Expression and Localization of Thrombospondins, Plastin 3, and STIM1 in Different Cartilage Compartments of the Osteoarthritic Varus Knee
Osteoarthritis (OA) is a multifactorial disease which is characterized by a change in the homeostasis of the extracellular matrix (ECM). The ECM is essential for the function of the articular cartilage and plays an important role in cartilage mechanotransduction. To provide a better understanding of...
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| Veröffentlicht in: | International journal of molecular sciences 2021-03, Vol.22 (6), p.3073 |
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| description | Osteoarthritis (OA) is a multifactorial disease which is characterized by a change in the homeostasis of the extracellular matrix (ECM). The ECM is essential for the function of the articular cartilage and plays an important role in cartilage mechanotransduction. To provide a better understanding of the interaction between the ECM and the actin cytoskeleton, we investigated the localization and expression of the Ca
-dependent proteins cartilage oligomeric matrix protein (COMP), thrombospondin-1 (TSP-1), plastin 3 (PLS3) and stromal interaction molecule 1 (STIM1). We investigated 16 patients who suffered from varus knee OA and performed a topographical analysis of the cartilage from the medial and lateral compartment of the proximal tibial plateau. In a varus knee, OA is more pronounced in the medial compared to the lateral compartment as a result of an overloading due to the malalignment. We detected a location-dependent staining of PLS3 and STIM1 in the articular cartilage tissue. The staining intensity for both proteins correlated with the degree of cartilage degeneration. The staining intensity of TSP-1 was clearly reduced in the cartilage of the more affected medial compartment, an observation that was confirmed in cartilage extracts by immunoblotting. The total amount of COMP was unchanged; however, slight changes were detected in the localization of the protein. Our results provide novel information on alterations in OA cartilage suggesting that Ca
-dependent mechanotransduction between the ECM and the actin cytoskeleton might play an essential role in the pathomechanism of OA. |
| doi_str_mv | 10.3390/ijms22063073 |
| format | Article |
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-dependent proteins cartilage oligomeric matrix protein (COMP), thrombospondin-1 (TSP-1), plastin 3 (PLS3) and stromal interaction molecule 1 (STIM1). We investigated 16 patients who suffered from varus knee OA and performed a topographical analysis of the cartilage from the medial and lateral compartment of the proximal tibial plateau. In a varus knee, OA is more pronounced in the medial compared to the lateral compartment as a result of an overloading due to the malalignment. We detected a location-dependent staining of PLS3 and STIM1 in the articular cartilage tissue. The staining intensity for both proteins correlated with the degree of cartilage degeneration. The staining intensity of TSP-1 was clearly reduced in the cartilage of the more affected medial compartment, an observation that was confirmed in cartilage extracts by immunoblotting. The total amount of COMP was unchanged; however, slight changes were detected in the localization of the protein. Our results provide novel information on alterations in OA cartilage suggesting that Ca
-dependent mechanotransduction between the ECM and the actin cytoskeleton might play an essential role in the pathomechanism of OA.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms22063073</identifier><identifier>PMID: 33802838</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Actin ; Aged ; Aged, 80 and over ; Arthritis ; Biomedical materials ; Calcium ; Calcium ions ; Cartilage ; Cartilage (articular) ; Cartilage diseases ; Cartilage oligomeric matrix protein ; Cartilage Oligomeric Matrix Protein - metabolism ; Cartilage, Articular - metabolism ; Cell adhesion & migration ; Chondrocytes - metabolism ; Cytoskeleton ; Degeneration ; Disease ; Extracellular matrix ; Female ; Glycoproteins ; Homeostasis ; Humans ; Immunoblotting ; Knee ; Knee Joint - metabolism ; Knee Joint - pathology ; Localization ; Male ; Matrix protein ; Mechanotransduction ; Membrane Glycoproteins - metabolism ; Metabolism ; Microfilament Proteins - metabolism ; Middle Aged ; Mutation ; Osteoarthritis ; Osteoarthritis, Knee - metabolism ; Osteoarthritis, Knee - pathology ; Osteoporosis ; Protein Transport ; Proteins ; Signal transduction ; Staining ; STIM1 protein ; Stromal Interaction Molecule 1 - metabolism ; Thrombospondin ; Thrombospondins - metabolism</subject><ispartof>International journal of molecular sciences, 2021-03, Vol.22 (6), p.3073</ispartof><rights>2021. This work is licensed under http://creativecommons.org/licenses/by/3.