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Age-related differences in human skin proteoglycans.

David A Carrino1, Anthony Calabro, Aniq B Darr

  • 1Department of Biology, Skeletal Research Center, Case Western Reserve University, Cleveland, OH 44106, USA. dac5@case.edu

Glycobiology
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Summary

Human skin proteoglycans like versican and decorin change with age, particularly in their glycosaminoglycans (GAGs) and catabolic fragments. These shifts suggest age-related differences in proteoglycan metabolism impacting skin properties.

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Area of Science:

  • Biochemistry
  • Dermatology
  • Aging Research

Background:

  • Versican, decorin, and decorunt are abundant proteoglycans in human skin.
  • Four core protein species of versican are present from fetal to adult stages.
  • Versican V0 and V1 isoforms and their catabolic fragments are identified.

Purpose of the Study:

  • To investigate age-related differences in human skin proteoglycans (versican and decorin).
  • To analyze changes in proteoglycan core proteins, glycosaminoglycans (GAGs), and catabolic fragments with age.
  • To understand the implications of these changes on skin properties and injury response.

Main Methods:

  • Analysis of versican and decorin core proteins and GAGs in human skin across different age groups (fetal to adult).
  • Characterization of GAG size and sulfation patterns.
  • Identification and quantification of proteoglycan catabolic fragments.

Main Results:

  • Adult skin versican shows smaller GAGs and altered sulfation compared to fetal skin.
  • Adult skin decorin has smaller GAGs than fetal skin, with minimal sulfation changes.
  • Catabolic fragments of versican decrease with age, while decorin fragments increase in adult skin.

Conclusions:

  • Significant age-related differences exist in human skin proteoglycan composition and metabolism.
  • Changes in versican and decorin GAGs and catabolism may contribute to age-related alterations in skin properties and healing.
  • Proteoglycan catabolism shows distinct age-dependent patterns in human skin.