Universität zu Köln

Maehlich, Daniela, Glasmacher, Anne, Mueller, Ilka, Oppermann, Johannes, Grevenstein, David ORCID: 0000-0003-4823-7739, Eysel, Peer, Heilig, Juliane, Wirth, Brunhilde ORCID: 0000-0003-4051-5191, Zaucke, Frank ORCID: 0000-0002-7680-9354 and Niehoff, Anja ORCID: 0000-0002-4165-0929 (2021). Expression and Localization of Thrombospondins, Plastin 3, and STIM1 in Different Cartilage Compartments of the Osteoarthritic Varus Knee. Int. J. Mol. Sci., 22 (6). BASEL: MDPI. ISSN 1422-0067

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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.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Maehlich, Daniela UNSPECIFIED UNSPECIFIED UNSPECIFIED Glasmacher, Anne UNSPECIFIED UNSPECIFIED UNSPECIFIED Mueller, Ilka UNSPECIFIED UNSPECIFIED UNSPECIFIED Oppermann, Johannes UNSPECIFIED UNSPECIFIED UNSPECIFIED Grevenstein, David UNSPECIFIED orcid.org/0000-0003-4823-7739 UNSPECIFIED Eysel, Peer UNSPECIFIED UNSPECIFIED UNSPECIFIED Heilig, Juliane UNSPECIFIED UNSPECIFIED UNSPECIFIED Wirth, Brunhilde UNSPECIFIED orcid.org/0000-0003-4051-5191 UNSPECIFIED Zaucke, Frank UNSPECIFIED orcid.org/0000-0002-7680-9354 UNSPECIFIED Niehoff, Anja UNSPECIFIED orcid.org/0000-0002-4165-0929 UNSPECIFIED
URN:	urn:nbn:de:hbz:38-584185
DOI:	10.3390/ijms22063073
Journal or Publication Title:	Int. J. Mol. Sci.
Volume:	22
Number:	6
Date:	2021
Publisher:	MDPI
Place of Publication:	BASEL
ISSN:	1422-0067
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language OLIGOMERIC MATRIX PROTEIN; EXTRACELLULAR-MATRIX Multiple languages Biochemistry & Molecular Biology; Chemistry, Multidisciplinary Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/58418