Smoking affects collagen synthesis and extracellular matrix turnover in human skin

University of Helsinki, Helsinki, Uusimaa, Finland
British Journal of Dermatology (Impact Factor: 4.1). 05/2002; 146(4):588-94. DOI: 10.1046/j.1365-2133.2002.04694.x
Source: PubMed

ABSTRACT Smoking is associated with premature facial wrinkling and aberrant wound healing, but the underlying mechanisms of skin injury are poorly understood.
To compare the in vivo collagen synthesis and degradation in the skin of smokers and non-smokers.
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.
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.
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.

  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Introduction: Smoking has a negative impact on postoperative wound and tissue healing, presumably due to impaired wound healing. A detrimental effect on collagen metabolism seems to be involved, but the exact pathophysiological mechanisms remain unknown. Material and Methods: A formal computer-assisted search of Pubmed was performed together with a cross-reference search of eligible papers. A total of 46 papers were systematically reviewed. Results: Smoking affects collagen synthesis and deposition of mature collagen in the wound and increases collagen degradation. Attenuated fibroblast migration and proliferation in addition to enhanced neutrophil collagenase (MMP-8) release from inflammatory cells appear to be involved. Depressed tissue oxygenation and low vitamin C levels by smoking most probably interfere with the molecular pathways of collagen metabolism. Smoking cessation restores MMP-8 levels but does not reverse collagen synthesis or deposition. Conclusion: The impact of smoking on collagen metabolism is complex attenuating synthesis and enhancing degradation. Abstinence from smoking for 3 months decreases the release of proteases but does not restore collagen metabolism. Further studies are needed to clarify if the detrimental effect of smoking is reversible at all.
  • [Show abstract] [Hide abstract]
    ABSTRACT: Objectifs Le patient tabagique bénéficiant d’une intervention de chirurgie plastique est exposé à un risque majoré de complications péri- et postopératoires. Il nous semblait utile d’établir une mise au point sur le retentissement négatif, en particulier cicatriciel, du tabagisme et sur les bénéfices incontestables du sevrage. Nous souhaitons proposer un délai minimal de sevrage pré- et postopératoire en vue de réduire les risques et d’optimiser les résultats de l’intervention. Méthodes Une revue de la littérature a été réalisée sur la période 1972–2014 en interrogeant cinq bases de données (Medline, PubMed Central, Cochrane library, Pascal et Web of Science). Résultats La fumée de cigarette agit de manière diffuse et multifactorielle dans l’organisme. L’hypoxie et l’ischémie tissulaire ainsi que les désordres immunitaires induits par le tabac sont responsables de l’altération du processus cicatriciel. Une partie de ces effets est réversible au sevrage. Les données de la littérature conseillent un délai d’arrêt du tabagisme préopératoire situé entre 3 et 8 semaines et allant jusqu’à 4 semaines postopératoires. L’utilisation de traitements substitutifs nicotiniques double le taux d’abstinence à court terme. Le chirurgien doit s’aider d’un tabacologue en cas de dépendance importante de son patient. Conclusions Un sevrage tabagique total de 4 semaines préopératoires et jusqu’à la cicatrisation primaire du site opératoire, soit 2 semaines postopératoires, semble optimiser les conditions chirurgicales sans majorer le risque anesthésique. Un accompagnement du sevrage aussi bien humain que médicamenteux est recommandé.
    Annales de Chirurgie Plastique Esthétique 10/2014; 60(1). DOI:10.1016/j.anplas.2014.06.011 · 0.59 Impact Factor
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Breast cancer metastasis is the leading cause of cancer-related deaths in women worldwide. Collagen in the tumor microenvironment plays a crucial role in regulating tumor progression. We have shown that type III collagen (Col3), a component of tumor stroma, regulates myofibroblast differentiation and scar formation after cutaneous injury. During the course of these wound-healing studies, we noted that tumors developed at a higher frequency in Col3(+/-) mice compared to wild-type littermate controls. We, therefore, examined the effect of Col3 deficiency on tumor behavior, using the murine mammary carcinoma cell line 4T1. Notably, tumor volume and pulmonary metastatic burden after orthotopic injection of 4T1 cells were increased in Col3(+/-) mice compared to Col3(+/+) littermates. By using murine (4T1) and human (MDA-MB-231) breast cancer cells grown in Col3-poor and Col3-enriched microenvironments in vitro, we found that several major events of the metastatic process were suppressed by Col3, including adhesion, invasion, and migration. In addition, Col3 deficiency increased proliferation and decreased apoptosis of 4T1 cells both in vitro and in primary tumors in vivo. Mechanistically, Col3 suppresses the procarcinogenic microenvironment by regulating stromal organization, including density and alignment of fibrillar collagen and myofibroblasts. We propose that Col3 plays an important role in the tumor microenvironment by suppressing metastasis-promoting characteristics of the tumor-associated stroma. Copyright © 2015 American Society for Investigative Pathology. Published by Elsevier Inc. All rights reserved.
    American Journal Of Pathology 03/2015; DOI:10.1016/j.ajpath.2015.01.029 · 4.60 Impact Factor