Plasma Glycosaminoglycan Profiles in Systemic Sclerosis: Associations with MMP-3, MMP-10, TIMP-1, TIMP-2, and TGF-Beta
The aim of the study was to determine whether plasma levels of total glycosaminoglycans (GAGs), matrix metalloproteinases (MMPs) (MMP-3, MMP-10), and their tissue inhibitors (TIMPs) (TIMP-1, TIMP-2) as well as transforming growth factor β (TGF-β) differ in the patients with systemic sclerosis (SSc)...
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Published in | BioMed research international Vol. 2020; no. 2020; pp. 1 - 8 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Cairo, Egypt
Hindawi Publishing Corporation
2020
Hindawi John Wiley & Sons, Inc |
Subjects | |
Online Access | Get full text |
ISSN | 2314-6133 2314-6141 2314-6141 |
DOI | 10.1155/2020/6416514 |
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Abstract | The aim of the study was to determine whether plasma levels of total glycosaminoglycans (GAGs), matrix metalloproteinases (MMPs) (MMP-3, MMP-10), and their tissue inhibitors (TIMPs) (TIMP-1, TIMP-2) as well as transforming growth factor β (TGF-β) differ in the patients with systemic sclerosis (SSc) in relation to the healthy subjects. Plasma samples were obtained from 106 people (64 patients with SSc and 42 healthy individuals) and measured for MMP-3, MMP-10, TIMP-1, TIMP-2, and TGF-β levels using ELISA methods. GAGs isolated from plasma samples were quantified using a hexuronic acid assay. The plasma levels of total GAGs, TIMP-1, TIMP-2, and TGF-β were significantly higher, while MMP-3 was significantly decreased in SSc patients compared to the controls. We have revealed a significant correlation between plasma GAGs and TGF-β (r=–0.47) and TIMP-2 (r=0.38), respectively. The results of this study revealed that remodeling of the extracellular matrix, reflected by quantitative changes in plasma glycosaminoglycans, occurs during systemic sclerosis. Thus, the alterations in GAG metabolism connected with SSc may lead to systemic changes in the properties of the connective tissue extracellular matrix. |
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AbstractList | The aim of the study was to determine whether plasma levels of total glycosaminoglycans (GAGs), matrix metalloproteinases (MMPs) (MMP-3, MMP-10), and their tissue inhibitors (TIMPs) (TIMP-1, TIMP-2) as well as transforming growth factor β (TGF-β) differ in the patients with systemic sclerosis (SSc) in relation to the healthy subjects. Plasma samples were obtained from 106 people (64 patients with SSc and 42 healthy individuals) and measured for MMP-3, MMP-10, TIMP-1, TIMP-2, and TGF-β levels using ELISA methods. GAGs isolated from plasma samples were quantified using a hexuronic acid assay. The plasma levels of total GAGs, TIMP-1, TIMP-2, and TGF-β were significantly higher, while MMP-3 was significantly decreased in SSc patients compared to the controls. We have revealed a significant correlation between plasma GAGs and TGF-β (r = -0.47) and TIMP-2 (r = 0.38), respectively. The results of this study revealed that remodeling of the extracellular matrix, reflected by quantitative changes in plasma glycosaminoglycans, occurs during systemic sclerosis. Thus, the alterations in GAG metabolism connected with SSc may lead to systemic changes in the properties of the connective tissue extracellular matrix.The aim of the study was to determine whether plasma levels of total glycosaminoglycans (GAGs), matrix metalloproteinases (MMPs) (MMP-3, MMP-10), and their tissue inhibitors (TIMPs) (TIMP-1, TIMP-2) as well as transforming growth factor β (TGF-β) differ in the patients with systemic sclerosis (SSc) in relation to the healthy subjects. Plasma samples were obtained from 106 people (64 patients with SSc and 42 healthy individuals) and measured for MMP-3, MMP-10, TIMP-1, TIMP-2, and TGF-β levels using ELISA methods. GAGs isolated from plasma samples were quantified using a hexuronic acid assay. The plasma levels of total GAGs, TIMP-1, TIMP-2, and TGF-β were significantly higher, while MMP-3 was significantly decreased in SSc patients compared to the controls. We have revealed a significant correlation between plasma GAGs and TGF-β (r = -0.47) and TIMP-2 (r = 0.38), respectively. The results of this study revealed that remodeling of the extracellular matrix, reflected by quantitative changes in plasma glycosaminoglycans, occurs during systemic sclerosis. Thus, the alterations in GAG metabolism connected with SSc may lead to systemic changes in the properties of the connective tissue extracellular matrix. The aim of the study was to determine whether plasma levels of total glycosaminoglycans (GAGs), matrix metalloproteinases (MMPs) (MMP‐3, MMP‐10), and their tissue inhibitors (TIMPs) (TIMP‐1, TIMP‐2) as well as transforming growth factor β (TGF‐ β ) differ in the patients with systemic sclerosis (SSc) in relation to the healthy subjects. Plasma samples were obtained from 106 people (64 patients with SSc and 42 healthy individuals) and measured for MMP‐3, MMP‐10, TIMP‐1, TIMP‐2, and TGF‐ β levels using ELISA methods. GAGs isolated from plasma samples were quantified using a hexuronic acid assay. The plasma levels of total GAGs, TIMP‐1, TIMP‐2, and TGF‐ β were significantly higher, while MMP‐3 was significantly decreased in SSc patients compared to the controls. We have revealed a significant correlation between plasma GAGs and TGF‐ β ( r = –0.47) and TIMP‐2 ( r = 0.38), respectively. The results of this study revealed that remodeling of the extracellular matrix, reflected by quantitative changes in plasma glycosaminoglycans, occurs during systemic sclerosis. Thus, the alterations in GAG metabolism connected with SSc may lead to systemic changes in the properties of the connective tissue extracellular matrix. The aim of the study was to determine whether plasma levels of total glycosaminoglycans (GAGs), matrix metalloproteinases (MMPs) (MMP-3, MMP-10), and their tissue inhibitors (TIMPs) (TIMP-1, TIMP-2) as well as transforming growth factor (TGF- ) differ in the patients with systemic sclerosis (SSc) in relation to the healthy subjects. Plasma samples were obtained from 106 people (64 patients with SSc and 42 healthy individuals) and measured for MMP-3, MMP-10, TIMP-1, TIMP-2, and TGF- levels using ELISA methods. GAGs isolated from plasma samples were quantified using a hexuronic acid assay. The plasma levels of total GAGs, TIMP-1, TIMP-2, and TGF- were significantly higher, while MMP-3 was significantly decreased in SSc patients compared to the controls. We have revealed a significant correlation between plasma GAGs and TGF- ( = -0.47) and TIMP-2 ( = 0.38), respectively. The results of this study revealed that remodeling of the extracellular matrix, reflected by quantitative changes in plasma glycosaminoglycans, occurs during systemic sclerosis. Thus, the alterations in GAG metabolism connected with SSc may lead to systemic changes in the properties of the connective tissue extracellular matrix. The aim of the study was to determine whether plasma levels of total glycosaminoglycans (GAGs), matrix metalloproteinases (MMPs) (MMP-3, MMP-10), and their tissue inhibitors (TIMPs) (TIMP-1, TIMP-2) as well as transforming growth factor β (TGF-β) differ in the patients with systemic sclerosis (SSc) in relation to the healthy subjects. Plasma samples were obtained from 106 people (64 patients with SSc and 42 healthy individuals) and measured for MMP-3, MMP-10, TIMP-1, TIMP-2, and TGF-β levels using ELISA methods. GAGs isolated from plasma samples were quantified using a hexuronic acid assay. The plasma levels of total GAGs, TIMP-1, TIMP-2, and TGF-β were significantly higher, while MMP-3 was significantly decreased in SSc patients compared to the controls. We have revealed a significant correlation between plasma GAGs and TGF-β (r=–0.47) and TIMP-2 (r=0.38), respectively. The results of this study revealed that remodeling of the extracellular matrix, reflected by quantitative changes in plasma glycosaminoglycans, occurs during systemic sclerosis. Thus, the alterations in GAG metabolism connected with SSc may lead to systemic changes in the properties of the connective tissue extracellular matrix. |
Audience | Academic |
Author | Kotulska-Kucharz, Anna Winsz-Szczotka, Katarzyna Jura-Półtorak, Agnieszka Komosinska-Vassev, Katarzyna Kuźnik-Trocha, Kornelia Kotyla, Przemyslaw J. Kucharz, Eugeniusz J. Olczyk, Krystyna |
