116 161. Aldonyte R, Jansson L, Ljungberg O, Larsson S, Janciauskiene S. Polymerized alpha(1) antitrypsin is present on lung vascular endothelium. New insights int o the biological significance of alpha(1) antitrypsin polymerization. Histopathology 2004;45:587592. 162. Wang RL, McLaughlin T, Cossette T, Tang Q, Foust K, Campbell Thompson M, Martino A, et al. Recombinant AAV Serotype and Capsid Mutant Comparison for Pulmonary Gene Transfer of alpha1 Antitrypsin Using Invasive and Noninvasive Delivery. Molecular Therapy 2009;17:8187. 163. Carlson JA, Rogers BB, Sifers RN, Finegold MJ, Clift SM, DeMayo FJ, Bullock DW, et al. Accumulation of PiZ alpha 1antitrypsin causes liver damage in transgenic mice. J Clin Invest 1989;83:11831190. 164. Sifers RN, Rogers BB, Hawkins HK, Finegold MJ, Woo SL. Elevated synthesis of human alpha 1antitrypsin hinders the secretion of murine alpha 1antitrypsin from hepatocytes of transg enic mice. J Biol Chem 1989;264:1569615700. 165. Kang Y, Stein CS, Heth JA, Sinn PL, ...
QIU-LING, Li et al. Association of polymorphism of the alpha 1-antitrypsin gene with milk production traits in Chinese Holstein. S. Afr. j. anim. sci. [online]. 2010, vol.40, n.2. ISSN 2221-4062.. Protein degradation in bovine milk affects the quality of dairy products. Alpha 1-antitrypsin (AAT) can protect vulnerable elastic tissues from degradation by neutrophil elastase. The aim of this study was to assess the association of polymorphisms in bovine AAT gene with milk yield and milk composition in Chinese Holstein. Traits analyzed were fat percentage, protein percentage, 305-day milk yield and somatic cell score (SCS). Polymerase chain reaction-restriction fragment length polymorphism (PCR-RFLP), created restriction site-polymerase chain reaction (CRS-PCR) and allele specific-polymerase chain reaction (AS-PCR) methods were used to genotype five loci in coding regions of the sequence, including position 5504, 5609, 5624, 5747 and 8178 in Chinese Holstein. The five mutations were all silent ...
Alpha-1-antitrypsin or α1-antitrypsin (A1AT, A1A, or AAT) is a protein belonging to the serpin superfamily. It is encoded in humans by the SERPINA1 gene. A protease inhibitor, it is also known as alpha1-proteinase inhibitor (A1PI) or alpha1-antiproteinase (A1AP) because it inhibits various proteases (not just trypsin). In older biomedical literature it was sometimes called serum trypsin inhibitor (STI, dated terminology), because its capability as a trypsin inhibitor was a salient feature of its early study. As a type of enzyme inhibitor, it protects tissues from enzymes of inflammatory cells, especially neutrophil elastase, and has a reference range in blood of 0.9-2.3 g/L (in the US the reference range is expressed as mg/dL or micromoles), but the concentration can rise manyfold upon acute inflammation. When the blood contains inadequate amounts of A1AT or functionally defective A1AT (such as in alpha-1 antitrypsin deficiency), neutrophil elastase is excessively free to break down elastin, ...
TY - JOUR. T1 - Intrapleural administration of a serotype 5 adeno-associated virus coding for α1-antitrypsin mediates persistent, high lung and serum levels of α1-antitrypsin. AU - De, Bishnu. AU - Heguy, Adriana. AU - Leopold, Philip L.. AU - Wasif, Nabil. AU - Korst, Robert J.. AU - Hackett, Neil R.. AU - Crystal, Ronald. PY - 2004/12/1. Y1 - 2004/12/1. N2 - α1-Antitrypsin (α1AT) is a serine proteinase inhibitor that protects the lung from degradation by neutrophil proteases. In α1AT deficiency, an autosomal recessive disorder resulting from mutations in the α1AT (approved symbol SERPINA1) gene, serum α1AT levels of ,570 μg/ml are associated with development of emphysema. Adeno-associated virus (AAV) serotype 2 (AAV2) vectors expressing α1AT administered intramuscularly or intravenously mediate sustained serum levels of α1AT in experimental animals. Since the lung is only 2% of the body weight, AAV vector delivery to the muscle or liver is inefficient, as most of the α1AT does not ...