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2021 by the authors. 2021</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c455t-252b746da8f5864bc7259b8108bc1127753d7480b296bbdc22c78529c1566f1a3</citedby><cites>FETCH-LOGICAL-c455t-252b746da8f5864bc7259b8108bc1127753d7480b296bbdc22c78529c1566f1a3</cites><orcidid>0000-0003-4051-5191 ; 0000-0002-7680-9354 ; 0000-0003-4823-7739 ; 0000-0002-4165-0929</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8002632/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8002632/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33802838$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mählich, Daniela</creatorcontrib><creatorcontrib>Glasmacher, Anne</creatorcontrib><creatorcontrib>Müller, Ilka</creatorcontrib><creatorcontrib>Oppermann, Johannes</creatorcontrib><creatorcontrib>Grevenstein, David</creatorcontrib><creatorcontrib>Eysel, Peer</creatorcontrib><creatorcontrib>Heilig, Juliane</creatorcontrib><creatorcontrib>Wirth, Brunhilde</creatorcontrib><creatorcontrib>Zaucke, Frank</creatorcontrib><creatorcontrib>Niehoff, Anja</creatorcontrib><title>Expression and Localization of Thrombospondins, Plastin 3, and STIM1 in Different Cartilage Compartments of the Osteoarthritic Varus Knee</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><description>Osteoarthritis (OA) is a multifactorial disease which is characterized by a change in the homeostasis of the extracellular matrix (ECM). The ECM is essential for the function of the articular cartilage and plays an important role in cartilage mechanotransduction. To provide a better understanding of the interaction between the ECM and the actin cytoskeleton, we investigated the localization and expression of the Ca
-dependent proteins cartilage oligomeric matrix protein (COMP), thrombospondin-1 (TSP-1), plastin 3 (PLS3) and stromal interaction molecule 1 (STIM1). We investigated 16 patients who suffered from varus knee OA and performed a topographical analysis of the cartilage from the medial and lateral compartment of the proximal tibial plateau. In a varus knee, OA is more pronounced in the medial compared to the lateral compartment as a result of an overloading due to the malalignment. We detected a location-dependent staining of PLS3 and STIM1 in the articular cartilage tissue. The staining intensity for both proteins correlated with the degree of cartilage degeneration. The staining intensity of TSP-1 was clearly reduced in the cartilage of the more affected medial compartment, an observation that was confirmed in cartilage extracts by immunoblotting. The total amount of COMP was unchanged; however, slight changes were detected in the localization of the protein. Our results provide novel information on alterations in OA cartilage suggesting that Ca
-dependent mechanotransduction between the ECM and the actin cytoskeleton might play an essential role in the pathomechanism of OA.</description><subject>Actin</subject><subject>Aged</subject><subject>Aged, 80 and over</subject><subject>Arthritis</subject><subject>Biomedical materials</subject><subject>Calcium</subject><subject>Calcium ions</subject><subject>Cartilage</subject><subject>Cartilage (articular)</subject><subject>Cartilage diseases</subject><subject>Cartilage oligomeric matrix protein</subject><subject>Cartilage Oligomeric Matrix Protein - metabolism</subject><subject>Cartilage, Articular - metabolism</subject><subject>Cell adhesion & migration</subject><subject>Chondrocytes - metabolism</subject><subject>Cytoskeleton</subject><subject>Degeneration</subject><subject>Disease</subject><subject>Extracellular matrix</subject><subject>Female</subject><subject>Glycoproteins</subject><subject>Homeostasis</subject><subject>Humans</subject><subject>Immunoblotting</subject><subject>Knee</subject><subject>Knee Joint - 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metabolism</topic><topic>Cartilage, Articular - metabolism</topic><topic>Cell adhesion & migration</topic><topic>Chondrocytes - metabolism</topic><topic>Cytoskeleton</topic><topic>Degeneration</topic><topic>Disease</topic><topic>Extracellular matrix</topic><topic>Female</topic><topic>Glycoproteins</topic><topic>Homeostasis</topic><topic>Humans</topic><topic>Immunoblotting</topic><topic>Knee</topic><topic>Knee Joint - metabolism</topic><topic>Knee Joint - pathology</topic><topic>Localization</topic><topic>Male</topic><topic>Matrix protein</topic><topic>Mechanotransduction</topic><topic>Membrane Glycoproteins - metabolism</topic><topic>Metabolism</topic><topic>Microfilament Proteins - metabolism</topic><topic>Middle Aged</topic><topic>Mutation</topic><topic>Osteoarthritis</topic><topic>Osteoarthritis, Knee - metabolism</topic><topic>Osteoarthritis, Knee - pathology</topic><topic>Osteoporosis</topic><topic>Protein Transport</topic><topic>Proteins</topic><topic>Signal transduction</topic><topic>Staining</topic><topic>STIM1 