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31 results on '"Jiang, Shanya"'

4. Selective In Vitro and Ex Vivo Staining of Brain Neurofibrillary Tangles and Amyloid Plaques by Novel Ethylene Ethynylene-Based Optical Sensors

Author

Monge, Florencia A., primary, Fanni, Adeline M., additional, Donabedian, Patrick L., additional, Hulse, Jonathan, additional, Maphis, Nicole M., additional, Jiang, Shanya, additional, Donaldson, Tia N., additional, Clark, Benjamin J., additional, Whitten, David G., additional, Bhaskar, Kiran, additional, and Chi, Eva Y., additional

Published
2023
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9. Proteopathic tau primes and activates interleukin-1β via myeloid-cell-specific MyD88- and NLRP3-ASC-inflammasome pathway

Author

Jiang, Shanya, primary, Maphis, Nicole M., additional, Binder, Jessica, additional, Chisholm, Devon, additional, Weston, Lea, additional, Duran, Walter, additional, Peterson, Crina, additional, Zimmerman, Amber, additional, Mandell, Michael A., additional, Jett, Stephen D., additional, Bigio, Eileen, additional, Geula, Changiz, additional, Mellios, Nikolaos, additional, Weick, Jason P., additional, Rosenberg, Gary A., additional, Latz, Eicke, additional, Heneka, Michael T., additional, and Bhaskar, Kiran, additional

Published
2021
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14. Proteopathic Tau Primes and Activates Interleukin-1ß(Il-1ß) via MyD88- and NLRP3-ASC-Inflammasome Dependent Pathways

Author

Jiang, Shanya, primary, Maphis, Nicole, additional, Binder, Jessica, additional, Chisholm, Devon, additional, Weston, Lea, additional, Duran, Walter, additional, Floruta, Crina, additional, Zimmerman, Amber, additional, Jett, Stephen, additional, Bigio, Eileen, additional, Geula, Changiz, additional, Mellios, Nikolaos, additional, Weick, Jason, additional, Latz, Eicke, additional, Heneka, Michael, additional, and Bhaskar, Kiran, additional

Published
2019
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15. Protocol to measure apoptosis-associated speck-like protein containing a CARD (ASC) specks in human cerebrospinal fluid via imaging flow-cytometry.

Author

Sánchez, Kathryn E., Jiang, Shanya, Palencia-Desai, Sharina, Thompson, Jeffery, Hobson, Sasha, Rosenberg, Gary A., and Bhaskar, Kiran

Abstract

Apoptosis-associated speck-like protein containing CARD (ASC) specks are elevated in the cerebrospinal fluid (CSF) of Alzheimer’s disease and related dementias (AD/ADRD) patients. Here, we present a flow-cytometry protocol to quantify ASC specks. We describe steps for fluorescently labeling ASC specks using antibody technology, visualizing with imaging flow-cytometry, and gating based on physical characteristics. CSF ASC specks levels positively correlate with phosphorylated tau (Thr181) and negatively correlate with amyloid β ratio (Aβ 42/40) ratio, thus serving as a neuroinflammatory biomarker for diagnosing AD/ADRD.

Published
2024
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18. Cellular and molecular mechanism for secretory autophagy

Author

Kimura, Tomonori, primary, Jia, Jingyue, additional, Claude-Taupin, Aurore, additional, Kumar, Suresh, additional, Choi, Seong Won, additional, Gu, Yuexi, additional, Mudd, Michal, additional, Dupont, Nicolas, additional, Jiang, Shanya, additional, Peters, Ryan, additional, Farzam, Farzin, additional, Jain, Ashish, additional, Lidke, Keith A., additional, Adams, Christopher M., additional, Johansen, Terje, additional, and Deretic, Vojo, additional

Published
2017
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20. DedicatedSNAREs and specializedTRIMcargo receptors mediate secretory autophagy

