The Experts below are selected from a list of 66543 Experts worldwide ranked by ideXlab platform
Steven M Albelda - One of the best experts on this subject based on the ideXlab platform.
-
regulation of Extracellular Matrix Proteins and integrin cell substratum adhesion receptors on epithelium during cutaneous human wound healing in vivo
American Journal of Pathology, 1993Co-Authors: Istvan Juhasz, George F Murphy, Horng Chin Yan, Meenhard Herlyn, Steven M AlbeldaAbstract:Although changes in Extracellular Matrix Proteins during wound healing have been well documented, little is known about the regulation of corresponding Extracellular Matrix adhesion receptors (integrins). To study this process in a human in vivo model, full thickness human skin grafts were transplanted onto severe combined immunodeficient mice and deep excisional wounds involving both the epidermal and dermal layers were then made. The changes in the expression of cell Matrix Proteins and epithelial integrins over time were analyzed with specific antibodies using immunohistochemistry. Wounding was associated with alterations in Extracellular Matrix Proteins, namely, loss of laminin and type IV collagen in the region of the wound and expression of tenascin and fibronectin. Changes were also noted in the integrins on the migrating keratinocytes. There was marked up-regulation of the alpha v subunit and de novo expression of the fibronectin receptor (alpha 5 beta 1) during the stage of active migration (days 1 to 3 after wounding). In the later stages of wound healing, after epithelial integrity had been established, redistribution of the alpha 2, alpha 3, alpha 6, and beta 4 collagen/laminin-binding integrin subunits to suprabasal epidermal layers was noted. Thus, during cutaneous wound healing, keratinocytes up-regulate fibronectin/fibrinogen-binding integrins and redistribute collagen/laminin-binding integrins. This study demonstrates that the human skin/severe combined immunodeficient chimera provides a useful model to study events during human wound repair.
M. Koch - One of the best experts on this subject based on the ideXlab platform.
-
Making recombinant Extracellular Matrix Proteins.
Methods, 2008Co-Authors: Florence Ruggiero, M. KochAbstract:A variety of approaches to understand Extracellular Matrix protein structure and function require production of recombinant Proteins. Moreover, the expression of heterologous Extracellular Matrix Proteins, in particular collagens, using the recombinant technology is of major interest to the biomedical industry. Although Extracellular Matrix Proteins are large, modular and often multimeric, most of them have been successfully produced in various expression systems. This review provides important factors, including the design of the construct, the cloning strategies, the expression vectors, the transfection method and the host cell systems, to consider in choosing a reliable and cost-effective way to make recombinant Extracellular Matrix Proteins. Advantages and drawbacks of each system have been appraised. Protocols that may ease efficient recombinant production of Extracellular Matrix are described. Emphasis is placed on the recombinant collagen production. Members of the collagen superfamily exhibit specific structural features and generally require complex post-translational modifications to retain full biological activity that make more arduous their recombinant production.A variety of approaches to understand Extracellular Matrix protein structure and function require production of recombinant Proteins. Moreover, the expression of heterologous Extracellular Matrix Proteins, in particular collagens, using the recombinant technology is of major interest to the biomedical industry. Although Extracellular Matrix Proteins are large, modular and often multimeric, most of them have been successfully produced in various expression systems. This review provides important factors, including the design of the construct, the cloning strategies, the expression vectors, the transfection method and the host cell systems, to consider in choosing a reliable and cost-effective way to make recombinant Extracellular Matrix Proteins. Advantages and drawbacks of each system have been appraised. Protocols that may ease efficient recombinant production of Extracellular Matrix are described. Emphasis is placed on the recombinant collagen production. Members of the collagen superfamily exhibit specific structural features and generally require complex post-translational modifications to retain full biological activity that make more arduous their recombinant production.
-
Making recombinant Extracellular Matrix Proteins.
Methods (San Diego Calif.), 2008Co-Authors: Florence Ruggiero, M. KochAbstract:A variety of approaches to understand Extracellular Matrix protein structure and function require production of recombinant Proteins. Moreover, the expression of heterologous Extracellular Matrix Proteins, in particular collagens, using the recombinant technology is of major interest to the biomedical industry. Although Extracellular Matrix Proteins are large, modular and often multimeric, most of them have been successfully produced in various expression systems. This review provides important factors, including the design of the construct, the cloning strategies, the expression vectors, the transfection method and the host cell systems, to consider in choosing a reliable and cost-effective way to make recombinant Extracellular Matrix Proteins. Advantages and drawbacks of each system have been appraised. Protocols that may ease efficient recombinant production of Extracellular Matrix are described. Emphasis is placed on the recombinant collagen production. Members of the collagen superfamily exhibit specific structural features and generally require complex post-translational modifications to retain full biological activity that make more arduous their recombinant production.
Joh M Whitelock - One of the best experts on this subject based on the ideXlab platform.
