RAGE-dependent NF-kB inflammation processes in the capsule of frozen shoulders.


Journal

Journal of shoulder and elbow surgery
ISSN: 1532-6500
Titre abrégé: J Shoulder Elbow Surg
Pays: United States
ID NLM: 9206499

Informations de publication

Date de publication:
Sep 2020
Historique:
received: 13 09 2019
revised: 30 12 2019
accepted: 01 01 2020
pubmed: 14 4 2020
medline: 14 1 2021
entrez: 14 4 2020
Statut: ppublish

Résumé

The etiology of frozen shoulder (FS) remains uncertain. Advanced glycation end-products (AGEs) cause the cross-linking and stabilization of collagen and are increased in FS. The purpose of this study was to elucidate the pathogenesis of FS by evaluating the receptor of AGE (RAGE)-dependent pathways. Tissue samples of the coracohumeral ligament (CHL) and anterior inferior glenohumeral ligament (IGHL) were collected from 33 patients with FS, with severe stiffness, and 25 with rotator cuff tears (RCTs) as controls. Gene expression levels of RAGE, high-mobility group box 1 (HMGB1), Toll-like receptor 2 (TLR2), TLR4, nuclear factor-kappa B (NF-kB), and cytokines were evaluated using a quantitative real-time polymerase chain reaction. The immunoreactivities of carboxymethyllysine (CML), pentosidine, and RAGE were also evaluated. CML and pentosidine were further evaluated using high-performance liquid chromatography. Gene expression levels of RAGE, HMGB1, TLR2, TLR4, and NF-kB were significantly greater in the CHLs and IGHLs from the FS group than in those from the RCT group. Immunoreactivities of RAGE and CML were stronger in the CHLs and IGHLs from the FS group than in those from the RCT group. Pentosidine was weakly immunostained in the CHLs and IGHLs from the FS group. CML using high-performance liquid chromatography was significantly greater in the CHLs and IGHLs from the FS group than in those from the RCT group. AGEs and HMGB1 might play important roles in the pathogenesis of FS by binding to RAGE and activating NF-kB signaling pathways. Suppression of these pathways could be a treatment option for FS.

Sections du résumé

BACKGROUND BACKGROUND
The etiology of frozen shoulder (FS) remains uncertain. Advanced glycation end-products (AGEs) cause the cross-linking and stabilization of collagen and are increased in FS. The purpose of this study was to elucidate the pathogenesis of FS by evaluating the receptor of AGE (RAGE)-dependent pathways.
METHODS METHODS
Tissue samples of the coracohumeral ligament (CHL) and anterior inferior glenohumeral ligament (IGHL) were collected from 33 patients with FS, with severe stiffness, and 25 with rotator cuff tears (RCTs) as controls. Gene expression levels of RAGE, high-mobility group box 1 (HMGB1), Toll-like receptor 2 (TLR2), TLR4, nuclear factor-kappa B (NF-kB), and cytokines were evaluated using a quantitative real-time polymerase chain reaction. The immunoreactivities of carboxymethyllysine (CML), pentosidine, and RAGE were also evaluated. CML and pentosidine were further evaluated using high-performance liquid chromatography.
RESULTS RESULTS
Gene expression levels of RAGE, HMGB1, TLR2, TLR4, and NF-kB were significantly greater in the CHLs and IGHLs from the FS group than in those from the RCT group. Immunoreactivities of RAGE and CML were stronger in the CHLs and IGHLs from the FS group than in those from the RCT group. Pentosidine was weakly immunostained in the CHLs and IGHLs from the FS group. CML using high-performance liquid chromatography was significantly greater in the CHLs and IGHLs from the FS group than in those from the RCT group.
CONCLUSIONS CONCLUSIONS
AGEs and HMGB1 might play important roles in the pathogenesis of FS by binding to RAGE and activating NF-kB signaling pathways. Suppression of these pathways could be a treatment option for FS.

Identifiants

pubmed: 32279986
pii: S1058-2746(20)30113-0
doi: 10.1016/j.jse.2020.01.076
pii:
doi:

Substances chimiques

HMGB1 Protein 0
NF-kappa B 0
Receptor for Advanced Glycation End Products 0
TLR2 protein, human 0
TLR4 protein, human 0
Toll-Like Receptor 2 0
Toll-Like Receptor 4 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

1884-1891

Informations de copyright

Copyright © 2020 Journal of Shoulder and Elbow Surgery Board of Trustees. Published by Elsevier Inc. All rights reserved.

Auteurs

Toshihisa Yano (T)

Department of Orthopaedic Surgery, Tohoku University School of Medicine, Sendai, Japan.

Yoshihiro Hagiwara (Y)

Department of Orthopaedic Surgery, Tohoku University School of Medicine, Sendai, Japan. Electronic address: hagi@med.tohoku.ac.jp.

Akira Ando (A)

Department of Orthopaedic Surgery, Matsuda Hospital, Sendai, Japan.

Kenji Kanazawa (K)

Department of Orthopaedic Surgery, South Miyagi Medical Center, Ogawara, Japan.

Masashi Koide (M)

Department of Orthopaedic Surgery, Matsuda Hospital, Sendai, Japan.

Takuya Sekiguchi (T)

Department of Orthopaedic Surgery, Iwate Prefectural Central Hospital, Morioka, Japan.

Nobuyuki Itaya (N)

Department of Orthopaedic Surgery, Sendai Hospital of East Japan Railway Company, Sendai, Japan.

Takahiro Onoki (T)

Department of Orthopaedic Surgery, Tohoku University School of Medicine, Sendai, Japan.

Kazuaki Suzuki (K)

Department of Orthopaedic Surgery, Tohoku University School of Medicine, Sendai, Japan.

Masahiro Tsuchiya (M)

Department of Nursing, Tohoku Fukushi University, Sendai, Japan.

Yasuhito Sogi (Y)

Department of Orthopaedic Surgery, Tohoku University School of Medicine, Sendai, Japan.

Yutaka Yabe (Y)

Department of Orthopaedic Surgery, Tohoku University School of Medicine, Sendai, Japan.

Eiji Itoi (E)

Department of Orthopaedic Surgery, Tohoku University School of Medicine, Sendai, Japan.

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Classifications MeSH