Healing of Full-Thickness Cutaneous Wounds in the Pig. I. Immunohistochemical Study of Epidermo-Dermal Junction Regeneration

Rigal, Claudine; Pieraggi, M T; Vincent, Christian; Prost, Cathérine; Bouissou, H; Serre, Guy

doi:10.1111/1523-1747.ep12471745

Cited by 35 publications

(21 citation statements)

References 53 publications

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“…These factors could also explain the differences between our results and the findings of Rigal et al [15] concerning the time-dependent reappearance of collagen I V and collagen VII. These authors evaluated unsutured skin wounds in pigs from day 1 to day 20 after wounding and found that collagen V I I was detectable as early as the 3rd day after wounding.…”

Section: Discussioncontrasting

confidence: 98%

The time-dependent rearrangement of the epithelial basement membrane in human skin wounds —immunohistochemical localization of Collagen IV and VII

et al. 1992

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S u m m a r y . In 62 human skin wounds (surgical wounds, stab wounds and lacerations after surgical treatment) we analyzed the immunohistochemical localization of collagen IV in the epithelial basement membrane. In 27 of these wounds the distribution of collagen VII, which represents a specific component of the basement membrane of stratified epithelia, was also analyzed. We were able to demonstrate a virtually identical co-distribution of both collagen IV and VII in the wound area with no significant time-dependent differences in the appearance of both collagen types. Fragments of the epithelial basement membrane could be detected in the wound area from as early as 4 days after wounding and after 8 days a complete restitution of the epithelial basement membrane was observed, in all cases with a wound age of more than 21 days the basement membrane was completely reformed over the former lesional area. The period between 8 and 21 days after wounding was characterized by a wide variability ranging from complete restitution to deposition of basement membrane fragments or total lack of the epidermal basement membrane. K e y words: I m m u n o h i s t o c h e m i s t r y - Schliisselwiirter: I m m u n h i s t o c h e m i e -Kollagen IVKollagen VII -Basalmembran -Wundalter I n t r o d u c t i o nImmunohistochemistry is not only useful for the detection of early changes during wound repair [3], but also provides significant information on the time-dependent appearance of various extracellular matrix components during the proliferative and reparative phases of wound healing.In open skin wounds the closure of the wounded skin surface by reepithelialization starts from undamaged skin. Dividing basal cells of the epidermal layer proliferate to cover the lesional area. This migration is directed towards the wounded region [13]. Experimental studies have provided evidence that the migration of these epithelial cells is associated with the formation of a provisional matrix consisting of fibrin and fibronectin and that the basement membrane components laminin and collagen IV reappear when the fibrin and fibronectin in the wound area are organized [5].The epidermal basement membrane is composed not only of laminin and collagen IV, but also contains collagen VII which is specific for the basement membrane. This unique collagen molecule forms the anchoring fibrils. Collagen VII has been localized exclusively in the basement membrane of the epidermis and other basement membranes of stratified epithelia [20].The time-dependent rearrangement of the epithelial basement membrane component collagen IV in human

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Section: Discussioncontrasting

confidence: 98%

The time-dependent rearrangement of the epithelial basement membrane in human skin wounds —immunohistochemical localization of Collagen IV and VII

et al. 1992

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“…Our understanding of wound closure continues to be greatly enhanced using the synergistic combination of IHC techniques and microscopy to compare the localization of proteins in unwounded vs wounded skin. This technology has been applied with relative ease to tissue sections at the light microscopic level (Rigal et al 1991;Larjava et al 1993;Olerud et al 1998Olerud et al ,1999Usui et al 2005) but suffered from limited cellular resolution. Although the technological leap of TEM cannot be overstated in extending observations to the subcellular level, the synergy of structure and protein localization that flourished at the LM level proved difficult at the TEM level (Ortonne et al 1981), clearly requiring new techniques.…”

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confidence: 99%

Ultrastructural Localization of Integrin Subunits β4 and α3 Within the Migrating Epithelial Tongue of In Vivo Human Wounds

Underwood

Carter

Usui

et al. 2008

J Histochem Cytochem.

