Article (Scientific journals)
Topically applied vitamin C enhances the mRNA level of collagens I and III, their processing enzymes and tissue inhibitor of matrix metalloproteinase 1 in the human dermis.
Nusgens, Betty; Humbert, Philippe; Rougier, André et al.
2001In Journal of Investigative Dermatology, 116 (6), p. 853-9
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Keywords :
Administration, Topical; Aging/metabolism; Ascorbic Acid/administration & dosage/pharmacology; Collagen/analysis/genetics/metabolism; Female; Humans; Metalloendopeptidases/genetics; Middle Aged; RNA, Messenger/analysis; Reverse Transcriptase Polymerase Chain Reaction; Skin/drug effects/metabolism; Tissue Inhibitor of Metalloproteinase-1/genetics
Abstract :
[en] Ascorbic acid (vitamin C) is a cofactor required for the function of several hydroxylases and monooxygenases. It is not synthesized in humans and some other animal species and has to be provided by diet or pharmacologic means. Its absence is responsible for scurvy, a condition related in its initial phases to a defective synthesis of collagen by the reduced function of prolylhydroxylase and production of collagen polypeptides lacking hydroxyproline, therefore, they are unable to assemble into stable triple-helical collagen molecules. In fibroblast cultures, vitamin C also stimulates collagen production by increasing the steady-state level of mRNA of collagen types I and III through enhanced transcription and prolonged half-life of the transcripts. The aim of the experimental work has been to evaluate the effect on dermal cells of a preparation of vitamin C topically applied on one side vs placebo on the other side of the dorsal face of the upper forearm of postmenopausal women. Biopsies were collected on both sides and the level of mRNA measured by non competitive reverse transcription-polymerase chain reaction made quantitative by the simultaneous transcription and amplification of synthetic RNA used as internal standards. The mRNA of collagen type I and type III were increased to a similar extent by vitamin C and that of three post-translational enzymes, the carboxy- and amino-procollagen proteinases and lysyloxidase similarly increased. The mRNA of decorin was also stimulated, but elastin, and fibrillin 1 and 2 were not modified by the vitamin. The expression of matrix metalloproteinases 1, 2, and 9 was not significantly changed, but an increased level of tissue inhibitor of matrix metalloproteinase 1 mRNA was observed without modification of tissue inhibitor of matrix metalloproteinase 2 mRNA. The stimulating activity of topical vitamin C was most conspicuous in the women with the lowest dietary intake of the vitamin and unrelated to the level of actinic damage. The results indicate that the functional activity of the dermal cells is not maximal in postmenopausal women and can be increased.
Disciplines :
Dermatology
Biochemistry, biophysics & molecular biology
Author, co-author :
Nusgens, Betty ;  Université de Liège - ULiège > Département des sciences biomédicales et précliniques > Département des sciences biomédicales et précliniques
Humbert, Philippe;  Université de Franche-Comté, Besançon, France > Dermatologie
Rougier, André;  La Roche Posay, Asnières France
Colige, Alain ;  Université de Liège - ULiège > Département des sciences biomédicales et précliniques > Laboratoire des tissus conjonctifs
Haftek, Marek;  Institut National de la Santé et de la Recherche Médicale - INSERM > U346/CNRS, Hôpital Herriot, Lyon, France
Lambert, Charles ;  Université de Liège - ULiège > Département des sciences biomédicales et précliniques > Laboratoire des tissus conjonctifs
Richard, Alain;  Laboratoire La Roche Posay > Asnières, France
Creidi, Pierre;  Université Franche-Comté, Besançon - France > Dermatologie
Lapière, Charles M.;  Université de Liège - ULiège
Language :
English
Title :
Topically applied vitamin C enhances the mRNA level of collagens I and III, their processing enzymes and tissue inhibitor of matrix metalloproteinase 1 in the human dermis.
Publication date :
2001
Journal title :
Journal of Investigative Dermatology
ISSN :
0022-202X
eISSN :
1523-1747
Publisher :
Nature Publishing Group, New York, United States - New York
Volume :
116
Issue :
6
Pages :
853-9
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 03 November 2009

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