protein</topic><topic>Stromal Interaction Molecule 1 - metabolism</topic><topic>Thrombospondin</topic><topic>Thrombospondins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mählich, Daniela</creatorcontrib><creatorcontrib>Glasmacher, Anne</creatorcontrib><creatorcontrib>Müller, Ilka</creatorcontrib><creatorcontrib>Oppermann, Johannes</creatorcontrib><creatorcontrib>Grevenstein, David</creatorcontrib><creatorcontrib>Eysel, Peer</creatorcontrib><creatorcontrib>Heilig, Juliane</creatorcontrib><creatorcontrib>Wirth, Brunhilde</creatorcontrib><creatorcontrib>Zaucke, Frank</creatorcontrib><creatorcontrib>Niehoff, Anja</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Complete (ProQuest Database)</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>ProQuest research library</collection><collection>Research Library (Corporate)</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>International journal of molecular sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mählich, Daniela</au><au>Glasmacher, Anne</au><au>Müller, Ilka</au><au>Oppermann, Johannes</au><au>Grevenstein, David</au><au>Eysel, Peer</au><au>Heilig, Juliane</au><au>Wirth, Brunhilde</au><au>Zaucke, Frank</au><au>Niehoff, Anja</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression and Localization of Thrombospondins, Plastin 3, and STIM1 in Different Cartilage Compartments of the Osteoarthritic Varus Knee</atitle><jtitle>International journal of molecular sciences</jtitle><addtitle>Int J Mol Sci</addtitle><date>2021-03-17</date><risdate>2021</risdate><volume>22</volume><issue>6</issue><spage>3073</spage><pages>3073-</pages><issn>1422-0067</issn><issn>1661-6596</issn><eissn>1422-0067</eissn><abstract>Osteoarthritis (OA) is a multifactorial disease which is characterized by a change in the homeostasis of the extracellular matrix (ECM). The ECM is essential for the function of the articular cartilage and plays an important role in cartilage mechanotransduction. To provide a better understanding of the interaction between the ECM and the actin cytoskeleton, we investigated the localization and expression of the Ca
-dependent proteins cartilage oligomeric matrix protein (COMP), thrombospondin-1 (TSP-1), plastin 3 (PLS3) and stromal interaction molecule 1 (STIM1). We investigated 16 patients who suffered from varus knee OA and performed a topographical analysis of the cartilage from the medial and lateral compartment of the proximal tibial plateau. In a varus knee, OA is more pronounced in the medial compared to the lateral compartment as a result of an overloading due to the malalignment. We detected a location-dependent staining of PLS3 and STIM1 in the articular cartilage tissue. The staining intensity for both proteins correlated with the degree of cartilage degeneration. The staining intensity of TSP-1 was clearly reduced in the cartilage of the more affected medial compartment, an observation that was confirmed in cartilage extracts by immunoblotting. The total amount of COMP was unchanged; however, slight changes were detected in the localization of the protein. Our results provide novel information on alterations in OA cartilage suggesting that Ca
-dependent mechanotransduction between the ECM and the actin cytoskeleton might play an essential role in the pathomechanism of OA.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>33802838</pmid><doi>10.3390/ijms22063073</doi><orcidid>https://orcid.org/0000-0003-4051-5191</orcidid><orcidid>https://orcid.org/0000-0002-7680-9354</orcidid><orcidid>https://orcid.org/0000-0003-4823-7739</orcidid><orcidid>https://orcid.org/0000-0002-4165-0929</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | International journal of molecular sciences, 2021-03, Vol.22 (6), p.3073 |
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| subjects | Actin Aged Aged, 80 and over Arthritis Biomedical materials Calcium Calcium ions Cartilage Cartilage (articular) Cartilage diseases Cartilage oligomeric matrix protein Cartilage Oligomeric Matrix Protein - metabolism Cartilage, Articular - metabolism Cell adhesion & migration Chondrocytes - metabolism Cytoskeleton Degeneration Disease Extracellular matrix Female Glycoproteins Homeostasis Humans Immunoblotting Knee Knee Joint - metabolism Knee Joint - pathology Localization Male Matrix protein Mechanotransduction Membrane Glycoproteins - metabolism Metabolism Microfilament Proteins - metabolism Middle Aged Mutation Osteoarthritis Osteoarthritis, Knee - metabolism Osteoarthritis, Knee - pathology Osteoporosis Protein Transport Proteins Signal transduction Staining STIM1 protein Stromal Interaction Molecule 1 - metabolism Thrombospondin Thrombospondins - metabolism |
| title | Expression and Localization of Thrombospondins, Plastin 3, and STIM1 in Different Cartilage Compartments of the Osteoarthritic Varus Knee |
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