PRELP protein inhibits the formation of the complement membrane attack complex.

Happonen, Kaisa E.; Fürst, Camilla Melin; Saxne, Tore; Blom, Anna M.

doi:10.1074/jbc.a111.291476

Cited by 6 publications

(7 citation statements)

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“…Adam8, which is a metalloproteinase induced by TNF acting as a sheddase for the TNF receptor I thereby limiting TNF activity,41 has the ability to limit leucocyte recruitment and inflammation 42 . Prelp , an extracellular matrix protein found in the synovial fluid of patients with RA, limits inflammation and complement activation-mediated cartilage attack and represses osteoclast differentiation 43 44 . Prg4 encodes for Lubricin, a protein essential for the maintenance of articular cartilage and a negative regulator of synovial hyperplasia, thereby protecting against arthritis-induced joint destruction 45–47 .…”

Section: Discussionmentioning

confidence: 99%

Rsk2 controls synovial fibroblast hyperplasia and the course of arthritis

et al. 2014

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Section: Discussionmentioning

confidence: 99%

Rsk2 controls synovial fibroblast hyperplasia and the course of arthritis

et al. 2014

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“…Normal human serum (NHS) was prepared as described (14). Cartilage explants, collected after culture with or without IL-1a for different numbers of days, were washed three times with 200 ml HEPES ++ buffer (20 mM HEPES [pH 7.35], 120 mM NaCl, 1 mM MgCl 2 , 1 mM CaCl 2 ).…”

Section: Incubation Of Cartilage With Serum and Trypsin Digestionmentioning

confidence: 99%

“…Some activate complement, whereas others act as inhibitors. Thus, PRELP inhibits the formation of MAC and the assembly of the alternative pathway convertase (14). Fibromodulin (15), osteoadherin (16), and the G3 domain of aggrecan (17) activate the classical pathway of complement by binding C1q, whereas decorin, biglycan, and cartilage oligomeric matrix protein (COMP) inhibit the same pathway (16,18,19).…”

mentioning

confidence: 99%

Quantitative Mass Spectrometry To Study Inflammatory Cartilage Degradation and Resulting Interactions with the Complement System

Fürst

Åhrman

Bratteby

et al. 2016

The Journal of Immunology

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Joint diseases are often characterized by inflammatory processes that result in pathological changes in joint tissues, including cartilage degradation and release of components into the synovial fluid. The complement system plays a central role in promoting the inflammation. Because several cartilage proteins are known to interact with complement, causing either activation or inhibition of the system, we aimed to investigate these interactions comprehensively. Bovine cartilage explants were cultured with IL-1α to induce cartilage degradation, followed by incubation with human serum. Label-free selected reaction monitoring mass spectrometry was used to specifically quantify complement proteins interacting with the cartilage explant. In parallel, the time-dependent degradation of cartilage was detected using mass spectrometry analysis (liquid chromatography–tandem mass spectrometry). Complement proteins resulting from activation of the classical, alternative, and terminal pathways were detected on IL-1α–stimulated cartilage at time points when clear alterations in extracellular matrix composition had occurred. Increased levels of the complement activation product C4d, as detected by ELISA in serum after incubation with IL-1α–stimulated cartilage, confirmed the selected reaction monitoring results indicating complement activation. Further, typical activated (cleaved) C3 fragments were detected by Western blotting in extracts of IL-1α–stimulated cartilage. No complement activation was triggered by cartilage cultured in the absence of IL-1α. Components released from IL-1α–stimulated cartilage during culture had an inhibitory effect on complement activation. These were released after a longer incubation period with IL-1α and may represent a feedback reaction to cartilage-triggered complement activation observed after a shorter incubation period.

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“…Moreover, it locally regulates complement activation by capturing the complement inhibitor C4BP. It is also a known inhibitor of MAC formation at the level of C9 and inhibits C9 polymerization and C3 convertase of the alternative pathway …”

Section: Discussionmentioning

confidence: 99%

Comparative profiling of extractable proteins in extracellular matrices of porcine cholecyst and jejunum intended for preparation of tissue engineering scaffolds

Muhamed

Rajan

Surendran

et al. 2015

J. Biomed. Mater. Res.

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Scaffolds prepared from cholecyst and jejunum have differential immunological potential, despite similar biocompatibility, when used as subcutaneous grafts. The reason for differential immunogenicity is probably due to differences in the nature of protein composition and biomolecules in the extracellular matrices (ECMs) of source organs that are used for preparation of the scaffolds. Against this background, the present study aims to identify the extractable proteins of ECMs derived from porcine cholecyst and jejunum. The proteins were extracted and identified through a conventional database search following sodium dodecyl sulfate-polyacrylamide gel-electrophoresis separation and mass spectroscopy. The resultant protein profile was analyzed and at least 154 proteins in cholecyst-derived extracellular matrix (CDE) and 186 proteins in jejunum-derived extracellular matrix (JDE) were identified. Both the matrices contained several extracelluar proteins including fibronectin, nidogen, decorin, and lumican that are known to participate in wound healing responses. However, the CDE had fewer cellular proteins than JDE, especially the latter contained class-I and class-II histocompatibility antigens which are incriminated as potent immunogens responsible for graft rejection. The results of the study suggested that the ECMs used for the scaffold preparation need not be "acellular" and differences in the protein composition of the ECMs might have caused the differential wound healing responses. © 2015 Wiley Periodicals, Inc. J Biomed Mater Res Part B: Appl Biomater, 105B: 489-496, 2017.

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PRELP protein inhibits the formation of the complement membrane attack complex.

Cited by 6 publications

References 0 publications

Rsk2 controls synovial fibroblast hyperplasia and the course of arthritis

Rsk2 controls synovial fibroblast hyperplasia and the course of arthritis

Quantitative Mass Spectrometry To Study Inflammatory Cartilage Degradation and Resulting Interactions with the Complement System

Comparative profiling of extractable proteins in extracellular matrices of porcine cholecyst and jejunum intended for preparation of tissue engineering scaffolds

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