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Article: Akt Protein Kinase, miR-200/miR-182 Expression and Epithelial-Mesenchymal Transition Proteins in Hibernating Ground Squirrels.

Lee, Yang-Ja / Bernstock, Joshua D / Klimanis, Dace / Hallenbeck, John M

2018 Volume 11, Page(s) 22

Abstract: Hibernating 13-lined ground squirrels ( ...

Abstract	Hibernating 13-lined ground squirrels (
Language	English
Publishing date	2018-01-30
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2452967-9
ISSN	1662-5099
ISSN	1662-5099
DOI	10.3389/fnmol.2018.00022
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Article ; Online: SUMO and ischemic tolerance.

Lee, Yang-ja / Hallenbeck, John M

Neuromolecular medicine

2013 Volume 15, Issue 4, Page(s) 771–781

Abstract: Hibernating squirrels slow blood flow to a crawl, but sustain no damage to brain or other tissues. This phenomenon provides an excellent model of natural tolerance to ischemia. Small ubiquitin-like modifier (SUMO) is a 100-residue peptide that modifies ... ...

Abstract	Hibernating squirrels slow blood flow to a crawl, but sustain no damage to brain or other tissues. This phenomenon provides an excellent model of natural tolerance to ischemia. Small ubiquitin-like modifier (SUMO) is a 100-residue peptide that modifies other proteins by being attached to the epsilon amino group of specific lysine residues. The discovery of massive SUMOylation (by both SUMO-1 and SUMO-2/3) occurring in the brains of 13-lined ground squirrels (Ictidomys tridecemlineatus) during hibernation torpor had opened the door to the studies on SUMO and ischemic tolerance reviewed here. Ischemic stress was shown to increase the levels of SUMO conjugation, especially SUMO-2/3, mostly during reperfusion in animal models and during restoration of oxygen and glucose in cell culture systems. Over-expression or depletion of SUMOs and/or Ubc9 (the SUMO E2 conjugating enzyme) increases or decreases (respectively) the levels of SUMO conjugates. Elevated global SUMO conjugations were shown to cytoprotect from ischemic insults; conversely, depressed SUMOylation sensitized cells. Global protein conjugation not only by SUMOs, but also by other ubiquitin-like modifiers (ULMs) including NEDD8, ISG15, UFM1 and FUB1 was shown to be significantly increased in the brains of hibernating ground squirrels during torpor. These increases in multiple ULM conjugations may orchestrate the cellular events in hibernating ground squirrels that induce a state of natural tolerance through their multipronged effects. Certain miRNAs such as the miR-200 family and the miR-182 family were shown, at least partly, to control the levels of these ULM conjugations. Lowering the levels of these miRNAs leads to an increase in global SUMOylation/ULM conjugation, thereby providing the tolerance to ischemia. This suggests that these miRNAs may be good targets for therapeutic intervention in stroke.
MeSH term(s)	Animals ; Brain Ischemia/physiopathology ; Cells, Cultured ; Cysteine Endopeptidases/physiology ; Disease Models, Animal ; Glucose/metabolism ; Hibernation/physiology ; Humans ; Hypothermia/physiopathology ; Hypothermia, Induced ; Ischemia/physiopathology ; Mice ; Mice, Transgenic ; MicroRNAs/physiology ; Models, Animal ; Nerve Tissue Proteins/physiology ; Neurons/metabolism ; Oxidative Stress ; Rats ; Reperfusion Injury/physiopathology ; Reperfusion Injury/prevention & control ; Sciuridae/physiology ; Small Ubiquitin-Related Modifier Proteins/physiology ; Sumoylation/physiology ; Ubiquitin/metabolism ; Ubiquitin-Conjugating Enzymes/genetics ; Ubiquitin-Conjugating Enzymes/physiology ; Ubiquitins/physiology
Chemical Substances	MicroRNAs ; Nerve Tissue Proteins ; Small Ubiquitin-Related Modifier Proteins ; Ubiquitin ; Ubiquitins ; Ubiquitin-Conjugating Enzymes (EC 2.3.2.23) ; Cysteine Endopeptidases (EC 3.4.22.-) ; ubiquitin-conjugating enzyme UBC9 (EC 6.3.2.-) ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2013-06-18
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Review
ZDB-ID	2077809-0
ISSN	1559-1174 ; 1535-1084
ISSN (online)	1559-1174
ISSN	1535-1084
DOI	10.1007/s12017-013-8239-9
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Article ; Online: Global protein conjugation by ubiquitin-like-modifiers during ischemic stress is regulated by microRNAs and confers robust tolerance to ischemia.

