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39 results on '"Panwar, Preety"'

2. Extracellular Matrix Remodeling in Atopic Dermatitis Harnesses the Onset of an Asthmatic Phenotype and Is a Potential Contributor to the Atopic March

Author

Graff, Patrick, Woerz, Dana, Wilzopolski, Jenny, Voss, Anne, Sarrazin, Jana, Blimkie, Travis M., Weiner, January, Kershaw, Olivia, Panwar, Preety, Hackett, Tillie, Lau, Susanne, Brömme, Dieter, Beule, Dieter, Lee, Young-Ae, Hancock, Robert E.W., Gruber, Achim D., Bäumer, Wolfgang, and Hedtrich, Sarah

Published
2024
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4. Immune regulatory and anti‐resorptive activities of tanshinone IIA sulfonate attenuates rheumatoid arthritis in mice.

Author

Panwar, Preety, Andrault, Pierre Marie, Saha, Dipon, and Brömme, Dieter

Subjects
*JOINT pain, *T helper cells, *RHEUMATOID arthritis, *AUTOIMMUNE diseases, *DISEASE progression
Abstract

Background and Purpose Experimental Approach Key Results Conclusions Rheumatoid arthritis (RA) is an autoimmune disease characterized by chronic inflammation and painful joint destruction. Current treatments are helpful in RA remission, but strong immunosuppressive activity and patient resistance are clinical issues. This study explores a dual‐action inhibitor, possessing both anti‐inflammatory and anti‐resorptive properties, as a novel treatment for RA.Therapeutic efficacy and mechanisms of ectosteric (tanshinone IIA sulfonate [T06]) and active site‐directed (odanacatib [ODN]) inhibitors of cathepsin K (CatK) were evaluated in RA mouse models. Pathology was assessed through biochemical analyses and histopathological examination. Flow cytometry analysis was performed to characterize immune cells. Anti‐inflammatory effects of T06 on nuclear factor kappa beta (NF‐κB) pathway were studied in macrophages.T06 effectively lowered the number of joint‐resident immune cells, accompanied by significantly reduced production of inflammatory cytokines and collagenolytic proteases. This also included the suppression of Th17 cells and IL‐17, resulting in the reduction of osteoclasts in arthritic joints and amplification of the overall anti‐resorptive effect of T06, which has been attributed to its selective inhibition of the collagenolytic activity of CatK by preventing its oligomerization. The anti‐inflammatory mechanism of T06 was based on blocking the phosphorylation of IκBα in the NF‐κB pathway, resulting in reduced activation and expression of inflammatory cytokines. In contrast, ODN had no effect on inflammation and disease progression and was limited to the inhibition of CatK.The combined anti‐resorptive and anti‐inflammatory activities characterize T06 as a novel therapeutic agent for RA. [ABSTRACT FROM AUTHOR]

Published
2024
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5. Extracellular Matrix Remodeling in Atopic Dermatitis Harnesses the Onset of an Asthmatic Phenotype and Is a Potential Contributor to the Atopic March

Author

Graff, Patrick, primary, Woerz, Dana, additional, Wilzopolski, Jenny, additional, Voss, Anne, additional, Sarrazin, Jana, additional, Blimkie, Travis M., additional, Weiner, January, additional, Kershaw, Olivia, additional, Panwar, Preety, additional, Hackett, Tillie, additional, Lau, Susanne, additional, Brömme, Dieter, additional, Beule, Dieter, additional, Lee, Young-Ae, additional, Hancock, Robert E.W., additional, Gruber, Achim D., additional, Bäumer, Wolfgang, additional, and Hedtrich, Sarah, additional

Published
2023
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11. EXTRACELLULAR MATRIX REMODELING IN ATOPIC DERMATITIS HARNESSES THE ONSET OF AN ASTHMATIC PHENOTYPE AND IS A POTENTIAL CONTRIBUTOR TO THE ATOPIC MARCH

Author

Graff, Patrick, primary, Wilzopolski, Jenny, additional, Voss, Anne, additional, Blimkie, Travis M., additional, Weiner, January, additional, Kershaw, Olivia, additional, Panwar, Preety, additional, Hackett, Tillie, additional, Brömme, Dieter, additional, Loyal, Lucie, additional, Thiel, Andreas, additional, Beule, Dieter, additional, Hancock, Robert E.W., additional, Gruber, Achim D., additional, Bäumer, Wolfgang, additional, and Hedtrich, Sarah, additional

