Evidence map›Paper›PMID 39224588›Full record

ReviewFrontiers in immunology2024

Immunological and homeostatic pathways of alpha -1 antitrypsin: a new therapeutic potential.

Carmen Mazzuca, Laura Vitiello, Silvia Travaglini, Fatima Maurizi, Panaiotis Finamore, Simona Santangelo, Amelia Rigon, Marta Vadacca, Silvia Angeletti, Simone Scarlata

Abstract readReview
In one paragraph

Review in Frontiers in immunology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed.

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  13. Case Report:Frontiers in immunology · 2026
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  18. Impact of Saharan Dust andInternational journal of molecular sciences · 2025
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Carmen MazzucaUnit of Internal Medicine and Geriatrics, Respiratory Pathophysiology and Thoracic Endoscopy, Fondazione Policlinico Campus Bio Medico University Hospital- Rome, Rome, Italy.
Laura VitielloDepartment of Human Sciences and Promotion of the Quality of Life, San Raffaele University, Rome, Italy.
Silvia TravagliniUnit of Internal Medicine and Geriatrics, Respiratory Pathophysiology and Thoracic Endoscopy, Fondazione Policlinico Campus Bio Medico University Hospital- Rome, Rome, Italy.
Fatima MauriziUnit of Internal Medicine and Geriatrics, Respiratory Pathophysiology and Thoracic Endoscopy, Fondazione Policlinico Campus Bio Medico University Hospital- Rome, Rome, Italy.
Panaiotis FinamoreUnit of Internal Medicine and Geriatrics, Respiratory Pathophysiology and Thoracic Endoscopy, Fondazione Policlinico Campus Bio Medico University Hospital- Rome, Rome, Italy.
Simona SantangeloUnit of Internal Medicine and Geriatrics, Respiratory Pathophysiology and Thoracic Endoscopy, Fondazione Policlinico Campus Bio Medico University Hospital- Rome, Rome, Italy.
Amelia RigonClinical and Research Section of Rheumatology and Clinical Immunology, Fondazione Policlinico Universitario Campus Bio-Medico, Rome, Italy.
Marta VadaccaClinical and Research Section of Rheumatology and Clinical Immunology, Fondazione Policlinico Universitario Campus Bio-Medico, Rome, Italy.
Silvia AngelettiUnit of Clinical Laboratory Science, University Campus Bio-Medico of Rome, Rome, Italy.
Simone ScarlataUnit of Internal Medicine and Geriatrics, Respiratory Pathophysiology and Thoracic Endoscopy, Fondazione Policlinico Campus Bio Medico University Hospital- Rome, Rome, Italy.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α -1 antitrypsin (A1AT) is a 52 kDa acute-phase glycoprotein belonging to the serine protease inhibitor superfamily (SERPIN). It is primarily synthesized by hepatocytes and to a lesser extent by monocytes, macrophages, intestinal epithelial cells, and bronchial epithelial cells. A1AT is encoded by SERPINA1 locus, also known as PI locus, highly polymorphic with at least 100 allelic variants described and responsible for different A1AT serum levels and function. A1AT inhibits a variety of serine proteinases, but its main target is represented by Neutrophil Elastase (NE). However, recent attention has been directed towards its immune-regulatory and homeostatic activities. A1AT exerts immune-regulatory effects on different cell types involved in innate and adaptive immunity. Additionally, it plays a role in metal and lipid metabolism, contributing to homeostasis. An adequate comprehension of these mechanisms could support the use of A1AT augmentation therapy in many disorders characterized by a chronic immune response. The aim of this review is to provide an up-to-date understanding of the molecular mechanisms and regulatory pathways responsible for immune-regulatory and homeostatic activities of A1AT. This knowledge aims to support the use of A1AT in therapeutic applications. Furthermore, the review summarizes the current state of knowledge regarding the application of A1AT in clinical and laboratory settings human and animal models.

Indexed as

alpha 1-AntitrypsinHomeostasisAdaptive ImmunityAnimalsHumansImmunity, Innatealpha 1-AntitrypsinSERPINA1 protein, humananti-inflammationautoimmune diseaseinfectious diseaseserine protease inhibitor superfamily (SERPIN)Severe Acute Respiratory Syndrome Coronavirus2 (SARS-CoV-2)

Identifiers

PMID39224588
PMCPMC11366583

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.