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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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