Secreted osteopontin is highly polymerized in human airways and fragmented in asthmatic airway secretions.

Osteopontin (OPN) is a member of the small integrin-binding ligand N-linked glycoprotein (SIBLING) family and a cytokine with diverse biologic roles. OPN undergoes extensive post-translational modifications, including polymerization and proteolytic fragmentation, which alters its biologic activity....

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Main Authors: Mehrdad Arjomandi, Jessica Frelinger, Aneesh Donde, Hofer Wong, Amritha Yellamilli, Wilfred Raymond
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2011-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3198733?pdf=render
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author Mehrdad Arjomandi
Jessica Frelinger
Aneesh Donde
Hofer Wong
Amritha Yellamilli
Wilfred Raymond
author_facet Mehrdad Arjomandi
Jessica Frelinger
Aneesh Donde
Hofer Wong
Amritha Yellamilli
Wilfred Raymond
author_sort Mehrdad Arjomandi
collection DOAJ
description Osteopontin (OPN) is a member of the small integrin-binding ligand N-linked glycoprotein (SIBLING) family and a cytokine with diverse biologic roles. OPN undergoes extensive post-translational modifications, including polymerization and proteolytic fragmentation, which alters its biologic activity. Recent studies suggest that OPN may contribute to the pathogenesis of asthma.To determine whether secreted OPN (sOPN) is polymerized in human airways and whether it is qualitatively different in asthma, we used immunoblotting to examine sOPN in bronchoalveolar lavage (BAL) fluid samples from 12 healthy and 21 asthmatic subjects (and in sputum samples from 27 healthy and 21 asthmatic subjects). All asthmatic subjects had mild to moderate asthma and abstained from corticosteroids during the study. Furthermore, we examined the relationship between airway sOPN and cellular inflammation.We found that sOPN in BAL fluid and sputum exists in polymeric, monomeric, and cleaved forms, with most of it in polymeric form. Compared to healthy subjects, asthmatic subjects had proportionately less polymeric sOPN and more monomeric and cleaved sOPN. Polymeric sOPN in BAL fluid was associated with increased alveolar macrophage counts in airways in all subjects.These results suggest that sOPN in human airways (1) undergoes extensive post-translational modification by polymerization and proteolytic fragmentation, (2) is more fragmented and less polymerized in subjects with mild to moderate asthma, and (3) may contribute to recruitment or survival of alveolar macrophages.
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spelling doaj.art-3c2492ff16a845989cdbe21ac43a2b292022-12-22T02:06:40ZengPublic Library of Science (PLoS)PLoS ONE1932-62032011-01-01610e2567810.1371/journal.pone.0025678Secreted osteopontin is highly polymerized in human airways and fragmented in asthmatic airway secretions.Mehrdad ArjomandiJessica FrelingerAneesh DondeHofer WongAmritha YellamilliWilfred RaymondOsteopontin (OPN) is a member of the small integrin-binding ligand N-linked glycoprotein (SIBLING) family and a cytokine with diverse biologic roles. OPN undergoes extensive post-translational modifications, including polymerization and proteolytic fragmentation, which alters its biologic activity. Recent studies suggest that OPN may contribute to the pathogenesis of asthma.To determine whether secreted OPN (sOPN) is polymerized in human airways and whether it is qualitatively different in asthma, we used immunoblotting to examine sOPN in bronchoalveolar lavage (BAL) fluid samples from 12 healthy and 21 asthmatic subjects (and in sputum samples from 27 healthy and 21 asthmatic subjects). All asthmatic subjects had mild to moderate asthma and abstained from corticosteroids during the study. Furthermore, we examined the relationship between airway sOPN and cellular inflammation.We found that sOPN in BAL fluid and sputum exists in polymeric, monomeric, and cleaved forms, with most of it in polymeric form. Compared to healthy subjects, asthmatic subjects had proportionately less polymeric sOPN and more monomeric and cleaved sOPN. Polymeric sOPN in BAL fluid was associated with increased alveolar macrophage counts in airways in all subjects.These results suggest that sOPN in human airways (1) undergoes extensive post-translational modification by polymerization and proteolytic fragmentation, (2) is more fragmented and less polymerized in subjects with mild to moderate asthma, and (3) may contribute to recruitment or survival of alveolar macrophages.http://europepmc.org/articles/PMC3198733?pdf=render
spellingShingle Mehrdad Arjomandi
Jessica Frelinger
Aneesh Donde
Hofer Wong
Amritha Yellamilli
Wilfred Raymond
Secreted osteopontin is highly polymerized in human airways and fragmented in asthmatic airway secretions.
PLoS ONE
title Secreted osteopontin is highly polymerized in human airways and fragmented in asthmatic airway secretions.
title_full Secreted osteopontin is highly polymerized in human airways and fragmented in asthmatic airway secretions.
title_fullStr Secreted osteopontin is highly polymerized in human airways and fragmented in asthmatic airway secretions.
title_full_unstemmed Secreted osteopontin is highly polymerized in human airways and fragmented in asthmatic airway secretions.
title_short Secreted osteopontin is highly polymerized in human airways and fragmented in asthmatic airway secretions.
title_sort secreted osteopontin is highly polymerized in human airways and fragmented in asthmatic airway secretions
url http://europepmc.org/articles/PMC3198733?pdf=render
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