» Articles » PMID: 29719508

The Multifaceted Effects of Alpha1-Antitrypsin on Neutrophil Functions

Overview
Journal Front Pharmacol
Date 2018 May 3
PMID 29719508
Citations 72
Authors
Affiliations
Soon will be listed here.
Abstract

Neutrophils are the predominant immune cells in human blood possessing heterogeneity, plasticity and functional diversity. The activation and recruitment of neutrophils into inflamed tissue in response to stimuli are tightly regulated processes. Alpha1-Antitrypsin (AAT), an acute phase protein, is one of the potent regulators of neutrophil activation via both -protease inhibitory and non-inhibitory functions. This review summarizes our current understanding of the effects of AAT on neutrophils, illustrating the interplay between AAT and the key effector functions of neutrophils.

Citing Articles

Advancing the understanding and treatment of lung pathologies associated with alpha 1 antitrypsin deficiency.

Turner A, Ficker J, Vianello A, Clarenbach C, Janciauskiene S, Chorostowska-Wynimko J Ther Adv Respir Dis. 2025; 19:17534666251318841.

PMID: 39980299 PMC: 11843710. DOI: 10.1177/17534666251318841.


Alpha-1 antitrypsin reduces inflammation and vasculopathy in mice with oxygen-induced retinopathy.

Suphapimol V, Liu Y, Prato S, Karnowski A, Hardy C, Morelli A J Inflamm (Lond). 2025; 22(1):6.

PMID: 39934776 PMC: 11817893. DOI: 10.1186/s12950-025-00431-3.


Elevated serum mtDNA in COVID-19 patients is linked to SARS-CoV-2 envelope protein targeting mitochondrial VDAC1, inducing apoptosis and mtDNA release.

Shteinfer-Kuzmine A, Verma A, Bornshten R, Ben Chetrit E, Ben-Yaacov A, Pahima H Apoptosis. 2024; 29(11-12):2025-2046.

PMID: 39375263 PMC: 11550248. DOI: 10.1007/s10495-024-02025-5.


Alpha-1-antitrypsin improves anastomotic healing in intestinal epithelial cells model.

Schukfeh N, Sivaraman K, Schmidt A, Vieten G, Dingemann J, Weidner J Pediatr Surg Int. 2024; 40(1):258.

PMID: 39347946 DOI: 10.1007/s00383-024-05841-7.


The Proteolytic Activity of Neutrophil-Derived Serine Proteases Bound to the Cell Surface Arming Lung Epithelial Cells for Viral Defense.

Assylbekova A, Allayarova M, Konysbekova M, Bekturgan A, Makhanova A, Brown S Molecules. 2024; 29(18).

PMID: 39339444 PMC: 11434079. DOI: 10.3390/molecules29184449.


References
1.
Coeshott C, Ohnemus C, Pilyavskaya A, Ross S, Wieczorek M, Kroona H . Converting enzyme-independent release of tumor necrosis factor alpha and IL-1beta from a stimulated human monocytic cell line in the presence of activated neutrophils or purified proteinase 3. Proc Natl Acad Sci U S A. 1999; 96(11):6261-6. PMC: 26869. DOI: 10.1073/pnas.96.11.6261. View

2.
van Wetering S, Sterk P, Rabe K, Hiemstra P . Defensins: key players or bystanders in infection, injury, and repair in the lung?. J Allergy Clin Immunol. 1999; 104(6):1131-8. DOI: 10.1016/s0091-6749(99)70004-7. View

3.
Reeves E, Lu H, Jacobs H, Messina C, Bolsover S, Gabella G . Killing activity of neutrophils is mediated through activation of proteases by K+ flux. Nature. 2002; 416(6878):291-7. DOI: 10.1038/416291a. View

4.
Panyutich A, Hiemstra P, van Wetering S, Ganz T . Human neutrophil defensin and serpins form complexes and inactivate each other. Am J Respir Cell Mol Biol. 1995; 12(3):351-7. DOI: 10.1165/ajrcmb.12.3.7873202. View

5.
Duranton J, Boudier C, Belorgey D, Mellet P, Bieth J . DNA strongly impairs the inhibition of cathepsin G by alpha(1)-antichymotrypsin and alpha(1)-proteinase inhibitor. J Biol Chem. 2000; 275(6):3787-92. DOI: 10.1074/jbc.275.6.3787. View