Targeted disruption of dermatopontin causes abnormal collagen fibrillogenesis

Ushio Takeda, Atsushi Utani, Jinghai Wu, Eijiro Adachi, Haruhiko Koseki, Masaru Taniguchi, Takeo Matsumoto, Toshiro Ohashi, Masaaki Sato, Hiroshi Shinkai

Research output: Contribution to journalArticlepeer-review

79 Citations (Scopus)


Gene targeting of a member of small leucine-rich repeat proteoglycans demonstrates that collagen fibrillogenesis is mediated by a set of extracellular matrix components, which interact with collagen. Collagen-associated protein dermatopontin knockout mice were generated in order to analyze the biologic involvement of dermatopontin in the formation of collagen fibrils. Although dermatopontin-null mice did not exhibit any obvious anatomical abnormality, skin elasticity was increased. Skin tensile tests revealed that the initial elastic modulus was 57% lower in dermatopontin-null mice than in wild-type mice, and that maximum tensile strength was similar. Remarkably, light microscopy study showed a significant decrease in the relative thickness of the dermis in dermatopontin-null mice compared with wild-type mice (45.2 ± 3.09% and 57.8 ± 4.25%, respectively). The skin collagen content was 40% lower in dermatopontin-null than in wild-type mice. Collagen fibrils in dermatopontin-null mice showed a great variety in diameter and irregular contours under the electron microscope. These data indicate that dermatopontin plays a critical role in elasticity of skin and collagen accumulation attributed to collagen fibrillogenesis in vivo.

Original languageEnglish
Pages (from-to)678-683
Number of pages6
JournalJournal of Investigative Dermatology
Issue number3
Publication statusPublished - 2002 Sep


  • Ehlers-Danlos Syndrome
  • Extracellular matrix
  • Knockout-out
  • Mice
  • Skin elasticity

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Dermatology
  • Cell Biology


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