Lee, Yang-ja / Johnson, Kory R / Hallenbeck, John M

PloS one

2012 Volume 7, Issue 10, Page(s) e47787

Abstract: Hibernation torpor provides an excellent model of natural tolerance to ischemia. We have previously shown that massive global SUMOylation occurs during hibernation torpor in ground squirrels. We have also shown that overexpression of Ubc9, SUMO-1, or ... ...

Abstract	Hibernation torpor provides an excellent model of natural tolerance to ischemia. We have previously shown that massive global SUMOylation occurs during hibernation torpor in ground squirrels. We have also shown that overexpression of Ubc9, SUMO-1, or SUMO-2/3 provides protection against ischemic damage in cell lines and cortical neurons exposed to oxygen/glucose deprivation, and in mice exposed to middle cerebral artery occlusion. We have now extended our study to other Ubiquitin-Like-Modifiers (ULMs), which have multiple cellular functions during stress, in order to assess the possibility that they also have roles in tolerance to ischemia. We found that not only SUMO conjugation, but also global protein conjugation by other ULMs including NEDD8, ISG15, UFM1 and FUB1 were significantly increased in the brains of hibernating ground squirrels during torpor. By means of miRNA microarrays of ground squirrel brain samples (from active and torpor phase) we found that the miR-200 family (miR-200a,b,c/miR-141/miR-429) and the miR-182 family (miR-182/miR-183/miR-96) were among the most consistently depressed miRNAs in the brain during the torpor phase as compared to active animals. In addition, we showed that these miRNAs are involved in the expression of various ULM proteins and their global conjugation to proteins. We observed that inhibition of the miR-200 family and/or miR-182 family miRNA activities in SHSY5Y cells increases global protein conjugation by the above ULMs and makes these cells more tolerant to OGD-induced cell death. This is the first report to describe that the natural tolerance to brain ischemia in hibernators is linked to regulation by microRNAs of a broad range of ubiquitin-like modifiers.
MeSH term(s)	Animals ; Brain/metabolism ; Brain Ischemia/genetics ; Brain Ischemia/metabolism ; Brain Ischemia/pathology ; Cell Line ; Female ; Gene Expression Regulation ; Glucose/deficiency ; Hibernation/physiology ; Male ; MicroRNAs/genetics ; MicroRNAs/metabolism ; Models, Biological ; Oxygen/metabolism ; Sciuridae/genetics ; Sciuridae/metabolism ; Small Ubiquitin-Related Modifier Proteins/genetics ; Small Ubiquitin-Related Modifier Proteins/metabolism ; Sumoylation ; Ubiquitin-Conjugating Enzymes/genetics ; Ubiquitin-Conjugating Enzymes/metabolism
Chemical Substances	MicroRNAs ; Small Ubiquitin-Related Modifier Proteins ; Ubiquitin-Conjugating Enzymes (EC 2.3.2.23) ; ubiquitin-conjugating enzyme UBC9 (EC 6.3.2.-) ; Glucose (IY9XDZ35W2) ; Oxygen (S88TT14065)
Language	English
Publishing date	2012-10-18
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0047787
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Article ; Online: Global SUMOylation facilitates the multimodal neuroprotection afforded by quercetin against the deleterious effects of oxygen/glucose deprivation and the restoration of oxygen/glucose.

Lee, Yang-Ja / Bernstock, Joshua D / Nagaraja, Nandakumar / Ko, Brian / Hallenbeck, John M

Journal of neurochemistry

2016 Volume 138, Issue 1, Page(s) 101–116

Abstract: The putative neuroprotective properties of various flavonoids have long been reported. Among this class of chemicals, quercetin, a major flavone/flavonol naturally occurring in plants, deserves focused attention because of the myriad of beneficial ... ...

