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See detailGalectin-1 in Melanoma Biology and Related Neo-Angiogenesis Processes.
Mathieu, V.; de Lassalle, Elisabeth Martin; Toelen, J. et al

in Journal of Investigative Dermatology (2012)

Aggressiveness of advanced melanomas relates in part to their marked propensity to develop neoangiogenesis and metastases. Among its numerous pro-cancer roles, galectin (gal)-1 expressed and/or secreted ... [more ▼]

Aggressiveness of advanced melanomas relates in part to their marked propensity to develop neoangiogenesis and metastases. Among its numerous pro-cancer roles, galectin (gal)-1 expressed and/or secreted by both cancer and endothelial cells stimulates proliferation and angiogenesis. This study first shows that gal-1 is more highly expressed at both mRNA and protein levels than its congeners in melanomas and particularly in advanced lesions. The roles of gal-1 were further investigated in vivo in the highly proliferating and vascularized pseudometastatic B16F10 mouse melanoma model using stable knockdown B16F10 cells and wild-type versus gal-1 knockout mice, and then in vitro in B16F10 tumoral and lung microvascular cells. Gal-1 depletion in the B16F10 tumor cells but not in the tumor-bearing mice significantly increased melanoma-bearing mice survival. Tumor-derived gal-1 thus seems to have more critical roles than the host-derived one. In fact, gal-1 displays distinct effects on the H-Ras-dependent p53/p21 pathways: in primary lung microvessel endothelial cells, gal-1 seems to be involved in the maintenance of senescent status through the induction of both p53 and p21 while it stimulates B16F10 cancer cell proliferation through a p53/p21 decrease. Altogether, these data point to gal-1 as a potential target to combat melanomas.Journal of Investigative Dermatology advance online publication, 24 May 2012; doi:10.1038/jid.2012.142. [less ▲]

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See detailTranscriptional Profiling after Lipid Raft Disruption in Keratinocytes Identifies Critical Mediators of Atopic Dermatitis Pathways
Mathay, Conny; Pierre, Michael; Depiereux, Eric et al

in Journal of Investigative Dermatology (2011), 131

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See detailIsolation of a Microsporum canis gene family encoding three subtilisin-like proteases expressed in vivo
Descamps, Frédéric; Brouta, Frédéric; Monod, Michel et al

in Journal of Investigative Dermatology (2002), 119(4), 830-835

Microsporum canis is the main agent of dermatophytosis in dogs and cats and is responsible for frequent zoonosis. The pathogenesis of the disease remains largely unknown, however. Among potential fungal ... [more ▼]

Microsporum canis is the main agent of dermatophytosis in dogs and cats and is responsible for frequent zoonosis. The pathogenesis of the disease remains largely unknown, however. Among potential fungal virulence factors are secreted keratinolytic proteases, whose molecular characterization would be an important step towards the understanding of dermatophytic infection pathogenesis. M. canis secretes a 31.5 kDa keratinolytic subtilisin-like protease as the major component in a culture medium containing cat keratin as the sole nitrogen source. Using a probe corresponding to a gene's internal fragment, which was obtained by polymerase chain reaction, the entire gene encoding this protease named SUB3 was cloned from a M. canis lambdaEMBL3 genomic library. Two closely related genes, termed SUB1 and SUB2, were also cloned from the library using as a probe the gene coding for Aspergillus fumigatus 33 kDa alkaline protease (ALP). Deduced amino acid sequence analysis revealed that SUB1, SUB2, and SUB3 are secreted proteases and show large regions of identity between themselves and with subtilisin-like proteases of other filamentous fungi. Interestingly, mRNA of SUB1, SUB2, and SUBS were detected by reverse transcriptase nested-polymerase chain reaction from hair of experimentally infected guinea pigs. These results show that SUB1, SUB2, and SUB3 encode a family of subtilisin-like proteases and strongly suggest that these proteases are produced by M. canis during the invasion of keratinized structures. This is the first report describing the isolation of a gene family encoding potential virulence-related factors in dermatophytes. [less ▲]

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See detailTopically 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 ULg; Humbert, Philippe; Rougier, André et al

in Journal of Investigative Dermatology (2001), 116(6), 853-9

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 ... [more ▼]

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. [less ▲]

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See detailGranulomatous reactions following herpes-zoster contain varicella-zoster glycoprotein GPI
Nikkels, Arjen ULg; Sadzot-Delvaux, Catherine ULg; Cloes, Jean-Michel et al

in Journal of Investigative Dermatology (1992), 98(4), 522

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See detailFibroblasts Induce the Assembly of the Macromolecules of the Basement Membrane
Delvoye, Pierre ULg; Piérard, D.; Noël, Agnès ULg et al

in Journal of Investigative Dermatology (1988), 90(3), 276-82

The mechanism regulating the deposition of basement membrane components (BMCs) in a polymeric structure at the junction with the connective tissues is not yet understood. Cultures and cocultures of ... [more ▼]

