Results 21 to 30 of about 2,894 (182)

Exogenous alpha 1-antitrypsin down-regulates SERPINA1 expression. [PDF]

open access: yesPLoS ONE, 2017
The main goal of the therapy with purified human plasma alpha1-antitrypsin (A1AT) is to increase A1AT levels and to prevent lungs from elastolytic activity in patients with PiZZ (Glu342Lys) A1AT deficiency-related emphysema.
Ahmad Karadagi   +14 more
doaj   +1 more source

Active trafficking of alpha 1 antitrypsin across the lung endothelium. [PDF]

open access: yesPLoS ONE, 2014
The homeostatic lung protective effects of alpha-1 antitrypsin (A1AT) may require the transport of circulating proteinase inhibitor across an intact lung endothelial barrier.
Angelia D Lockett   +13 more
doaj   +1 more source

How Can We Improve the Detection of Alpha1-Antitrypsin Deficiency? [PDF]

open access: yesPLoS ONE, 2015
The Z deficiency in α1-antitrypsin (A1ATD) is an under-recognized condition. Alpha1-antitrypsin (A1AT) is the main protein in the α1-globulin fraction of serum protein electrophoresis (SPE); however, evaluation of the α1-globulin protein fraction has ...
Ilaria Ferrarotti   +14 more
doaj   +1 more source

Impact of serine protease inhibitor alpha1-antitrypsin on expression of endoplasmic reticulum stress-induced proinflammatory factors in adipocytes

open access: yesBiochemistry and Biophysics Reports, 2021
Obesity-induced endoplasmic reticulum (ER) stress contributes to low-grade chronic inflammation in adipose tissue and may cause metabolic disorders such as diabetes mellitus and dyslipidemia.
Yukari Ando   +5 more
doaj   +1 more source

Optimal alpha-1 antitrypsin level cutoffs for genotype identification in patients with chronic liver disease

open access: yesHepatology Communications, 2023
Background:. Controversy exists whether alpha-1 antitrypsin (A1AT) genotype testing should be performed as a first-line screening for A1AT heterozygous variants. Methods:.
Sameer Prakash, Arvind R. Murali
doaj   +1 more source

Alpha 1-antitrypsin does not inhibit human monocyte caspase-1. [PDF]

open access: yesPLoS ONE, 2015
BACKGROUND:Alpha 1-antitrypsin (A1AT) is a 52 kDa serine protease inhibitor produced largely by hepatocytes but also by mononuclear phagocytes. A1AT chiefly inhibits neutrophil elastase and proteinase-3 but has also been reported to have immune ...
Mohd Akhlakur Rahman   +3 more
doaj   +1 more source

Proteoform Profiles Reveal That Alpha-1-Antitrypsin in Human Serum and Milk Is Derived From a Common Source

open access: yesFrontiers in Molecular Biosciences, 2022
The Alpha-1-Antitrypsin (A1AT) protein is an important protease inhibitor highly abundant in human serum and other body fluids. Additional to functioning as a protease inhibitor, A1AT is an important acute phase protein.
Shelley Jager   +14 more
doaj   +1 more source

Novel Vascularized Human Liver Organoids for Modeling Alcohol-Induced Liver Injury and Developing Hepatoprotective Therapy. [PDF]

open access: yesAdv Sci (Weinh)
This study successfully engineered vascularized liver organoids (3HLOs) by co‐culturing human reprogrammed hepatocyte‐like cells (hrHLs) with human umbilical vein endothelial cells (HUVECs) and human umbilical mesenchymal stem cells (HUMSCs). Upon implantation, the 3HLOs established functional vascular anastomosis with the host circulation and ...
Yang K   +13 more
europepmc   +2 more sources

Role of the P2 residue of human alpha 1-antitrypsin in determining target protease specificity. [PDF]

open access: yesPLoS ONE, 2017
Alpha 1-antitrypsin (A1AT) is a serine protease inhibitor that mainly inhibits neutrophil elastase in the lungs. A variant of A1AT at the P1 position with methionine 358 to arginine (A1AT-Pittsburgh) is a rapid inhibitor of thrombin with greatly ...
Hye-Shin Chung   +3 more
doaj   +1 more source

α-Linoleic Acid Enhances the Capacity of α1-Antitrypsin to Inhibit Lipopolysaccharide-Induced IL-1β in Human Blood Neutrophils

open access: yesMolecular Medicine, 2016
Alphal-antitrypsin (A1AT, SERPINA1), a major circulating inhibitor of neutrophil elastase (NE) and protelnase-3 (PR3), has been proposed to reduce the processing and release of IL-1β.
Nupur Aggarwal   +7 more
doaj   +1 more source

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