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Structural change in decorin with skin aging.

Yoshihiro Nomura1

  • 1Department of Applied Protein Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology, Tokyo, Japan. ny318@cc.tuat.ac.jp

Connective Tissue Research
|November 23, 2006
PubMed
Summary

Decorin, a skin proteoglycan, regulates collagen assembly. Age-related changes in its glycosaminoglycan (GAG) chain length and structure may alter collagen matrix organization during aging.

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Area of Science:

  • Biochemistry
  • Dermatology
  • Extracellular Matrix Biology

Background:

  • Decorin is a key proteoglycan in skin, crucial for regulating collagen matrix assembly.
  • It consists of a core protein and a glycosaminoglycan (GAG) chain, influencing collagen fibril spacing.
  • The decorin GAG chain's length directly impacts the distance between collagen fibrils.

Purpose of the Study:

  • To investigate the role of decorin in collagen matrix assembly.
  • To examine age-related alterations in decorin structure, particularly its GAG chain.
  • To understand how these changes might affect collagen organization during aging.

Main Methods:

  • Analysis of decorin structure, focusing on core protein and GAG chain characteristics.
  • Assessment of decorin's distribution and interaction with collagen fibrils.
  • Comparison of decorin from aged and young skin samples.

Main Results:

  • Decorin's core protein (approximately 40kDa) remains unchanged with age.
  • Age-related modifications are observed in the decorin GAG chain's molecular size and sulfate positioning.
  • These structural GAG changes correlate with altered collagen matrix assembly.

Conclusions:

  • Age-specific structural changes in the decorin GAG chain, not the core protein, are identified.
  • These modifications in decorin's GAG chain are implicated in age-associated changes to the collagen matrix.
  • Decorin's GAG chain is a critical factor in maintaining skin structure and function throughout the aging process.

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