Search

Your search keyword '"Roedig, Heiko"' showing total 11 results
Start Over Author "Roedig, Heiko"
11 results on '"Roedig, Heiko"'

3. Biglycan evokes autophagy in macrophages via a novel CD44/Toll-like receptor 4 signaling axis in ischemia/reperfusion injury

Author

Poluzzi, Chiara, Nastase, Madalina-Viviana, Zeng-Brouwers, Jinyang, Roedig, Heiko, Hsieh, Louise Tzung-Harn, Michaelis, Jonas B., Buhl, Eva Miriam, Rezende, Flavia, Manavski, Yosif, Bleich, André, Boor, Peter, Brandes, Ralf P., Pfeilschifter, Josef, Stelzer, Ernst H.K., Münch, Christian, Dikic, Ivan, Brandts, Christian, Iozzo, Renato V., Wygrecka, Malgorzata, and Schaefer, Liliana

Published
2019
Full Text
View/download PDF

5. Affinity Proteomics Identifies Interaction Partners and Defines Novel Insights into the Function of the Adhesion GPCR VLGR1/ADGRV1

Author

Knapp, Barbara, Roedig, Jens, Roedig, Heiko, Krzysko, Jacek, Horn, Nicola, Güler, Baran E., Kusuluri, Deva Krupakar, Yildirim, Adem, Boldt, Karsten, Ueffing, Marius, Liebscher, Ines, Wolfrum, Uwe, Knapp, Barbara, Roedig, Jens, Roedig, Heiko, Krzysko, Jacek, Horn, Nicola, Güler, Baran E., Kusuluri, Deva Krupakar, Yildirim, Adem, Boldt, Karsten, Ueffing, Marius, Liebscher, Ines, and Wolfrum, Uwe

Abstract

The very large G-protein-coupled receptor 1 (VLGR1/ADGRV1) is the largest member of the adhesion G-protein-coupled receptor (ADGR) family. Mutations in VLGR1/ADGRV1 cause human Usher syndrome (USH), a form of hereditary deaf-blindness, and have been additionally linked to epilepsy. In the absence of tangible knowledge of the molecular function and signaling of VLGR1, the pathomechanisms underlying the development of these diseases are still unknown. Our study aimed to identify novel, previously unknown protein networks associated with VLGR1 in order to describe new functional cellular modules of this receptor. Using affinity proteomics, we have identified numerous new potential binding partners and ligands of VLGR1. Tandem affinity purification hits were functionally grouped based on their Gene Ontology terms and associated with functional cellular modules indicative of functions of VLGR1 in transcriptional regulation, splicing, cell cycle regulation, ciliogenesis, cell adhesion, neuronal development, and retinal maintenance. In addition, we validated the identified protein interactions and pathways in vitro and in situ. Our data provided new insights into possible functions of VLGR1, related to the development of USH and epilepsy, and also suggest a possible role in the development of other neuronal diseases such as Alzheimer’s disease.

Published
2022

6. Affinity Proteomics Identifies Interaction Partners and Defines Novel Insights into the Function of the Adhesion GPCR VLGR1/ADGRV1

Author

Knapp, Barbara, primary, Roedig, Jens, additional, Roedig, Heiko, additional, Krzysko, Jacek, additional, Horn, Nicola, additional, Güler, Baran E., additional, Kusuluri, Deva Krupakar, additional, Yildirim, Adem, additional, Boldt, Karsten, additional, Ueffing, Marius, additional, Liebscher, Ines, additional, and Wolfrum, Uwe, additional

Published
2022
Full Text
View/download PDF

10. Biglycan- and Sphingosine Kinase-1 Signaling Crosstalk Regulates the Synthesis of Macrophage Chemoattractants

Author

Hsieh, Louise, primary, Nastase, Madalina-Viviana, additional, Roedig, Heiko, additional, Zeng-Brouwers, Jinyang, additional, Poluzzi, Chiara, additional, Schwalm, Stephanie, additional, Fork, Christian, additional, Tredup, Claudia, additional, Brandes, Ralf, additional, Wygrecka, Malgorzata, additional, Huwiler, Andrea, additional, Pfeilschifter, Josef, additional, and Schaefer, Liliana, additional

Published
2017
Full Text
View/download PDF

11. Small Leucine-Rich Proteoglycans in Renal Inflammation: Two Sides of the Coin

Author

Schaefer, Liliana, Frevert, Charles W., Nastase, Madalina V., Janicova, Andrea, Roedig, Heiko, Hsieh, Louise Tzung-Harn, Wygrecka, Malgorzata, and Schaefer, Liliana

Abstract

It is now well-established that members of the small leucine-rich proteoglycan (SLRP) family act in their soluble form, released proteolytically from the extracellular matrix (ECM), as danger-associated molecular patterns (DAMPs). By interacting with Toll-like receptors (TLRs) and the inflammasome, the two SLRPs, biglycan and decorin, autonomously trigger sterile inflammation. Recent data indicate that these SLRPs, besides their conventional role as pro-inflammatory DAMPs, additionally trigger anti-inflammatory signaling pathways to tightly control inflammation. This is brought about by selective employment of TLRs, their co-receptors, various adaptor molecules, and through crosstalk between SLRP-, reactive oxygen species (ROS)-, and sphingolipid-signaling. In this review, the complexity of SLRP signaling in immune and kidney resident cells and its relevance for renal inflammation is discussed. We propose that the dichotomy in SLRP signaling (pro- and anti-inflammatory) allows for fine-tuning the inflammatory response, which is decisive for the outcome of inflammatory kidney diseases.

Published
2018
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results