Black Swan Analysis Epiomic Epidemiology Series Forecast Report on Alpha-1 Anti-Trypsin in 9 Major Markets Alpha-1 Anti-Trypsin (AAT) is an enzyme belonging to the serpin super
Alpha-1 antitrypsin (AAT) is a protein that protects the lungs from damage caused by activated enzymes. Alpha-1 antitrypsin tests help diagnose alpha-1 antitrypsin deficiency.
In the present study, we evaluated the impact of the two most relevant AAT variants in two large and well-characterised cohorts of biopsy-proven NAFLD (both cohorts: n=1184) and chronic alcohol misuse (both cohorts: n=2462). We unambiguously found that the Pi*Z variant is a major risk factor for cirrhosis in the context of chronic metabolic injury such as NAFLD and chronic alcohol misuse. These findings are in line with previously published, smaller studies or studies pointing to an association with end-stage liver disease or cryptogenic cirrhosis in general.12 14 15 17 18 21 22 24 25 36 These findings provide a definitive answer and end the controversy about the clinical relevance of heterozygous carriage of the Pi*Z variant in NAFLD and ALD (online supplementary table 1). Moreover, this study is the first report that has systematically investigated the role of the Pi*S variant providing evidence that this variant does not pose a major risk to develop alcoholic or NAFLD-associated cirrhosis. ...
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Cosmid clones containing alpha 1-antitrypsin (alpha 1AT) gene sequences were observed to contain alpha 1AT-like sequences approximately 12 kb downstream of the authentic alpha 1AT gene. Restriction mapping suggested the alpha 1AT-like gene lacks promoter sequences. Cosmid clones from one library con …
Alpha1-antitrypsin molecule. Computer model showing the structure of alpha1-antitrypsin (blue-green) with its reactive loop (pink). This protein, also known as alpha-1 proteinase inhibitor, is a type of serine protease inhibitor (serpin) and is named after its ability to covalently bind and irreversibly inactivate serine proteases, including the digestive enzyme trypsin. It plays a key role in mediating inflammation and a deficiency results in the lung disease emphysema. - Stock Image C035/5538
A protease/anti-protease imbalance is a characteristic feature of inflammatory lung diseases such as cystic fibrosis (CF) and COPD. However, alpha-1-antitrypsin (AAT) enzyme replace- ment therapy (ERT) trials have not shown conclusive evidence of therapeutic benefit. Here, we assessed whether transduction of murine lungs with a pseudotyped SIV vector, rSIV.F/HN-hCEF-AAT, generates therapeutic levels of AAT. Mice were transduced with rSIV.F/HN-hCEF-AAT (1.4e8 TU/mouse) by nasal instillation and culled 10 days post-trans- duction. AAT levels in lung homogenate and epithelial lining fluid (ELF) were 3 logs above controls (p | 0.05), and hAAT concentration in ELF was 92-28lg/ml, similar to the thera- peutic AAT level in ELF of 70lg/ml. For comparison trans- fection of mouse lung with cationic lipid GL67A complexed to hCEFI-AAT only led to 0.4-0.1lg/ml AAT in ELF. A neutrophil elastase (NE) activity assay showed that the recombinant AAT successfully neutralised NE activity (p | 0.05). In a separate
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The AAT gene contains at least two enhancer elements , one at the 5 end of the gene and the other at the 3 end. The 5 enhancer is dominant under basal conditions and, following stimulation with IL-6 and related cytokines, both enhancers are essential and the 3 enhancer plays a major role.. Interferon γ and transforming growth factor β also modulate the hepatocyte response to IL-6. In addition to cytokines having an effect on AAT gene regulation, dexamethasone and oestrogen may have a stimulatory effect on gene regulation.. Monocyte AAT production appears to be primarily under the control of IL-6, although lipopolysaccharide , interleukin-1β (IL-1β) and tumour necrosis factor α (TNFα) all cause a 2±3-fold increase in AAT production by peripheral blood monocytes.. ...
The study was a Phase 1B/2A, uncontrolled, open-label, single-center study in individuals with congenital AAT (alpha 1-antitrypsin) deficiency. A baseline bronchoscopy with bronchoalveolar lavage (BAL) was performed 3 to a maximum of 4 weeks prior to the first administration of study drug. Fifteen eligible subjects were randomized to receive 1 of 3 dosing regimens of rAAT (100 mg daily, 100 mg twice daily, or 200 mg daily) administered via nebulization for 7 consecutive days. A post-treatment nadir BAL was obtained on study Day 8 (12 hours after last dose for subjects who receive drug therapy twice daily and 24 hours after the last dose for subjects who receive study product daily). BALs were conducted in the same lung lobe/segment. Follow-up visits took place on Day 15 and Day 36 ...