Author

Kimura, Tomonori, primary, Jia, Jingyue, additional, Kumar, Suresh, additional, Choi, Seong Won, additional, Gu, Yuexi, additional, Mudd, Michal, additional, Dupont, Nicolas, additional, Jiang, Shanya, additional, Peters, Ryan, additional, Farzam, Farzin, additional, Jain, Ashish, additional, Lidke, Keith A, additional, Adams, Christopher M, additional, Johansen, Terje, additional, and Deretic, Vojo, additional

Published
2016
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23. Pharmaceutical screen identifies novel target processes for activation of autophagy with a broad translational potential

Author

Chauhan, Santosh, primary, Ahmed, Zahra, additional, Bradfute, Steven B., additional, Arko-Mensah, John, additional, Mandell, Michael A., additional, Won Choi, Seong, additional, Kimura, Tomonori, additional, Blanchet, Fabien, additional, Waller, Anna, additional, Mudd, Michal H., additional, Jiang, Shanya, additional, Sklar, Larry, additional, Timmins, Graham S., additional, Maphis, Nicole, additional, Bhaskar, Kiran, additional, Piguet, Vincent, additional, and Deretic, Vojo, additional

Published
2015
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24. Dedicated SNAREs and specialized TRIM cargo receptors mediate secretory autophagy.

Author

Kimura, Tomonori, Jia, Jingyue, Kumar, Suresh, Choi, Seong Won, Gu, Yuexi, Mudd, Michal, Dupont, Nicolas, Jiang, Shanya, Peters, Ryan, Farzam, Farzin, Jain, Ashish, Lidke, Keith A, Adams, Christopher M, Johansen, Terje, and Deretic, Vojo

Subjects
AUTOPHAGY, CELL membranes, LYSOSOMES, SYNTAXINS, DOWNREGULATION
Abstract

Autophagy is a process delivering cytoplasmic components to lysosomes for degradation. Autophagy may, however, play a role in unconventional secretion of leaderless cytosolic proteins. How secretory autophagy diverges from degradative autophagy remains unclear. Here we show that in response to lysosomal damage, the prototypical cytosolic secretory autophagy cargo IL-1β is recognized by specialized secretory autophagy cargo receptor TRIM16 and that this receptor interacts with the R- SNARE Sec22b to recruit cargo to the LC3- II+ sequestration membranes. Cargo secretion is unaffected by downregulation of syntaxin 17, a SNARE promoting autophagosome-lysosome fusion and cargo degradation. Instead, Sec22b in combination with plasma membrane syntaxin 3 and syntaxin 4 as well as SNAP-23 and SNAP-29 completes cargo secretion. Thus, secretory autophagy utilizes a specialized cytosolic cargo receptor and a dedicated SNARE system. Other unconventionally secreted cargo, such as ferritin, is secreted via the same pathway. [ABSTRACT FROM AUTHOR]

Published
2017
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29. MOLECULAR MECHANISM OF AUTOPHAGY-BASED UNCONVENTIONAL SECRETION OF IL-1β