Abstract	The putative neuroprotective properties of various flavonoids have long been reported. Among this class of chemicals, quercetin, a major flavone/flavonol naturally occurring in plants, deserves focused attention because of the myriad of beneficial effects observed in various in vitro and in vivo models of central nervous system damage/degeneration. However, the mechanisms governing the beneficial outcomes mediated by quercetin remain to be elucidated. In an effort to define the underlying molecular mechanisms, our study employed human/rat neuroblastoma cell lines (SHSY5Y and B35, respectively) and E18-derived rat primary cortical neurons upon which the effects of various flavonoids were examined. Of note, increases in the levels of global SUMOylation, a post-translational modification with the Small Ubiquitin-like MOdifier (SUMO) were pronounced. Quercetin treatment increased SUMOylation levels in both SHSY5Y cells and rat cortical neurons in a dose and time-dependent manner, possibly via the direct inactivation of certain SENPs (SUMO-specific isopeptidases). Of particular interest, cells treated with quercetin displayed increased tolerance to oxygen/glucose deprivation exposure, an in vitro model of ischemia. SHSY5Y cells treated with quercetin also increased the expression of Nrf2 (via a decrease in the levels of Keap1), heme oxygenase-1 (HO-1), and nitric oxide synthase 1 (NOS1), which provide further protection from oxidative stress. In addition, the increased SUMOylation of HIF-1α was noted and deemed to be significant. We hypothesize that SUMOylated HIF-1α plays a fundamental role in the protection afforded and may underlie some of quercetin's ability to protect cells from oxygen/glucose deprivation-induced cell death, via an up-regulation of HO-1 and NOS1, which ultimately leads to the induction of pro-life NOS1/protein kinase G signaling. Quercetin acts to increase survival in the face of ischemia via an increase of SENP3 expression, the possible inactivation of SENPs 1/2, and via a decrease in KEAP1 levels (thereby increasing Nrf2 stability). These changes may then lead to increase in HIF-1α SUMOylation and HO-1 activation, followed by an up-regulation of NOS1/PKG signaling. Pathways altered via quercetin treatment within our experimental system are represented by blue arrowheads. Solid black arrows represent relationships that have been explored while a dotted arrow represents a relationship that has yet to be confirmed.
MeSH term(s)	Animals ; Cell Death/drug effects ; Cell Hypoxia/drug effects ; Cell Line, Tumor ; Cells, Cultured ; Cerebral Cortex/cytology ; Female ; Glucose/deficiency ; Humans ; Hypoxia/drug therapy ; L-Lactate Dehydrogenase/metabolism ; Neuroblastoma/pathology ; Neurons/drug effects ; Neuroprotective Agents/pharmacology ; Pregnancy ; Quercetin/pharmacology ; RNA, Small Interfering/genetics ; RNA, Small Interfering/metabolism ; Rats ; Rats, Sprague-Dawley ; Small Ubiquitin-Related Modifier Proteins/metabolism ; Sumoylation/drug effects ; Up-Regulation/drug effects
Chemical Substances	Neuroprotective Agents ; RNA, Small Interfering ; Small Ubiquitin-Related Modifier Proteins ; Quercetin (9IKM0I5T1E) ; L-Lactate Dehydrogenase (EC 1.1.1.27) ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2016-06-06
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	80158-6
ISSN	1471-4159 ; 0022-3042 ; 1474-1644
ISSN (online)	1471-4159
ISSN	0022-3042 ; 1474-1644
DOI	10.1111/jnc.13643
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Article: Drugging SUMOylation for neuroprotection and oncotherapy.

Bernstock, Joshua D / Ye, Daniel G / Lee, Yang-Ja / Gessler, Florian / Friedman, Gregory K / Zheng, Wei / Hallenbeck, John M

Neural regeneration research

2018 Volume 13, Issue 3, Page(s) 415–416

Language	English
Publishing date	2018-05-21
Publishing country	India
Document type	Journal Article
ZDB-ID	2388460-5
ISSN	1876-7958 ; 1673-5374
ISSN (online)	1876-7958
ISSN	1673-5374
DOI	10.4103/1673-5374.228718
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Article ; Online: SUMOylation in brain ischemia: Patterns, targets, and translational implications.

Bernstock, Joshua D / Yang, Wei / Ye, Daniel G / Shen, Yuntian / Pluchino, Stefano / Lee, Yang-Ja / Hallenbeck, John M / Paschen, Wulf

Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism

2017 Volume 38, Issue 1, Page(s) 5–16

Abstract: Post-translational protein modification by small ubiquitin-like modifier (SUMO) regulates a myriad of homeostatic and stress responses. The SUMOylation pathway has been extensively studied in brain ischemia. Convincing evidence is now at hand to support ... ...

