Expression and Localization of Thrombospondins, Plastin 3, and STIM1 in Different Cartilage Compartments of the Osteoarthritic Varus Knee

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Expression and Localization of Thrombospondins, Plastin 3, and STIM1 in Different Cartilage Compartments of the Osteoarthritic Varus Knee. / Mählich, Daniela; Glasmacher, Anne; Müller, Ilka; Oppermann, Johannes; Grevenstein, David; Eysel, Peer; Heilig, Juliane; Wirth, Brunhilde; Zaucke, Frank; Niehoff, Anja.

in: International journal of molecular sciences, Jahrgang 22, Nr. 6, 3073, 03.2021, S. 1-19.

Publikationen: Beitrag in FachzeitschriftZeitschriftenaufsätzeForschungBegutachtung

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@article{b5c7c15414c14fbf91be2c0ecf09bbcf,
title = "Expression and Localization of Thrombospondins, Plastin 3, and STIM1 in Different Cartilage Compartments of the Osteoarthritic Varus Knee",
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 Ca2+-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 Ca2+-dependent mechanotransduction between the ECM and the actin cytoskeleton might play an essential role in the pathomechanism of OA.",
keywords = "Aged, Aged, 80 and over, Cartilage Oligomeric Matrix Protein/metabolism, Cartilage, Articular/metabolism, Chondrocytes/metabolism, Female, Humans, Knee Joint/metabolism, Male, Membrane Glycoproteins/metabolism, Microfilament Proteins/metabolism, Middle Aged, Osteoarthritis, Knee/metabolism, Protein Transport, Stromal Interaction Molecule 1/metabolism, Thrombospondins/metabolism",
author = "Daniela M{\"a}hlich and Anne Glasmacher and Ilka M{\"u}ller and Johannes Oppermann and David Grevenstein and Peer Eysel and Juliane Heilig and Brunhilde Wirth and Frank Zaucke and Anja Niehoff",
year = "2021",
month = mar,
doi = "10.3390/ijms22063073",
language = "English",
volume = "22",
pages = "1--19",
journal = "International journal of molecular sciences",
issn = "1422-0067",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
number = "6",

}

RIS

TY - JOUR

T1 - Expression and Localization of Thrombospondins, Plastin 3, and STIM1 in Different Cartilage Compartments of the Osteoarthritic Varus Knee

AU - Mählich, Daniela

AU - Glasmacher, Anne

AU - Müller, Ilka

AU - Oppermann, Johannes

AU - Grevenstein, David

AU - Eysel, Peer

AU - Heilig, Juliane

AU - Wirth, Brunhilde

AU - Zaucke, Frank

AU - Niehoff, Anja

PY - 2021/3

Y1 - 2021/3

N2 - 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 Ca2+-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 Ca2+-dependent mechanotransduction between the ECM and the actin cytoskeleton might play an essential role in the pathomechanism of OA.

AB - 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 Ca2+-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 Ca2+-dependent mechanotransduction between the ECM and the actin cytoskeleton might play an essential role in the pathomechanism of OA.

KW - Aged

KW - Aged, 80 and over

KW - Cartilage Oligomeric Matrix Protein/metabolism

KW - Cartilage, Articular/metabolism

KW - Chondrocytes/metabolism

KW - Female

KW - Humans

KW - Knee Joint/metabolism

KW - Male

KW - Membrane Glycoproteins/metabolism

KW - Microfilament Proteins/metabolism

KW - Middle Aged

KW - Osteoarthritis, Knee/metabolism

KW - Protein Transport

KW - Stromal Interaction Molecule 1/metabolism

KW - Thrombospondins/metabolism

UR - https://www.mendeley.com/catalogue/d8b69194-52d2-3a8e-a08c-eb11d7a25305/

U2 - 10.3390/ijms22063073

DO - 10.3390/ijms22063073

M3 - Journal articles

C2 - 33802838

VL - 22

SP - 1

EP - 19

JO - International journal of molecular sciences

JF - International journal of molecular sciences

SN - 1422-0067

IS - 6

M1 - 3073

ER -

ID: 5964313