NDLI: ß-Glucuronidase, a Regulator of Lyme Arthritis Severity, Modulates Lysosomal Trafficking and MMP-9 Secretion in Response to Inflammatory Stimuli.

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ß-Glucuronidase, a Regulator of Lyme Arthritis Severity, Modulates Lysosomal Trafficking and MMP-9 Secretion in Response to Inflammatory Stimuli.

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ß-Glucuronidase, a Regulator of Lyme Arthritis Severity, Modulates Lysosomal Trafficking and MMP-9 Secretion in Response to Inflammatory Stimuli.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Ma, Ying Weis, John H. Weis, Janis J. Mock, Kelton Teuscher, Cory Bramwell, Kenneth K. C.
Description	Author Affiliation: Bramwell KK ( Division of Microbiology and Immunology, Department of Pathology, University of Utah, Salt Lake City, UT 84112); Mock K ( University of Puget Sound, Tacoma, WA 98416); Ma Y ( Division of Microbiology and Immunology, Department of Pathology, University of Utah, Salt Lake City, UT 84112); Weis JH ( Division of Microbiology and Immunology, Department of Pathology, University of Utah, Salt Lake City, UT 84112); Teuscher C ( Department of Medicine, University of Vermont, Burlington, VT 05405.); Weis JJ ( Division of Microbiology and Immunology, Department of Pathology, University of Utah, Salt Lake City, UT 84112)
Abstract	The lysosomal enzyme ß-glucuronidase (Gusb) is a key regulator of Lyme-associated and K/B×N-induced arthritis severity. The luminal enzymes present in lysosomes provide essential catabolic functions for the homeostatic degradation of a variety of macromolecules. In addition to this essential catabolic function, lysosomes play important roles in the inflammatory response following infection. Secretory lysosomes and related vesicles can participate in the inflammatory response through fusion with the plasma membrane and release of bioactive contents into the extracellular milieu. In this study, we show that GUSB hypomorphism potentiates lysosomal exocytosis following inflammatory stimulation. This leads to elevated secretion of lysosomal contents, including glycosaminoglycans, lysosomal hydrolases, and matrix metalloproteinase 9, a known modulator of Lyme arthritis severity. This mechanistic insight led us to test the efficacy of rapamycin, a drug known to suppress lysosomal exocytosis. Both Lyme and K/B×N-associated arthritis were suppressed by this treatment concurrent with reduced lysosomal release.
ISSN	00221767
e-ISSN	15506606
DOI	10.4049/jimmunol.1500212
Journal	The Journal of Immunology
Issue Number	4
Volume Number	195
Language	English
Publisher	The American Association of Immunologists
Publisher Date	2015-08-15
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Glucuronidase Metabolism Lyme Disease Lysosomes Matrix Metalloproteinase 9 Animals Cell Membrane Disease Models, Animal Exocytosis Drug Effects Immunology Deficiency Genetics Immunosuppressive Agents Pharmacology Drug Therapy Pathology Lysosomal-associated Membrane Protein 1 Macrophages Ultrastructure Mice Mice, Knockout Models, Biological Protein Transport Sirolimus Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't Discipline Immunology
Content Type	Text
Resource Type	Article
Subject	Immunology and Allergy Immunology

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