number 4, , 2000 779-788

Differential Expression of Lumican and Fibromodulin Regulate Collagen Fibrillogenesis in Developing Mouse Tendons

^a Department of Pathology Anatomy and Cell Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107
^b Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205
^c Department of Cell and Molecular Biology, University of Lund, SE-22100 Lund, Sweden
^d Biostatistics Section, Division of Clinical Pharmacology, Department of Medicine, Thomas Jefferson University, Philadelphia, Pennsylvania 19107
Department of Pathology, Anatomy & Cell Biology, Jefferson Medical College, 1020 Locust Street, JAH543, Philadelphia, PA 19107.(215) 923-9618(215) 503-7855

Collagen fibrillogenesis is finely regulated during development of tissue-specific extracellular matrices. The role(s) of a leucine-rich repeat protein subfamily in the regulation of fibrillogenesis during tendon development were defined. Lumican-, fibromodulin-, and double-deficient mice demonstrated disruptions in fibrillogenesis. With development, the amount of lumican decreases to barely detectable levels while fibromodulin increases significantly, and these changing patterns may regulate this process. Electron microscopic analysis demonstrated structural abnormalities in the fibrils and alterations in the progression through different assembly steps. In lumican-deficient tendons, alterations were observed early and the mature tendon was nearly normal. Fibromodulin-deficient tendons were comparable with the lumican-null in early developmental periods and acquired a severe phenotype by maturation. The double-deficient mice had a phenotype that was additive early and comparable with the fibromodulin-deficient mice at maturation. Therefore, lumican and fibromodulin both influence initial assembly of intermediates and the entry into fibril growth, while fibromodulin facilitates the progression through growth steps leading to mature fibrils. The observed increased ratio of fibromodulin to lumican and a competition for the same binding site could mediate these transitions. These studies indicate that lumican and fibromodulin have different developmental stage and leucine-rich repeat protein specific functions in the regulation of fibrillogenesis.

Key Words: collagen • proteoglycans • lumican • fibromodulin • tendon

© 2000 The Rockefeller University Press

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