Published
2022
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17. Bone innervation and vascularization regulated by osteoclasts contribute to refractive pain-related behavior in the collagen antibody-induced arthritis model

Author

Rudjito, Resti, primary, Agalave, Nilesh M, additional, Farinotti, Alex Bersellini, additional, Baharpoor, Azar, additional, Martinez Martinez, Arisai, additional, Islas, Enriqueta Muñoz, additional, Panwar, Preety, additional, Brömme, Dieter, additional, Barbier, Julie, additional, Marchand, Fabien, additional, Mehlen, Patrick, additional, Andersen, Thomas Levin, additional, Andrade, Juan Miguel Jimenez, additional, and Svensson, Camilla I., additional

Published
2021
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18. Expression of elastolytic cathepsins in human skin and their involvement in age-dependent elastin degradation

Author

Panwar, Preety, Hedtke, Tobias, Heinz, Andrea, Andrault, Pierre-Marie, Hoehenwarter, Wolfgang, Granville, David J, Schmelzer, Christian E H, Brömme, Dieter, Panwar, Preety, Hedtke, Tobias, Heinz, Andrea, Andrault, Pierre-Marie, Hoehenwarter, Wolfgang, Granville, David J, Schmelzer, Christian E H, and Brömme, Dieter

Abstract

BACKGROUND: Skin ageing is associated with structure-functional changes in the extracellular matrix, which is in part caused by proteolytic degradation. Since cysteine cathepsins are major matrix protein-degrading proteases, we investigated the age-dependent expression of elastolytic cathepsins K, S, and V in human skin, their in vitro impact on the integrity of the elastic fibre network, their cleavage specificities, and the release of bioactive peptides.METHODS: Cathepsin-mediated degradation of human skin elastin samples was assessed from young to very old human donors using immunohistochemical and biochemical assays, scanning electron microscopy, and mass spectrometry.RESULTS: Elastin samples derived from patients between 10 and 86 years of age were analysed and showed an age-dependent deterioration of the fibre structure from a dense network of thinner fibrils into a beaded and porous mesh. Reduced levels of cathepsins K, S, and V were observed in aged skin with a predominant epidermal expression. Cathepsin V was the most potent elastase followed by cathepsin K and S. Biomechanical analysis of degraded elastin fibres corroborated the destructive activity of cathepsins. Mass spectrometric determination of the cleavage sites in elastin revealed that all three cathepsins predominantly cleaved in hydrophobic domains. The degradation of elastin was efficiently inhibited by an ectosteric inhibitor. Furthermore, the degradation of elastin fibres resulted in the release of bioactive peptides, which have previously been associated with various pathologies.CONCLUSION: Cathepsins are powerful elastin-degrading enzymes and capable of generating a multitude of elastokines. They may represent a viable target for intervention strategies to reduce skin ageing.

Published
2020

25. A novel approach to inhibit bone resorption: exosite inhibitors against cathepsin K

Author

Panwar, Preety, Søe, Kent, Guido, Rafael VC, Bueno, Renata V C, Delaisse, Jean-Marie, and Brömme, Dieter

Subjects
Dose-Response Relationship, Drug, Abietanes, Biphenyl Compounds, Cathepsin K, Animals, Humans, Osteoclasts, Cattle, Bone Resorption, Fibroblasts, Research Papers, Protein Structure, Tertiary
Abstract

BACKGROUND AND PURPOSE: Cathepsin K (CatK) is a major drug target for the treatment of osteoporosis. Potent active site-directed inhibitors have been developed and showed variable success in clinical trials. These inhibitors block the entire activity of CatK and thus may interfere with other pathways. The present study investigates the antiresorptive effect of an exosite inhibitor that selectively inhibits only the therapeutically relevant collagenase activity of CatK.EXPERIMENTAL APPROACH: Human osteoclasts and fibroblasts were used to analyse the effect of the exosite inhibitor, ortho-dihydrotanshinone (DHT1), and the active site inhibitor, odanacatib (ODN), on bone resorption and TGF-ß1 degradation. Cell cultures, Western blot, light and scanning electron microscopy as well as energy dispersive X-ray spectroscopy, molecular modelling and enzymatic assays were used to evaluate the inhibitors.KEY RESULTS: DHT1 selectively inhibited the collagenase activity of CatK, without affecting the viability of osteoclasts. Both inhibitors abolished the formation of resorption trenches, with DHT1 having a slightly higher IC50 value than ODN. Maximal reductions of other resorption parameters by DHT1 and ODN were comparable, respectively 41% and 33% for total resorption surface, 46% and 48% for resorption depths, and 83% and 61% for C-terminal telopetide fragment (CTX) release. DHT1 did not affect the turnover of fibrosis-associated TGF-ß1 in fibroblasts, whereas 500 nM ODN was inhibitory.CONCLUSIONS AND IMPLICATIONS: Our study shows that an exosite inhibitor of CatK can specifically block bone resorption without interfering with other pathways.

