Smoking affects collagen synthesis and extracellular matrix turnover in human skin

Br J Dermatol. 2002 Apr;146(4):588-94. doi: 10.1046/j.1365-2133.2002.04694.x.


Background: Smoking is associated with premature facial wrinkling and aberrant wound healing, but the underlying mechanisms of skin injury are poorly understood.

Objectives: To compare the in vivo collagen synthesis and degradation in the skin of smokers and non-smokers.

Methods: The study population consisted of 47 current smokers and 51 individuals who had never smoked from northern Finland. Suction blisters were induced in the sun-protected upper inner arm of the study subjects, after which suction blister fluid (SBF) was collected for analyses of the levels of aminoterminal procollagen propeptides of type I and III collagens (PINP and PIIINP, respectively), matrix metalloproteinase (MMP)-8 and tissue inhibitor of MMP (TIMP)-1. PINP, PIIINP and TIMP-1 were also determined from serum samples. The levels of active and pro MMP-1 were assessed from deep-frozen skin biopsies by Western blotting.

Results: The synthesis rates of type I and III collagens were lower by 18% and 22%, respectively, in the SBF of the smokers compared with the non-smokers. The levels of MMP-8 were higher by 100% in the SBF of the smokers. The levels of MMP-1 in the skin biopsies did not differ significantly between the groups. The levels of TIMP-1 in SBF were 14% lower in the smokers than in the non-smokers, whereas the serum concentrations of TIMP-1 did not differ between the groups.

Conclusions: Smoking decreases the synthesis rates of type I and III collagens in skin in vivo and alters the balance of extracellular matrix turnover in skin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Age Factors
  • Aged
  • Biopsy
  • Collagen / biosynthesis*
  • Extracellular Matrix / metabolism*
  • Humans
  • Male
  • Matrix Metalloproteinase 8 / analysis
  • Middle Aged
  • Peptide Fragments / analysis
  • Procollagen / analysis
  • Skin / metabolism*
  • Smoking / metabolism*
  • Tissue Inhibitor of Metalloproteinase-1 / analysis


  • Peptide Fragments
  • Procollagen
  • Tissue Inhibitor of Metalloproteinase-1
  • procollagen Type I N-terminal peptide
  • procollagen Type III-N-terminal peptide
  • Collagen
  • Matrix Metalloproteinase 8