Smoking affects collagen synthesis and extracellular matrix turnover in human skin.

Abstract

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.

• Authors: A Knuutinen, N Kokkonen, J Risteli, K Vähäkangas, M Kallioinen, T Salo, T Sorsa, A Oikarinen
• Journal: The British journal of dermatology (Br J Dermatol) Vol. 146 Issue 4 Pg. 588-94 (Apr 2002) ISSN: 0007-0963 [Print] England
• PMID: 11966688 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

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

Topics

• 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)