A Review of Alpha-1 Antitrypsin Binding Partners for Immune Regulation and Potential Therapeutic Application.
Apolipoproteins
/ metabolism
Binding Sites
/ genetics
COVID-19
/ metabolism
Caspases
/ metabolism
Complement System Proteins
/ metabolism
Cytokines
/ metabolism
Glycosylation
Humans
Mutation
Protein Binding
Protein Domains
SARS-CoV-2
/ physiology
alpha 1-Antitrypsin
/ chemistry
alpha 1-Antitrypsin Deficiency
/ genetics
alpha-1 antitrypsin
alpha-1 antitrypsin deficiency
complement C3
coronavirus disease 2019 (COVID-19)
cytokines
interleukin-6
proteases
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
23 Feb 2022
23 Feb 2022
Historique:
received:
07
02
2022
revised:
17
02
2022
accepted:
18
02
2022
entrez:
10
3
2022
pubmed:
11
3
2022
medline:
22
3
2022
Statut:
epublish
Résumé
Alpha-1 antitrypsin (AAT) is the canonical serine protease inhibitor of neutrophil-derived proteases and can modulate innate immune mechanisms through its anti-inflammatory activities mediated by a broad spectrum of protein, cytokine, and cell surface interactions. AAT contains a reactive methionine residue that is critical for its protease-specific binding capacity, whereby AAT entraps the protease on cleavage of its reactive centre loop, neutralises its activity by key changes in its tertiary structure, and permits removal of the AAT-protease complex from the circulation. Recently, however, the immunomodulatory role of AAT has come increasingly to the fore with several prominent studies focused on lipid or protein-protein interactions that are predominantly mediated through electrostatic, glycan, or hydrophobic potential binding sites. The aim of this review was to investigate the spectrum of AAT molecular interactions, with newer studies supporting a potential therapeutic paradigm for AAT augmentation therapy in disorders in which a chronic immune response is strongly linked.
Identifiants
pubmed: 35269582
pii: ijms23052441
doi: 10.3390/ijms23052441
pmc: PMC8910375
pii:
doi:
Substances chimiques
Apolipoproteins
0
Cytokines
0
alpha 1-Antitrypsin
0
Complement System Proteins
9007-36-7
Caspases
EC 3.4.22.-
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : US Alpha-1 Foundation
ID : Grant # 615848
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