The mechanism regulating the deposition of basement membrane components (BMCs) in a polymeric structure at the junction with the connective tissues is not yet understood. Cultures and cocultures of epithelial BMC-producing cells (L2 or PER cells) and fibroblasts were prepared in several experimental conditions and the organization of BMCs was studied by immunofluorescence. The pattern of BMCs in pure cultures of L2 or pulmonary epithelial rat (PER) cells consisted of intra- and extracellular granular deposits. At very high density, the cell contours were also underlined by a disrupted network of BMC deposits. A different fibrillar plexus--containing laminin, collagen type IV, and heparan-sulfate proteoglycan resistant to deoxycholate treatment and distant from the cell membrane--was observed in cocultures of L2 or PER cells with fibroblasts. Fibrils of fibronectin and/or collagen type I were most often dissociated from this plexus of BMCs. Similar results were obtained by adding a conditioned medium of L2 or PER cells to confluent fibroblasts, even when the cells were killed. Pure laminin also bound to the fibroblast layer. A coated film of fibronectin or polymeric collagen type I was unable to bind BMC provided by a conditioned medium. It is suggested that molecule(s) synthesized by fibroblasts and deposited in the pericellular matrix are involved in the assembly of BMCs. [less ▲]

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See detailInteractions between fibroblasts and a reconstituted basement membrane matrix
Emonard, H.; Calle, A.; Grimaud, J. A. et al

in Journal of Investigative Dermatology (1987), 89

A gel-like reconstituted basement membrane matrix containing type IV collagen, laminin, entactin, nidogen, and heparan sulfate proteoglycan was used to examine the interactions between normal calf skin ... [more ▼]

A gel-like reconstituted basement membrane matrix containing type IV collagen, laminin, entactin, nidogen, and heparan sulfate proteoglycan was used to examine the interactions between normal calf skin fibroblasts and basement membranes. Within 6 h after seeding, fibroblasts initiated a migration that resulted in the formation of a cellular network after 1 day of culture on top of the gel. Electron microscopy revealed that fibroblasts were able to remodel the basement membrane matrix by penetrating into the gel (from day 3), depositing fibronectin and collagen fibers, and retracting this extracellular matrix. Fibroblasts cultured on the Engelbreth-Holm-Swarm reconstituted basement membrane matrix displayed ultrastructural features characterized by a poor synthetic apparatus (rough endoplasmic reticulum and Golgi vesicles), a large cytoskeleton, and intracytoplasmic vesicles containing laminin. Thus the reconstituted basement membrane matrix is remodeled by skin fibroblasts, and reciprocally their ultrastructural morphologic features are affected by this matrix. [less ▲]

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See detailThe epidermal cell which selectively adheres to a collagen substrate is the basal cell.
Stanley, J. R.; Foidart, Jean-Michel ULg; Murray, J. C. et al

in Journal of Investigative Dermatology (1980), 74(1), 54-8

In order to determine whether a specific subpopulation of epidermal cells selectively attaches to collagen substrates in vitro, epidermal cell suspensions, obtained by trypsinization of guinea pig skin ... [more ▼]

In order to determine whether a specific subpopulation of epidermal cells selectively attaches to collagen substrates in vitro, epidermal cell suspensions, obtained by trypsinization of guinea pig skin, were incubated on type I or type IV collagen-coated glass cover slips. It was noted, morphologically and by electronic volume measurements, that small round cells, as opposed to the larger angulated flat cells, adhered to the collagen substrates. To further characterize the attached cells, the percentage of basal cells was determined in the attached cell population and in the initial epidermal cell suspension. Basal cells were identified by indirect immunofluorescence in 2 ways: (1) by the presence of pemphigoid antigen and (2) by the absence of upper cytoplasmic antigen, which is present in all keratinocytes except the basal cells. Whereas in the initial guinea pig epidermal cell suspensions about 50% of the cells were basal cells using either of these 2 criteria, 86-97% of the cells which adhered to the collagen substrates were basal cells. Human basal cells, as defined by pemphigoid antigen, also selectively adhered to the collagen substrates. [less ▲]

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See detailExpression of basement membrane zone antigens at the dermo-epibolic junction in organ cultures of human skin.
Hintner, H.; Fritsch, P. O.; Foidart, Jean-Michel ULg et al

in Journal of Investigative Dermatology (1980), 74(4), 200-4

Using the epithelial outgrowth in organ cultures of human skin ("epiboly") as a model system for basement membrane zone neogenesis, the emergence of various antigenic determinants of the junction zone ... [more ▼]

Using the epithelial outgrowth in organ cultures of human skin ("epiboly") as a model system for basement membrane zone neogenesis, the emergence of various antigenic determinants of the junction zone (bullous pemphigoid antigen, type IV collagen and laminin) was studied and the time sequence of their appearance assessed. All 3 antigens were found at the newly built dermo-epibolic junction; their synthesis, however, followed a distinct time sequence: bullous pemphigoid antigens emerged synchronously with the advancing tip of the migrating epithelium, whereas type IV collagen and to a greater extent, laminin, appeared with considerable delay. At the ultrastructural level, the formation of basal lamina accompanied the emergence of type IV collagen and laminin. [less ▲]

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See detailLocalization of the collagenous component in skin basement membrane.
Yaoita, H.; Foidart, Jean-Michel ULg; Katz, S. I.

in Journal of Investigative Dermatology (1978), 70(4), 191-3

Antibodies to type IV collagen were produced by immunizing rabbits with a basement membrane collagen obtained from a transplantable mouse tumor. Using specifically purified antibodies, type IV collagen ... [more ▼]

Antibodies to type IV collagen were produced by immunizing rabbits with a basement membrane collagen obtained from a transplantable mouse tumor. Using specifically purified antibodies, type IV collagen was localized ultrastructurally to the basal lamina part of the basement membrane zone [less ▲]

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