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The delivery of alpha1-antitrypsin therapy through transdermal route: is this worse to explore?

ABSTRACT: The delivery of alpha1-antitrypsin therapy through transdermal route: is this worse to explore?

PROVIDER: PRJNA634130 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR11819888_1.fastq.gz	Fastqsanger.gz
	SRR11819888_2.fastq.gz	Fastqsanger.gz
	SRR11819889_1.fastq.gz	Fastqsanger.gz
	SRR11819889_2.fastq.gz	Fastqsanger.gz
	SRR11819890_1.fastq.gz	Fastqsanger.gz

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The delivery of alpha1-antitrypsin therapy through transdermal route: is this worse to explore?

Project description:Human α1-antitrypsin (AAT) is an abundant acute phase glycoprotein performing anti-protease, anti-apoptotic and immunomodulatory functions. Purified human plasma AAT used as a specific therapy for patients with lung emphysema and panniculitis due to inherited AAT deficiency, and it is beneficial in treating of other disorders. This therapy administered intravenously although other routes of administration are tested. Herein, we examined the transdermal application of native or recombinant AAT by using epiCS®, the 3D human epidermis equivalent reconstructed from human primary epidermal keratinocytes. Topically applied AAT protein (50µl, prepared in Hank`s balance solution, HBSS) freely diffused across epidermis layers in a concentration and time-dependent manner. We concluded that within 18 hours topically added 0.2 mg AAT well penetrates the stratum corneum and can be detected inside the cytosol of keratinocytes. Importantly, treatments with AAT did not induce obvious morphological changes in keratinocyte layers. Next, we supplemented culture medium with 100µg/ml of combined bacterial lipopolysaccharide (LPS) and peptidoglycan (PNG) mixture and incubated epiCS for 18h with or without the topical application of 0.2 mg AAT. Under these conditions, LPS/PNG triggered a strongly activation of epidermis model. Even though AAT exhibited a limited capacity to neutralize the effect of LPS/PNG, it lowered expression of IL-18 and IL-8, and preserved levels of filaggrin, an important protein for maintaining the epidermal barrier integrity. Our results suggest that the transdermal route for delivering AAT is worth exploration. If successful, this approach may offer easy-to-use therapy with AAT.

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Alpha1-Antitrypsin Deficiency Registry (AADR-BioLINCC)

Project description:Alpha1-Antitrypsin Deficiency Registry (AADR-BioLINCC)

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Alpha1-Antitrypsin Deficiency Registry (AADR-BioLINCC)

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Mice inflammatory responses to inhaled aerosolized LPS: effects of various forms of human alpha1-antitrypsin

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Curative and beta cell regenerative effects of alpha1 antitrypsin treatment in autoimmune diabetic NOD mice

Project description:In this study, we performed the gene expression analysis of the Normal, Diabetic and AAT treated NOD mice to elucidate the transcriptional changes induced by AAT. This will assist in identifying the biological processes / pathways involved in curative mechanism of AAT. Keywords: alpha1 antitrypsin treatment

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Expression data from transgenic mice (3 mo) inducibly expressing human alpha1-antitrypsin in the liver

Project description:In the classical form of α1antitrypsin deficiency a mutant protein accumulates in a polymerized form in the ER of liver cells causing liver damage and carcinogenesis by a gain-of-toxic function mechanism. Recent studies have indicated that the accumulation of mutant α1antitrypsin Z in the ER specifically activates the autophagic response but not the unfolded protein response and that autophagy plays a critical role in disposal of insoluble α1antitrypsin Z. In this study, we used genomic analysis of the liver in a novel transgenic mouse model with inducible expression to screen for changes in gene expression that would potentially define how the liver responds to accumulation of this mutant protein. Keywords: genomic analysis, alpha1-antitrypsin deficiency, comparative study, adult animals, inducible expression, liver specific

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Transcription profiling of mouse transgenics (3 mo) inducibly expresssing human alpha1-antitrypsin in the liver

Project description:In the classical form of Î±1antitrypsin deficiency a mutant protein accumulates in a polymerized form in the ER of liver cells causing liver damage and carcinogenesis by a gain-of-toxic function mechanism. Recent studies have indicated that the accumulation of mutant Î±1antitrypsin Z in the ER specifically activates the autophagic response but not the unfolded protein response and that autophagy plays a critical role in disposal of insoluble Î±1antitrypsin Z. In this study, we used genomic analysis of the liver in a novel transgenic mouse model with inducible expression to screen for changes in gene expression that would potentially define how the liver responds to accumulation of this mutant protein. Experiment Overall Design: Liver RNA from adult (3 mo old) male mice inducibly expressing human alpha1-antitrypsin wild type (M) or mutant (Z) form exclusively in the liver was subjected to genomic analysis. Groups: mutant AAT (Z), wild type AAT (M), expressing (4), non-expressing (1), wild type littermates (WT); 3 biological replicates/each group

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Transcription profiling of mouse (6 wk) inducibly expresssing human alpha1-antitrypsin in the liver

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2008-06-16 | E-GEOD-8600 | biostudies-arrayexpress

Mice inflammatory responses to inhaled aerosolized LPS: effects of various forms of human alpha1-antitrypsin

Project description:Mice inflammatory responses to inhaled aerosolized LPS: effects of various forms of human alpha1-antitrypsin

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