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Nettesheim A, Shim MS, Dixon A, et al. Cathepsin B Localizes in the Caveolae and Participates in the Proteolytic Cascade in Trabecular Meshwork Cells. Potential New Drug Target for the Treatment of Glaucoma. J Clin Med. 2020;10(1)doi: 10.3390/jcm10010078.
Nettesheim, A., Shim, M. S., Dixon, A., Raychaudhuri, U., Gong, H., & Liton, P. B. (2020). Cathepsin B Localizes in the Caveolae and Participates in the Proteolytic Cascade in Trabecular Meshwork Cells. Potential New Drug Target for the Treatment of Glaucoma. Journal of clinical medicine, 10(1), . https://doi.org/10.3390/jcm10010078
Nettesheim, April, et al. "Cathepsin B Localizes in the Caveolae and Participates in the Proteolytic Cascade in Trabecular Meshwork Cells. Potential New Drug Target for the Treatment of Glaucoma." Journal of clinical medicine vol. 10,1 (2020). doi: https://doi.org/10.3390/jcm10010078
Nettesheim A, Shim MS, Dixon A, Raychaudhuri U, Gong H, Liton PB. Cathepsin B Localizes in the Caveolae and Participates in the Proteolytic Cascade in Trabecular Meshwork Cells. Potential New Drug Target for the Treatment of Glaucoma. J Clin Med. 2020 Dec 28;10(1). doi: 10.3390/jcm10010078. PMID: 33379277; PMCID: PMC7795952.
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J Clin Med. 2020 Dec 28;10(1). doi: 10.3390/jcm10010078.

Cathepsin B Localizes in the Caveolae and Participates in the Proteolytic Cascade in Trabecular Meshwork Cells. Potential New Drug Target for the Treatment of Glaucoma.

Journal of clinical medicine

April Nettesheim, Myoung Sup Shim, Angela Dixon, Urmimala Raychaudhuri, Haiyan Gong, Paloma B Liton

Affiliations

  1. Department of Ophthalmology & Pathology, Duke University, Durham, NC 27705, USA.
  2. Department of Ophthalmology, Boston University School of Medicine, Boston, MA 02118, USA.

PMID: 33379277 PMCID: PMC7795952 DOI: 10.3390/jcm10010078

Abstract

Extracellular matrix (ECM) deposition in the trabecular meshwork (TM) is one of the hallmarks of glaucoma, a group of human diseases and leading cause of permanent blindness. The molecular mechanisms underlying ECM deposition in the glaucomatous TM are not known, but it is presumed to be a consequence of excessive synthesis of ECM components, decreased proteolytic degradation, or both. Targeting ECM deposition might represent a therapeutic approach to restore outflow facility in glaucoma. Previous work conducted in our laboratory identified the lysosomal enzyme cathepsin B (CTSB) to be expressed on the cellular surface and to be secreted into the culture media in trabecular meshwork (TM) cells. Here, we further investigated the role of CTSB on ECM remodeling and outflow physiology in vitro and in CSTB

Keywords: ECM; PAI-1; TGFβ; cathepsin B; fibrosis; glaucoma; proteolytic cascade; trabecular meshwork

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