Peptidyl Arginine Deiminases in Chronic Diseases: A Focus on Rheumatoid Arthritis and Interstitial Lung Disease

Protein citrullination is accomplished by a broad enzyme family named Peptidyl Arginine Deiminases (PADs), which makes this post-translational modification in many proteins that perform physiological and pathologic mechanisms in the body. Due to these modifications, citrullination has become a signi...

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Main Authors: Karol J. Nava-Quiroz, Luis A. López-Flores, Gloria Pérez-Rubio, Jorge Rojas-Serrano, Ramcés Falfán-Valencia
Format: Article
Language:English
Published: MDPI AG 2023-12-01
Series:Cells
Subjects:
Online Access:https://www.mdpi.com/2073-4409/12/24/2829
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author Karol J. Nava-Quiroz
Luis A. López-Flores
Gloria Pérez-Rubio
Jorge Rojas-Serrano
Ramcés Falfán-Valencia
author_facet Karol J. Nava-Quiroz
Luis A. López-Flores
Gloria Pérez-Rubio
Jorge Rojas-Serrano
Ramcés Falfán-Valencia
author_sort Karol J. Nava-Quiroz
collection DOAJ
description Protein citrullination is accomplished by a broad enzyme family named Peptidyl Arginine Deiminases (PADs), which makes this post-translational modification in many proteins that perform physiological and pathologic mechanisms in the body. Due to these modifications, citrullination has become a significant topic in the study of pathological processes. It has been related to some chronic and autoimmune diseases, including rheumatoid arthritis (RA), interstitial lung diseases (ILD), multiple sclerosis (MS), and certain types of cancer, among others. Antibody production against different targets, including filaggrin, vimentin, and collagen, results in an immune response if they are citrullinated, which triggers a continuous inflammatory process characteristic of autoimmune and certain chronic diseases. PAD coding genes (<i>PADI1</i> to <i>PADI4</i> and <i>PADI6</i>) harbor variations that can be important in these enzymes’ folding, activity, function, and half-life. However, few studies have considered these genetic factors in the context of chronic diseases. Exploring PAD pathways and their role in autoimmune and chronic diseases is a major topic in developing new pharmacological targets and valuable biomarkers to improve diagnosis and prevention. The present review addresses and highlights genetic, molecular, biochemical, and physiopathological factors where PAD enzymes perform a major role in autoimmune and chronic diseases.
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spelling doaj.art-92220b56f835434498212a53d435e5d92023-12-22T13:59:43ZengMDPI AGCells2073-44092023-12-011224282910.3390/cells12242829Peptidyl Arginine Deiminases in Chronic Diseases: A Focus on Rheumatoid Arthritis and Interstitial Lung DiseaseKarol J. Nava-Quiroz0Luis A. López-Flores1Gloria Pérez-Rubio2Jorge Rojas-Serrano3Ramcés Falfán-Valencia4HLA Laboratory, Instituto Nacional de Enfermedades Respiratorias Ismael Cosío Villegas, Tlalpan, Mexico City 14080, MexicoHLA Laboratory, Instituto Nacional de Enfermedades Respiratorias Ismael Cosío Villegas, Tlalpan, Mexico City 14080, MexicoHLA Laboratory, Instituto Nacional de Enfermedades Respiratorias Ismael Cosío Villegas, Tlalpan, Mexico City 14080, MexicoRheumatology Clinic, Instituto Nacional de Enfermedades Respiratorias Ismael Cosío Villegas, Tlalpan, Mexico City 14080, MexicoHLA Laboratory, Instituto Nacional de Enfermedades Respiratorias Ismael Cosío Villegas, Tlalpan, Mexico City 14080, MexicoProtein citrullination is accomplished by a broad enzyme family named Peptidyl Arginine Deiminases (PADs), which makes this post-translational modification in many proteins that perform physiological and pathologic mechanisms in the body. Due to these modifications, citrullination has become a significant topic in the study of pathological processes. It has been related to some chronic and autoimmune diseases, including rheumatoid arthritis (RA), interstitial lung diseases (ILD), multiple sclerosis (MS), and certain types of cancer, among others. Antibody production against different targets, including filaggrin, vimentin, and collagen, results in an immune response if they are citrullinated, which triggers a continuous inflammatory process characteristic of autoimmune and certain chronic diseases. PAD coding genes (<i>PADI1</i> to <i>PADI4</i> and <i>PADI6</i>) harbor variations that can be important in these enzymes’ folding, activity, function, and half-life. However, few studies have considered these genetic factors in the context of chronic diseases. Exploring PAD pathways and their role in autoimmune and chronic diseases is a major topic in developing new pharmacological targets and valuable biomarkers to improve diagnosis and prevention. The present review addresses and highlights genetic, molecular, biochemical, and physiopathological factors where PAD enzymes perform a major role in autoimmune and chronic diseases.https://www.mdpi.com/2073-4409/12/24/2829peptidyl arginine deiminasesPADcitrullinationrheumatoid arthritisinterstitial lung diseaseinflammation
spellingShingle Karol J. Nava-Quiroz
Luis A. López-Flores
Gloria Pérez-Rubio
Jorge Rojas-Serrano
Ramcés Falfán-Valencia
Peptidyl Arginine Deiminases in Chronic Diseases: A Focus on Rheumatoid Arthritis and Interstitial Lung Disease
Cells
peptidyl arginine deiminases
PAD
citrullination
rheumatoid arthritis
interstitial lung disease
inflammation
title Peptidyl Arginine Deiminases in Chronic Diseases: A Focus on Rheumatoid Arthritis and Interstitial Lung Disease
title_full Peptidyl Arginine Deiminases in Chronic Diseases: A Focus on Rheumatoid Arthritis and Interstitial Lung Disease
title_fullStr Peptidyl Arginine Deiminases in Chronic Diseases: A Focus on Rheumatoid Arthritis and Interstitial Lung Disease
title_full_unstemmed Peptidyl Arginine Deiminases in Chronic Diseases: A Focus on Rheumatoid Arthritis and Interstitial Lung Disease
title_short Peptidyl Arginine Deiminases in Chronic Diseases: A Focus on Rheumatoid Arthritis and Interstitial Lung Disease
title_sort peptidyl arginine deiminases in chronic diseases a focus on rheumatoid arthritis and interstitial lung disease
topic peptidyl arginine deiminases
PAD
citrullination
rheumatoid arthritis
interstitial lung disease
inflammation
url https://www.mdpi.com/2073-4409/12/24/2829
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