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| Ortiz,Gustavo; Salica,Juan P; Chuluyan,Eduardo H; Gallo,Juan E. |
| Diabetic retinopathy is one of the most important causes of blindness. The underlying mechanisms of this disease include inflammatory changes and remodeling processes of the extracellular-matrix (ECM) leading to pericyte and vascular endothelial cell damage that affects the retinal circulation. In turn, this causes hypoxia leading to release of vascular endothelial growth factor (VEGF) to induce the angiogenesis process. Alpha-1 antitrypsin (AAT) is the most important circulating inhibitor of serine proteases (SERPIN). Its targets include elastase, plasmin, thrombin, trypsin, chymotrypsin, proteinase 3 (PR-3) and plasminogen activator (PAI). AAT modulates the effect of protease-activated receptors (PARs) during inflammatory responses. Plasma levels of AAT... |
| Tipo: Journal article |
Palavras-chave: Diabetic retinopathy; Alpha-1-antitrypsin; Diabetes; Endogenous anti-inflammatory agents; Retinal inflammation; NF-kB. |
| Ano: 2014 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602014000100052 |
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| Silva,Aline Correa da; Brass,Karin Erica; Loreto,Elgion da Silva; Vinocur,Myriam Elizabeth; Pozzobon,Ricardo; Azevedo,Marcos da Silva. |
| The aim was to detect the presence of polymorphisms at exons 1, 2, 3 and 4 of the Spi2 gene, and evaluate a possible association between them and recurrent airway obstruction (RAO) or inflammatory airway disease (IAD) in thoroughbred horses, through single-strand conformational-polymorphism (SSCP) screening. Although polymorphism was not detected in exons 1, 2 and 3, three alleles and six genotypes were identified in exon 4. The frequencies of allele A (0.6388) and genotype AA (0.3888) were higher in horses affected by RAO, although no association was found between polymorphism and horses with either RAO or IAD. |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Horse; Respiratory disease; SSCP; Alpha-1-antitrypsin; Serpin. |
| Ano: 2011 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572011000300015 |
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| Topic,Aleksandra; Juranic,Zorica; Jelic,Svetislav; Magazinovic,Ivana Golubicic. |
| Alpha-1-antitrypsin (AAT) or serine protease inhibitor A1 (SERPINA1) is an important serine protease inhibitor in humans. The main physiological role of AAT is to inhibit neutrophil elastase (NE) released from triggered neutrophils, with an additional lesser role in the defense against damage inflicted by other serine proteases, such as cathepsin G and proteinase 3. Although there is a reported association between AAT polymorphism and different types of cancer, this association with hematological malignancies (HM) is, as yet, unknown. We identified AAT phenotypes by isoelectric focusing (in the pH 4.2-4.9 range) in 151 serum samples from patients with HM (Hodgkins lymphomas, non-Hodgkins lymphomas and malignant monoclonal gammopathies). Healthy... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Alpha-1-antitrypsin; Polymorphism; Lymphomas. |
| Ano: 2009 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572009000400008 |
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| Ljujic,Mila; Topic,Aleksandra; Nikolic,Aleksandra; Divac,Aleksandra; Grujic,Milan; Mitic-Milikic,Marija; Radojkovic,Dragica. |
| The alpha-1-antitrypsin (A1AT) gene is highly polymorphic, with more than 100 genetic variants identified of which some can affect A1AT protein concentration and/or function and lead to pulmonary and/or liver disease. This study reports on the characterization of a p.G320R variant found in two patients, one with emphysema and the other with lung cancer. This variant results from a single base-pair substitution in exon 4 of the A1AT gene, and has been characterized as P by isoelectric focusing. Functional evaluation of the A1AT p.G320R variant was through comparing specific trypsin inhibitory activity in two patients with pulmonary disorders, carriers of the p.G320R variant, and 19 healthy individuals, carriers of normal A1AT M variants. Results showed that... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Alpha-1-antitrypsin; Emphysema; Lung cancer; P variant; Specific trypsin inhibitory activity. |
| Ano: 2010 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572010000100002 |
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