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This trial compared the tolerability and efficacy of three doses (40mg/kg, 60mg/kg and 80mg/kg) of alpha-1 antitrypsin [Glassia; Kamada] in paediatric and young
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Kamada announced the clinical plan for the initiation of a Phase 2/3 clinical trial in the United States of its Alpha-1 Antitrypsin (G1-AAT IV) for the treatment of acute Graft-Versus-Host Disease (GvHD), in collaboration with Shire plc.
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Health,New research shows a molecule that stops the growth of the AIDS virus in the blood may also inhibit the growth of other viruses.// Researchers say alpha-1 antitrypsin (AAT) -- a protein in the blood -- deactivates cells stopping viruses from multiplying. In order for cells to grow they must be in an active state. They say the concept is
Up-regulation of blood derived protein fragments in urine samples of the PREDICTIONS cohort.Displayed is the regulation of alpha-1-antitrypsin fragments, an alp
Representative macrographs (A, B) and light micrographs (C, D) of hearts from the diabetic rats. The diabetic rats kept under normoxia exhibited nearly normal m
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Research Corridor has published a new research study titled "Alpha 1-Antitrypsin Deficiency Treatment Market - Growth, Share, Opportunities, Competitive Analysis and Forecast, 2017 - 2025". The Alpha 1-Antitrypsin Deficiency Treatment Market report studies current as well as future aspects of the Alpha 1-Antitrypsin Deficiency Treatment Market based upon factors such as market dynamics, key ongoing trends and segmentation analysis. Apart from the above elements, the Alpha 1-Antitrypsin Deficiency Treatment Market research report provides a 360-degree view of the Lipstick Packing industry with geographic segmentation, statistical forecast and the competitive landscape.. Browse the complete report at http://www.researchcorridor.com/alpha-1-antitrypsin-deficiency-treatment-market/. Geographically, the Alpha 1-Antitrypsin Deficiency Treatment Market report comprises dedicated sections centering on the regional market revenue and trends. The Alpha 1-Antitrypsin Deficiency Treatment Market has been ...
Background Alpha-1 antitrypsin deficiency is an inherited disorder that can cause lung disease (chronic obstructive pulmonary disease or COPD, which is a chronic lung condition that prevents the air supply from getting to the lungs). It affects about 1 in 1600 to 1 in 5000 people. Patients with lung disease suffer from shortness of breath, reduced ability to exercise and wheezing. People who smoke are more seriously affected and have a greater risk of dying from the disease.. Study characteristics We reviewed the benefits and harms of treating patients who have the form of the disease that affects the lungs with alpha-1 antitrypsin extracted from blood donations. We found three randomised clinical trials (283 participants in the analyses) comparing treatment with alpha-1 antitrypsin with placebo (a pretend treatment) for two to three years. All participants were ex-smokers or had never smoked but had the genetic problem that carried a high risk of developing lung problems. The evidence is ...
TY - JOUR. T1 - α1-Antitrypsin Wbethesda. T2 - Molecular basis of an unusual α1-antitrypsin deficiency variant. AU - Holmes, M. D.. AU - Brantly, M. L.. AU - Fells, G. A.. AU - Crystal, Ronald. PY - 1990/8/16. Y1 - 1990/8/16. N2 - Molecular analysis of α1-antitrypsin (α1AT) Wbethesda revealed that it differs from the normal M1(A1a213) allele by a single base mutation causing an amino acid substitution A1a336GCT → Thr ACT. Evaluation of α1AT biosynthesis directed by the Wbethesda allele showed that although Wbethesda α1AT mRNA was translated normally invitro, transfection of the Wbethesda cDNA into COS-I cells was associated with human α1AT secretion of 50% that of cells transfected with a normal α1AT cDNA. The pattern of α1AT biosynthesis was not intracellular accumulation as observed with the common Z α1AT deficiency allele, but reduced intracellular α1AT, suggesting intracellular degradation of the newly synthesized Wbethesda molecule. Together these observations suggest that in ...