Abstract	Post-translational protein modification by small ubiquitin-like modifier (SUMO) regulates a myriad of homeostatic and stress responses. The SUMOylation pathway has been extensively studied in brain ischemia. Convincing evidence is now at hand to support the notion that a major increase in levels of SUMOylated proteins is capable of inducing tolerance to ischemic stress. Therefore, the SUMOylation pathway has emerged as a promising therapeutic target for neuroprotection in the face of brain ischemia. Despite this, it is prudent to acknowledge that there are many key questions still to be addressed in brain ischemia related to SUMOylation. Accordingly, herein, we provide a critical review of literature within the field to summarize current knowledge and in so doing highlight pertinent translational implications of the SUMOylation pathway in brain ischemia.
MeSH term(s)	Brain Ischemia/metabolism ; Humans ; Neuroprotection/physiology ; Sumoylation/physiology
Language	English
Publishing date	2017-11-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	604628-9
ISSN	1559-7016 ; 0271-678X
ISSN (online)	1559-7016
ISSN	0271-678X
DOI	10.1177/0271678X17742260
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Article ; Online: A method for hypothermia-induction and maintenance allows precise body and brain temperature control in mice.

Mou, Yongshan / Wilgenburg, Brian J / Lee, Yang-ja / Hallenbeck, John M

Journal of neuroscience methods

2012 Volume 213, Issue 1, Page(s) 1–5

Abstract: The benefits as well as mechanisms of hypothermia in brain injuries are actively studied at the bench and in the clinic. However, methods used in controlling hypothermia vary among laboratories, and usually brain temperatures are not monitored directly ... ...

Abstract	The benefits as well as mechanisms of hypothermia in brain injuries are actively studied at the bench and in the clinic. However, methods used in controlling hypothermia vary among laboratories, and usually brain temperatures are not monitored directly in animals due to the need for an invasive procedure. Here we show a method, water immersion technique, which we developed recently to regulate body temperature in mice during hypothermia process. This method significantly reduced the temperature variation around target temperature. Importantly, this method demonstrated a parallel and consistent relationship between rectal temperature and brain temperature (the brain temperature was consistently 0.5C higher than rectal temperature) throughout hypothermia maintenance. This technique may be well adapted to hypothermia studies in mice and other rodents, especially to the assessment and regulation of brain temperature during studies.
MeSH term(s)	Anesthesia ; Animals ; Body Temperature/physiology ; Brain/physiology ; Female ; Hypothermia, Induced/methods ; Ice ; Immersion ; Male ; Mice ; Rectum/physiology
Chemical Substances	Ice
Language	English
Publishing date	2012-11-19
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	282721-9
ISSN	1872-678X ; 0165-0270
ISSN (online)	1872-678X
ISSN	0165-0270
DOI	10.1016/j.jneumeth.2012.11.006
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Article: Global SUMOylation is a molecular mechanism underlying hypothermia-induced ischemic tolerance.

Lee, Yang-Ja / Mou, Yongshan / Klimanis, Dace / Bernstock, Joshua D / Hallenbeck, John M

Frontiers in cellular neuroscience

2014 Volume 8, Page(s) 416

Abstract: The molecular mechanisms underlying hypothermic neuroprotection have yet to be fully elucidated. Herein we demonstrate that global SUMOylation, a form of post-translational modification with the Small Ubiquitin-like MOdifer, participates in the ... ...

Abstract	The molecular mechanisms underlying hypothermic neuroprotection have yet to be fully elucidated. Herein we demonstrate that global SUMOylation, a form of post-translational modification with the Small Ubiquitin-like MOdifer, participates in the multimodal molecular induction of hypothermia-induced ischemic tolerance. Mild (32°C) to moderate (28°C) hypothermic treatment(s) during OGD (oxygen-glucose-deprivation) or ROG (restoration of oxygen/glucose) increased global SUMO-conjugation levels and protected cells (both SHSY5Y and E18 rat cortical neurons) from OGD and ROG-induced cell death. Hypothermic exposure either before or after permanent middle cerebral artery occlusion (pMCAO) surgery in wild type mice increased global SUMO-conjugation levels in the brain and in so doing protected these animals from pMCAO-induced ischemic damage. Of note, hypothermic exposure did not provide an additional increase in protection from pMCAO-induced ischemic brain damage in Ubc9 transgenic (Ubc9 Tg) mice, which overexpress the sole E2 SUMO conjugating enzyme and thereby display elevated basal levels of global SUMOylation under normothermic conditions. Such evidence suggests that increases in global SUMOylation are critical and may account for a substantial part of the observed increase in cellular tolerance to brain ischemia caused via hypothermia.
Language	English
Publishing date	2014-12-04
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2452963-1
ISSN	1662-5102
ISSN	1662-5102
DOI	10.3389/fncel.2014.00416
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Article: Cerebral Ischemia Increases Small Ubiquitin-Like Modifier Conjugation within Human Penumbral Tissue: Radiological-Pathological Correlation.