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Subsequent to wounding, keratinocytes must quickly restore barrier function. In vitro wound models have served to elucidate mechanisms of epithelial closure and key roles for integrins α6β4 and α3β1. To extrapolate in vitro data to in vivo human tissues, we used ultrathin cryomicrotomy to simultaneously observe tissue ultrastructure and immuno-gold localization in unwounded skin and acute human cutaneous wounds. Localization of the β4 integrin subunit in unwounded skin shows dominant hemidesmosomal association and minor basal keratinocyte lateral filopodic cell–cell expression. After wounding, β4 dominantly localized to cytokeratin-rich regions (trailing edge hemidesmosomes) and minor association with lamellipodia (leading edge). β4 colocalizes with α3 within filopodia juxtaposed to wound matrix, and increased concentrations of β4 were found in cytoplasmic vesicles within basal keratinocytes of the migrating tongue. α3 integrin subunit dominantly localized to filopodia within basal keratinocyte lateral cell–cell interfaces in unwounded skin and both cell–cell and cell–matrix filopodic interactions in wounded skin. This study indicates that β4 interacts with the extracellular environment through both stable and transient interactions and may be managed through a different endosomal trafficking pathway than α3. α3 integrin, despite its ability to respond to alternate ligands after wounding, does so through a single structure, the filopodia.

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“…The antibodies chosen for this study have been localized within the EDJ of human skin (36) did report that laminin, type IV collagen, and BP bound to the EDJ of normal skin of weanling Yorkshire pigs. Another study (33) found that porcine skin exhibited a high degree of cross-reactivity to murine laminin and to human type IV collagen and BP. The mapping of additional antibodies within the EDJ allows further characterization of normal porcine skin and the IPPSF.…”

Section: Discussionmentioning

confidence: 99%

“…Porcine skin is morphologically (17,19,20,26) and histochemically (16,33,42) similar to human skin and has been utilized as a model for the study of percutaneous absorption and toxicity ( 1,31 ). The IPPSF, an alternative in vitro model, is morphologically similar to human skin (22) and correlates well to in vivo (5,40) and human absorption (34) data.…”

Section: Introduction Sulfur Mustard (Bis [2-chloroethyl Sulfide] Hd)mentioning

confidence: 98%

Indirect Immunohistochemistry and Immunoelectron Microscopy Distribution of Eight Epidermal-Dermal Junction Epitopes in the Pig and in Isolated Perfused Skin Treated with Bis (2-Chloroethyl) Sulfide

Monteiro‐Riviere

Inman

1995

Toxicol Pathol

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Sulfur mustard (bis [2-chloroethyl] sulfide, HD) is a potent cutaneous vesicant that causes gross blisters by separation of the epidermal-dermal junction (EDJ). The EDJ of the skin is a highly specialized and complex structure composed of several components and plays a major role in the integrity of the skin. The isolated perfused porcine skin flap (IPPSF) was dosed with 0.2 mg/ml (n = 4), 5.0 mg/ml (n = 4), and 10.0 mg/ml (n = 5) HD or ethanol (n = 4) for 8 hr (dose-response study) and 10.0 mg/ml HD or ethanol for 1, 3, 5, and 8 hr (n = 4/treatment) (time-response study). Successful EDJ mapping was carried out in normal pig skin (NPS), ethanol-treated IPPSFs, and HD-treated IPPSFs using the following antibodies: laminin, type IV collagen, fibronectin, GB3 (Nicein), bullous pemphigoid (BP), and epidermolysis bullosa acquisita (EBA). Two mouse anti-human monoclonal antibodies, L3d and 19-DEJ-l (Uncein), did not cross-react with the EDJ of the pig. Antibody staining in NPS, ranging from very intense for laminin and type IV collagen to weak for fibronectin, was generally more discrete than in the IPPSF. No differences in staining were noted between the ethanol and nonblistered areas of the HD-treated IPPSFs. In HD-blistered areas, BP stained only the epidermal hemidesmosomes, and laminin, fibronectin, and GB3 stained primarily the dermis with fragments attached to the basal pole of the stratum basale cells, while type IV collagen and EBA stained only the dermis. Mapping of these epitopes determined that the precise plane of EDJ separation in the HD-treated skin occurred beneath the hemidesmosomes within the upper portion of the lamina lucida. The conservation of human epitopes in the EDJ of the pig further emphasizes the similarities between human skin and pig skin. Therefore, pig skin and the IPPSF may be used to study HD-induced vesication and blistering diseases.

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Healing of Full-Thickness Cutaneous Wounds in the Pig. I. Immunohistochemical Study of Epidermo-Dermal Junction Regeneration

Cited by 35 publications

References 53 publications

The time-dependent rearrangement of the epithelial basement membrane in human skin wounds —immunohistochemical localization of Collagen IV and VII

The time-dependent rearrangement of the epithelial basement membrane in human skin wounds —immunohistochemical localization of Collagen IV and VII

Ultrastructural Localization of Integrin Subunits β4 and α3 Within the Migrating Epithelial Tongue of In Vivo Human Wounds

Indirect Immunohistochemistry and Immunoelectron Microscopy Distribution of Eight Epidermal-Dermal Junction Epitopes in the Pig and in Isolated Perfused Skin Treated with Bis (2-Chloroethyl) Sulfide

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