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© The Rockefeller University Press, 0021-9525/1997//729 $5.00
The Journal of Cell Biology, Volume 136, Number 3, , 1997 729-743


Article

Targeted Disruption of Decorin Leads to Abnormal Collagen Fibril Morphology and Skin Fragility



Keith G. Danielson*, Helene Baribault{ddagger}, David F. Holmes§, Helen Graham§, Karl E. Kadler§, and Renato V. Iozzo*,||

* Department of Pathology, Anatomy, and Cell Biology, Jefferson Medical College, Thomas Jefferson University, Philadelphia, Pennsylvania 19107; {ddagger} The Burnham Institute, La Jolla, California 92037; § Wellcome Trust Centre for Cell-Matrix Research, School of Biological Sciences, University of Manchester, Manchester M13 9PT, United Kingdom; and || Kimmel Cancer Center, Jefferson Medical College, Thomas Jefferson University, Philadelphia, Pennsylvania 19107

Decorin is a member of the expanding group of widely distributed small leucine-rich proteoglycans that are expected to play important functions in tissue assembly. We report that mice harboring a targeted disruption of the decorin gene are viable but have fragile skin with markedly reduced tensile strength. Ultrastructural analysis revealed abnormal collagen morphology in skin and tendon, with coarser and irregular fiber outlines. Quantitative scanning transmission EM of individual collagen fibrils showed abrupt increases and decreases in mass along their axes, thereby accounting for the irregular outlines and size variability observed in cross-sections. The data indicate uncontrolled lateral fusion of collagen fibrils in the decorindeficient mice and provide an explanation for the reduced tensile strength of the skin. These findings demonstrate a fundamental role for decorin in regulating collagen fiber formation in vivo.


Abbreviations used in this paper: EDS, Ehlers-Danlos syndrome; ES, embryonic stem; SLRP, small leucine-rich proteoglycan; STEM, scanning transmission EM.

K.G. Danielson and H. Baribault contributed equally to this work.



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