AuthorAffiliation | 1 Department of Clinical Chemistry and Laboratory Diagnostics, Faculty of Pharmaceutical Sciences in Sosnowiec, Medical University of Silesia, Katowice, Poland 2 Department of Internal Medicine, Rheumatology and Clinical Immunology, Faculty of Medical Sciences in Katowice, Medical University of Silesia, Katowice, Poland |
AuthorAffiliation_xml | – name: 2 Department of Internal Medicine, Rheumatology and Clinical Immunology, Faculty of Medical Sciences in Katowice, Medical University of Silesia, Katowice, Poland – name: 1 Department of Clinical Chemistry and Laboratory Diagnostics, Faculty of Pharmaceutical Sciences in Sosnowiec, Medical University of Silesia, Katowice, Poland |
Author_xml | – sequence: 1 fullname: Olczyk, Krystyna – sequence: 2 fullname: Kucharz, Eugeniusz J. – sequence: 3 fullname: Kotulska-Kucharz, Anna – sequence: 4 fullname: Jura-Półtorak, Agnieszka – sequence: 5 fullname: Komosinska-Vassev, Katarzyna – sequence: 6 fullname: Winsz-Szczotka, Katarzyna – sequence: 7 fullname: Kuźnik-Trocha, Kornelia – sequence: 8 fullname: Kotyla, Przemyslaw J. |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/32382564$$D View this record in MEDLINE/PubMed |
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CitedBy_id | crossref_primary_10_1186_s12967_024_05411_4 crossref_primary_10_5114_reum_2020_102004 crossref_primary_10_1093_rheumatology_keab580 crossref_primary_10_17650_1818_8338_2022_16_4_K658 crossref_primary_10_3892_ijmm_2022_5194 |
Cites_doi | 10.1016/s0190-9622(00)90011-2 10.1016/S0928-4680(97)00170-3 10.1111/j.1432-1033.1992.tb16778.x 10.2147/btt.s2806 10.1016/S0021-9258(18)99267-7 10.1016/j.cardiores.2005.12.002 10.1016/0304-4165(94)00123-f 10.1186/s13075-015-0591-8 10.1080/14397595.2016.1206510 10.1007/s004030050224 10.1016/0003-2697(73)90377-1 10.1007/s11010-006-9230-7 10.1371/journal.pone.0115596 10.1002/jcla.21864 10.1111/j.1600-0625.2009.00999.x 10.1093/rheumatology/ken481 10.1016/0009-8981(94)90255-0 10.1136/annrheumdis-2012-201958 10.5604/17322693.1196355 10.1080/1354750X.2018.1548032 10.1093/rheumatology/kes090 10.1136/annrheumdis-2013-204424 10.1111/j.1365-2133.1992.tb08399.x 10.1136/ard.2006.066530 10.1172/JCI12020 10.4161/self.2.1.14058 10.1007/s004030050225 10.1007/s00403-009-0996-9 |
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Copyright | Copyright © 2020 Kornelia Kuźnik-Trocha et al. COPYRIGHT 2020 John Wiley & Sons, Inc. Copyright © 2020 Kornelia Kuźnik-Trocha et al. This is an open access article distributed under the Creative Commons Attribution License (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. http://creativecommons.org/licenses/by/4.0 Copyright © 2020 Kornelia Kuźnik-Trocha et al. 2020 |
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SubjectTerms | Adult Biosynthesis Bone morphogenetic proteins Connective tissues Disease Enzyme-linked immunosorbent assay Enzymes Extracellular matrix Female Glycosaminoglycans Glycosaminoglycans - blood Growth factors Hemoglobin Humans Immunoassay Laboratories Male Matrix metalloproteinase Matrix Metalloproteinase 10 - blood Matrix Metalloproteinase 3 - blood Matrix metalloproteinases Metabolism Middle Aged Physiological aspects Plasma Plasma levels Proteins Scleroderma Scleroderma (Disease) Scleroderma, Systemic - blood Skin Stromelysin 1 Stromelysin 2 Systemic scleroderma Systemic sclerosis Tissue inhibitor of metalloproteinase 1 Tissue inhibitor of metalloproteinase 2 Tissue Inhibitor of Metalloproteinase-1 - blood Tissue Inhibitor of Metalloproteinase-2 - blood Transforming Growth Factor beta - blood Transforming growth factor-b Transforming growth factors |
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Title | Plasma Glycosaminoglycan Profiles in Systemic Sclerosis: Associations with MMP-3, MMP-10, TIMP-1, TIMP-2, and TGF-Beta |
URI | https://search.emarefa.net/detail/BIM-1135862 https://dx.doi.org/10.1155/2020/6416514 https://www.ncbi.nlm.nih.gov/pubmed/32382564 https://www.proquest.com/docview/2397478646 https://www.proquest.com/docview/2400541328 https://pubmed.ncbi.nlm.nih.gov/PMC7196135 |
Volume | 2020 |
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