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1.
New Microbiol ; 33(3): 253-6, 2010 Jul.
Article in English | MEDLINE | ID: mdl-20954444

ABSTRACT

This study evaluated the detection of Human Cytomegalovirus (HCMV)-DNA in donors' skin samples. HCMV-DNA was quantified in 100 skin specimens, including 50 fresh samples and as many corresponding glycerol-preserved specimens by a home-made Real Time PCR. HCMV-DNA was detected in 19/50 (38%) fresh specimens and 23/50 (46%) glycerol-preserved (p = n.s.). Nevertheless, the mere detection of HCMV-DNA does not imply the presence of infectious virions and therefore does not imply a risk of HCMV transmission, as treatment with glycerol is particularly efficacious in inactivating viral particles. Therefore, HCMV serology confirms its pivotal role in the setting of skin grafting.


Subject(s)
Cytomegalovirus Infections/virology , Cytomegalovirus/isolation & purification , Skin Transplantation , Skin/microbiology , Cytomegalovirus/genetics , Dermatologic Surgical Procedures , Humans , Organ Preservation , Tissue Donors
2.
Article in English | MEDLINE | ID: mdl-20936183

ABSTRACT

Autologous epidermal cell cultures (CEA) represent a possibility to treat extensive burn lesions, since they allow a significative surface expansion which cannot be achieved with other surgical techniques based on autologous grafting. Moreover currently available CEA preparations are difficult to handle and their take rate is unpredictable. This study aimed at producing and evaluating a new cutaneous biosubstitute made up of alloplastic acellular glycerolized dermis (AAGD) and CEA to overcome these difficulties. A procedure that maintained an intact basement membrane was developed, so as to promote adhesion and growth of CEA on AAGD. Keratinocytes were seeded onto AAGD and cultured up to 21 days. Viability tests and immunohistochemical analysis with specific markers were carried out at 7, 14, and 21 days, to evaluate keratinocyte adhesion, growth, and maturation. Our results support the hypothesis that this newly formed skin substitute could allow its permanent engraftment in clinical application.


Subject(s)
Biocompatible Materials , Keratinocytes , Materials Testing , Skin, Artificial , Basement Membrane/cytology , Basement Membrane/metabolism , Biocompatible Materials/chemistry , Biocompatible Materials/metabolism , Biocompatible Materials/pharmacology , Cell Adhesion/drug effects , Cell Culture Techniques , Cell Survival/drug effects , Cells, Cultured , Glycerol , Humans , Immunohistochemistry , Keratinocytes/cytology , Keratinocytes/drug effects , Keratinocytes/metabolism , Tissue Scaffolds/chemistry
3.
Exp Dermatol ; 16(7): 600-10, 2007 Jul.
Article in English | MEDLINE | ID: mdl-17576240

ABSTRACT

Hypertrophic scarring is a skin disorder characterized by persistent inflammation and fibrosis that may occur after wounding or thermal injury. Altered production of cytokines and growth factors, such as TGF-beta, play an important role in this process. Activin A, a member of the TGF-beta family, shares the same intra-cellular Smad signalling pathway with TGF-beta, but binds to its own specific transmembrane receptors and to follistatin, a secreted protein that inhibits activin by sequestration. Recent studies provide evidences of a novel role of activin A in inflammatory and repair processes. The aim of this study was to evaluate the importance of activin A and follistatin expression in the different phases of scar evolution. Immunostaining of sections obtained from active phase hypertrophic scars (AHS) revealed the presence of a high number of alpha-SMA(+) myofibroblasts and DC-SIGN(+) dendritic cells coexpressing activin A. Ex-vivo AHS fibroblasts produced more activin and less follistatin than normal skin or remission phase hypertrophic scar (HS) fibroblasts, both in basal conditions and upon TGF-betas stimulation. We demonstrate that fibroblasts do express activin receptors, and that this expression is not affected by TGF-betas. Treatment of HS fibroblasts with activin A induced Akt phosphorylation, promoted cell proliferation, and enhanced alpha-SMA and type I collagen expression. Follistatin reduced proliferation and suppressed activin-induced collagen expression. These results indicate that the activin/follistatin interplay has a role in HS formation and evolution. The impact of these observations on the understanding of wound healing and on the identification of new therapeutic targets is discussed.


Subject(s)
Activins/metabolism , Cicatrix, Hypertrophic/metabolism , Fibroblasts/metabolism , Follistatin/metabolism , Actins/metabolism , Activin Receptors/metabolism , Adolescent , Adult , Aged , Burns/complications , Burns/metabolism , Cell Proliferation , Cells, Cultured , Cicatrix, Hypertrophic/etiology , Cicatrix, Hypertrophic/pathology , Dendritic Cells/metabolism , Female , Fibroblasts/physiology , Humans , Immunoassay , Male , Middle Aged , Reverse Transcriptase Polymerase Chain Reaction , Skin/metabolism , Skin/pathology , Transforming Growth Factor beta1/metabolism , Wound Healing/physiology
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