Published
2015

33. Preparation, characterization, and in vitro release study of albendazole-encapsulated nanosize liposomes

Author

Panwar,Preety, Pandey,Bhumika, Lakhera,P C, Singh,K P, Panwar,Preety, Pandey,Bhumika, Lakhera,P C, and Singh,K P

Abstract

Preety Panwar1, Bhumika Pandey1, P C Lakhera2, K P Singh11Biophysics and Nanotechnology Research Laboratory, CBSH, G.B. Pant University of Agriculture and Technology, Pantnagar, Uttarakhand, India; 2Department of Biotechnology, H.N.B. Garhwal University, Srinagar Garhwal, Uttarakhand, IndiaAbstract: The purpose of the present study was to formulate effective and controlled release albendazole liposomal formulations. Albendazole, a hydrophobic drug used for the treatment of hydatid cysts, was encapsulated in nanosize liposomes. Rapid evaporation method was used for the preparation of albendazole-encapsulated conventional and PEGylated liposomes consisting of egg phosphatidylcholine (PC) and cholesterol (CH) in the molar ratios of (6:4) and PC:CH:polyethylene glycol (PEG) (5:4:1), respectively. In this study, PEGylated and conventional liposomes containing albendazole were prepared and their characteristics, such as particle size, encapsulation efficiency, and in vitro drug release were investigated. The drug encapsulation efficiency of PEGylated and conventional liposomes was 81% and 72%, respectively. The biophysical characterization of both conventional and PEG-coated liposomes were done by transmission electron microscopy and UV-vis spectrophotometry. Efforts were made to study in vitro release of albendazole. The drug release rate showed decrease in albendazole release in descending order: free albendazole, albendazole-loaded conventional liposomes, and least with albendazole-loaded PEG-liposomes. Biologically relevant vesicles were prepared and in vitro release of liposome-entrapped albendazole was determined.Keywords: albendazole, PEGylated, in vitro release, liposomes, nanosize

Published
2010

38. Structural requirements for the collagenase and elastase activity of cathepsin K and its selective inhibition by an exosite inhibitor.

Author

Sharma, Vidhu, Panwar, Preety, O'Donoghue, Anthony J., Cui, Haoran, Guido, Rafael V. C., Cralk, Charles S., and Bromme, Dieter

Subjects
*COLLAGENASES, *ELASTASES, *CATHEPSINS, *TARGETED drug delivery, *BINDING sites, *ENZYME inhibitors
Abstract

Human cathepsin K (CatK) is a major drug target for the treatment of osteoporosis. Although its collagenase activity is unique, CatK also exerts a potent elastolytic activity that is shared with human cathepsins V and S. Other members of the cysteine cathepsin family, which are structurally similar, do not exhibit significant collagen and elastin degrading activities. This raises the question of the presence of specific structural elements, exosites, that are required for these activities. CatK has two exosites that control its collagenolytic and elastolytic activity. Modifications of exosites 1 and 2 block the elastase activity of CatK, whereas only exosite-1 alterations prevent collagenolysis. Neither exosite affects the catalytic activity, protease stability, subsite specificity of CatK or the degradation of other biological substrates by this protease. A low-molecular-mass inhibitor that docks into exosite-1 inhibits the elastase and collagenase activity of CatK without interfering with the degradation of other protein substrates. The identification of CatK exosites opens up the prospect of designing highly potent inhibitors that selectively inhibit the degradation of therapeutically relevant substrates by this multifunctional protease. [ABSTRACT FROM AUTHOR]

Published
2015
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