Bernstock, Joshua D / Ye, Daniel G / Griffin, Allison / Lee, Yang-Ja / Lynch, John / Latour, Lawrence L / Friedman, Gregory K / Maric, Dragan / Hallenbeck, John M

Frontiers in neurology

2018 Volume 8, Page(s) 738

Abstract: Posttranslational modification by small ubiquitin-like modifier (SUMO) regulates myriad physiological processes within cells and has been demonstrated to be highly activated in murine brains after cerebral ischemia. ... ...

Abstract	Posttranslational modification by small ubiquitin-like modifier (SUMO) regulates myriad physiological processes within cells and has been demonstrated to be highly activated in murine brains after cerebral ischemia. Numerous
Language	English
Publishing date	2018-01-12
Publishing country	Switzerland
Document type	Case Reports
ZDB-ID	2564214-5
ISSN	1664-2295
ISSN	1664-2295
DOI	10.3389/fneur.2017.00738
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Article ; Online: Quantitative high-throughput screening identifies cytoprotective molecules that enhance SUMO conjugation via the inhibition of SUMO-specific protease (SENP)2.

Bernstock, Joshua D / Ye, Daniel / Smith, Jayden A / Lee, Yang-Ja / Gessler, Florian A / Yasgar, Adam / Kouznetsova, Jennifer / Jadhav, Ajit / Wang, Zhuoran / Pluchino, Stefano / Zheng, Wei / Simeonov, Anton / Hallenbeck, John M / Yang, Wei

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

2018 Volume 32, Issue 3, Page(s) 1677–1691

Abstract: The development of novel neuroprotective treatments for acute stroke has been fraught with failures, which supports the view of ischemic brain damage as a highly complex multifactorial process. Post-translational modifications such as small ubiquitin- ... ...

Abstract	The development of novel neuroprotective treatments for acute stroke has been fraught with failures, which supports the view of ischemic brain damage as a highly complex multifactorial process. Post-translational modifications such as small ubiquitin-like modifier (SUMO)ylation have emerged as critical molecular regulatory mechanisms in states of both homeostasis and ischemic stress, as evidenced by our previous work. Accordingly, the clinical significance of the selective control of the global SUMOylation process has become apparent in studies of ischemic pathobiology and pathophysiology. Herein, we describe a process capable of identifying and characterizing small molecules with the potential of targeting the SUMO system through inhibition of SUMO deconjugation in an effort to develop novel stroke therapies.-Bernstock, J. D., Ye, D., Smith, J. A., Lee, Y.-J., Gessler, F. A., Yasgar, A., Kouznetsova, J., Jadhav, A., Wang, Z., Pluchino, S., Zheng, W., Simeonov, A., Hallenbeck, J. M., Yang, W. Quantitative high-throughput screening identifies cytoprotective molecules that enhance SUMO-conjugation via the inhibition of SUMO-specific protease (SENP)2.
MeSH term(s)	Adaptor Proteins, Signal Transducing/antagonists & inhibitors ; Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Cell Line, Transformed ; Cysteine Endopeptidases/genetics ; Cysteine Endopeptidases/metabolism ; Humans ; Protease Inhibitors/pharmacology ; Rats ; SUMO-1 Protein/genetics ; SUMO-1 Protein/metabolism ; Stroke/drug therapy ; Stroke/genetics ; Stroke/metabolism ; Stroke/pathology ; Sumoylation
Chemical Substances	Adaptor Proteins, Signal Transducing ; Protease Inhibitors ; SUMO-1 Protein ; Senp2 protein, rat ; Cysteine Endopeptidases (EC 3.4.22.-) ; SENP2 protein, human (EC 3.4.22.-)
Language	English
Publishing date	2018-01-03
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
ZDB-ID	639186-2
ISSN	1530-6860 ; 0892-6638
ISSN (online)	1530-6860
ISSN	0892-6638
DOI	10.1096/fj.201700711R
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