Author

Jiang, Shanya and Jiang, Shanya

Abstract

Proteins without signal peptides can still be released into extracellular space via ER/Golgi-independent unconventional secretory pathway(s) that remain to be revealed. A class of leaderless proteins including the pro-inflammatory cytokine interleukin-1β (IL-1β) is processed in the cytosol by proteolytic machineries such as the inflammasome prior to secretion. Studies in yeast uncovered a new unconventional secretory pathway that is dependent on GRASP (Golgi Reassembly and Stacking Protein) and autophagy proteins. The purpose of this work was to determine whether this autophagy-based unconventional secretory pathway (secretory autophagy) is conserved in mammals, how this secretory autophagy differs from the traditional degradative autophagy, and how GRASP intersects with the autophagy pathways. Here, we provide the first evidence that autophagy mediates unconventional secretion of IL-1β in an inflammasome, GRASP55, and Rab8-dependent manner in mouse bone marrow-derived macrophages, a route which also applies to IL-18 and non-inflammasome substrate HMGB1. GRASP55 was also found to be mediating autophagosome formation possibly making secretory autophagosomes. We also give initial insights to the divergence between degradative autophagy and this secretory autophagy pathway, which preferentially utilizes some of the autophagy-related proteins, LC3A, GABARAP, and p62, but not LC3B, NBR1, TBK1, and ULK1. We also discuss the way that GRASP55, the conserved player of unconventional secretion, negatively regulates removal of damaged mitochondria by mitophagy, which might be due to competition between secretory and degradative autophagy. Taken together, these data indicate there is a conserved, unconventional secretory pathway involving GRASP and autophagy. It also suggests that although secretory and degradative autophagy share some core components, secretory autophagy also involves specialized molecular machinery to execute its unconventional secretory function and balance, Biomedical Sciences, Doctoral, University of New Mexico. Biomedical Sciences Graduate Program, Deretic, Vojo, Wilson, Bridget, Prossnitz, Eric, Orlando, Robert

30. Autophagy protects against active tuberculosis by suppressing bacterial burden and inflammation.

Author

Eliseo F. Castillo, Dekonenko, Alexander, Arko-Mensah, John, Mandell, Michael A., Dupont, Nicolas, Jiang, Shanya, Delgado-Vargas, Monica, Timmins, Graham S., Bhattacharya, Dhruva, Hongliang Yang, Hutt, Julie, Lyons, C. Rick, Dobos, Karen M., and Deretic, Vojo

Subjects
AUTOPHAGY, MYCOBACTERIUM tuberculosis, INFLAMMATION, MACROPHAGES, CYTOKINES
Abstract

The article discusses the role of autophagy against active tuberculosis. Study shows that autophagy protects against Mycobacterium tuberculosis (M. tuberculosis) infection and excessive inflammation in vivo. It states that macrophages defective for autophagy secrete proinflammatory cytokines and in a cell-autonomous fashion.

Published
2012
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31. MOLECULAR MECHANISM OF AUTOPHAGY-BASED UNCONVENTIONAL SECRETION OF IL-β

Author

Jiang, Shanya

Subjects
Autophagy, Unconventional Secretion, IL-β
Abstract

Proteins without signal peptides can still be released into extracellular space via ER/Golgi-independent unconventional secretory pathway(s) that remain to be revealed. A class of leaderless proteins including the pro-inflammatory cytokine interleukin-β (IL-β) is processed in the cytosol by proteolytic machineries such as the inflammasome prior to secretion. Studies in yeast uncovered a new unconventional secretory pathway that is dependent on GRASP (Golgi Reassembly and Stacking Protein) and autophagy proteins. The purpose of this work was to determine whether this autophagy-based unconventional secretory pathway (secretory autophagy) is conserved in mammals, how this secretory autophagy differs from the traditional degradative autophagy, and how GRASP intersects with the autophagy pathways. Here, we provide the first evidence that autophagy mediates unconventional secretion of IL-β in an inflammasome, GRASP55, and Rab8-dependent manner in mouse bone marrow-derived macrophages, a route which also applies to IL-18 and non-inflammasome substrate HMGB1. GRASP55 was also found to be mediating autophagosome formation possibly making secretory autophagosomes. We also give initial insights to the divergence between degradative autophagy and this secretory autophagy pathway, which preferentially utilizes some of the autophagy-related proteins, LC3A, GABARAP, and p62, but not LC3B, NBR1, TBK1, and ULK1. We also discuss the way that GRASP55, the conserved player of unconventional secretion, negatively regulates removal of damaged mitochondria by mitophagy, which might be due to competition between secretory and degradative autophagy. Taken together, these data indicate there is a conserved, unconventional secretory pathway involving GRASP and autophagy. It also suggests that although secretory and degradative autophagy share some core components, secretory autophagy also involves specialized molecular machinery to execute its unconventional secretory function and balance with degradative autophagy.

Published
2014

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