-
the modulation of platelet adhesion and activation by chitosan through plasma and Extracellular Matrix Proteins
Biomaterials, 2011Co-Authors: Mega S Lord, Ill Cheng, Simo J Mccarthy, Moonsu Jung, Joh M WhitelockAbstract:Abstract Chitosan has been shown to promote initial wound closure events to prevent blood loss. Platelet adhesion and activation are crucial early events in these processes after traumatic bleeding leading to thrombus formation. Platelet adhesion to chitosan was found to be enhanced in the presence of adsorbed plasma and Extracellular Matrix Proteins and was found to be primarily mediated by α IIb β 3 integrins, while α 2 β 1 integrins were found to be involved in platelet adhesion to collagen and perlecan. Platelets were found to be activated by chitosan, as shown by an increase in the expression of α IIb β 3 integrins and P-selectin, while the extent of activation was modulated by the presence of Proteins including perlecan and fibrinogen. Collagen-coated chitosan was found to activate platelets to the same extent as either chitosan or collagen alone. These data support the role of plasma and Extracellular Matrix Proteins in promoting chitosan mediated platelet adhesion and activation supporting the hypothesis that chitosan promotes wound healing via these interactions.
Jin Ho Chung - One of the best experts on this subject based on the ideXlab platform.
-
the effects of a novel synthetic retinoid seletinoid g on the expression of Extracellular Matrix Proteins in aged human skin in vivo
Clinica Chimica Acta, 2005Co-Authors: Misun Kim, Serah Lee, Ho Sik Rho, Duck Hee Kim, Ih Seop Chang, Jin Ho ChungAbstract:Abstract Background Although retinoids have potential efficacy in aged skin, their side effect (skin irritation) remains a clinical problem. We designed a novel synthetic retinoid, seletinoid G, by using computer-aided molecular modeling, and investigated its effects on the expression of Extracellular Matrix Proteins in human skin in vivo. Methods Twenty-three subjects were tested on the buttocks using 4-day occlusive application of seletinoid G and all- trans retinoic acid ( t RA). Skin irritation after topical application was quantified by the degree of erythema and cutaneous blood flow. The expression of Extracellular Matrix Proteins and interstitial collagenase (MMP-1) in skin biopsies was investigated by immunohistochemical staining and Western blotting. Results The topical application of seletinoid G under occlusion induced no skin irritation in contrast to t RA, which caused severe erythema. The topical treatment with seletinoid G increased the expressions of type I procollagen, tropoelastin, and fibrillin-1, and reduced MMP-1 in old skin in vivo. Seletinoid G was found to inhibit not only the UV-induced decrease of type I procollagen but the UV-induced increase of MMP-1 and c-Jun protein in young skin in vivo. Conclusions Seletinoid G is a novel synthetic retinoid, which has little the side effect of skin irritation after topical application. Seletinoid G can repair altered connective tissue in old skin and inhibit UV-induced collagen deficiency in young skin.
James P Nataro - One of the best experts on this subject based on the ideXlab platform.
-
the major pilin subunit of the aaf ii fimbriae from enteroaggregative escherichia coli mediates binding to Extracellular Matrix Proteins
Infection and Immunity, 2008Co-Authors: Mauricio J Farfan, Keith G Inman, James P NataroAbstract:Enteroaggregative Escherichia coli (EAEC) adherence to human intestinal tissue is mediated by aggregative adherence fimbriae (AAF); however, the receptors involved in EAEC adherence remain uncharacterized. Adhesion to Extracellular Matrix Proteins is commonly observed among enteric pathogens, so we addressed the hypothesis that EAEC may bind to Extracellular Matrix Proteins commonly found in the intestine. We found that EAEC prototype strain 042 adhered more abundantly to surfaces that were precoated with the Extracellular Matrix Proteins fibronectin, laminin, and type IV collagen. Differences in fibronectin binding of almost 2 orders of magnitude were observed between EAEC 042 and a mutant in the AAF/II major pilin gene, aafA. Purified AafA, refolded as a donor strand complementation construct, bound fibronectin in a dose-dependent manner. Addition of fibronectin to the apical surfaces of polarized T84 cell monolayers augmented EAEC 042 adherence, and this effect required expression of aafA. Finally, increased bacterial adherence was observed when apical secretion of fibronectin was induced by adenosine in polarized T84 cells. Binding to fibronectin may contribute to colonization of the gastrointestinal tract by EAEC.
-
The Major Pilin Subunit of the AAF/II Fimbriae from Enteroaggregative Escherichia coli Mediates Binding to Extracellular Matrix Proteins
Infection and immunity, 2008Co-Authors: Mauricio J Farfan, Keith G Inman, James P NataroAbstract:Enteroaggregative Escherichia coli (EAEC) adherence to human intestinal tissue is mediated by aggregative adherence fimbriae (AAF); however, the receptors involved in EAEC adherence remain uncharacterized. Adhesion to Extracellular Matrix Proteins is commonly observed among enteric pathogens, so we addressed the hypothesis that EAEC may bind to Extracellular Matrix Proteins commonly found in the intestine. We found that EAEC prototype strain 042 adhered more abundantly to surfaces that were precoated with the Extracellular Matrix Proteins fibronectin, laminin, and type IV collagen. Differences in fibronectin binding of almost 2 orders of magnitude were observed between EAEC 042 and a mutant in the AAF/II major pilin gene, aafA. Purified AafA, refolded as a donor strand complementation construct, bound fibronectin in a dose-dependent manner. Addition of fibronectin to the apical surfaces of polarized T84 cell monolayers augmented EAEC 042 adherence, and this effect required expression of aafA. Finally, increased bacterial adherence was observed when apical secretion of fibronectin was induced by adenosine in polarized T84 cells. Binding to fibronectin may contribute to colonization of the gastrointestinal tract by EAEC.
