Search

Your search keyword '"Fan, Peidong"' showing total 112 results
Start Over Author "Fan, Peidong"
112 results on '"Fan, Peidong"'

15. Adenosine A2a blockade prevents synergy between [mu]-opiate and cannabinoid CB1 receptors and eliminates heroin-seeking behavior in addicted rats

Author

Yao, Lina, McFarland, Krista, Fan, Peidong, Jiang, Zhan, Ueda, Takashi, and Diamond, Ivan

Subjects
Adenosine -- Research, Opium -- Research, Science and technology
Abstract

Relapse is the most serious limitation of effective medical treatment of opiate addiction. Opiate-related behaviors appear to be modulated by cannabinoid CB1 receptors (CB1) through poorly understood cross-talk mechanisms. Opiate and CB1 receptors are coexpressed in the nucleus accumbens (NAc) and dorsal striatum. These regions also have the highest density of adenosine [A.sub.2A] receptors ([A.sub.2A]) in the brain. We have been investigating the postsynaptic signaling mechanisms of/[micro]-opiate receptors (MORs) and CB1 receptors in primary NAc/striatal neurons. In this article, we present evidence that MOR and CB1 act synergistically on cAMP/PKA signaling in NAc/striatal neurons. In addition, we find that synergy requires adenosine and [A.sub.2A]. Importantly, an [A.sub.2A] antagonist administered either directly into the NAc or indirectly by i.p. injection eliminates heroin-induced reinstatement in rats trained to self-administer heroin, a model of human craving and relapse. These findings suggest that [A.sub.2A] antagonists might be effective therapeutic agents in the management of abstinent heroin addicts. PKA | addiction | nucleus accumbens | gene activation

Published
2006

16. Addicting drugs utilize a synergistic molecular mechanism in common requiring adenosine and Gi-[beta][gamma] dimers

Author

Yao, Lina, Fan, Peidong, Jiang, Zhan, Mailliard, William S., Gordon, Adrienne S., and Diamond, Ivan

Subjects
Narcotics -- Research, Protein kinases -- Research, Science and technology
Abstract

The mesolimbic dopamine system and cAMP-dependent/protein kinase A (PKA) pathways are strongly implicated in addictive behaviors. Here we determine the role of dopamine D2 receptors (D2) in PKA signaling responses to [delta]-opioid (DOR) and cannabinoid (CB1) receptors. We find in NG108-15/D2 cells and in cultured primary neurons that a brief exposure to saturating concentrations of DOR and CB1 agonists increases cAMP, promotes PKA C[delta] translocation and increases cAMP-dependent gene expression. Activation of PKA signaling is mediated by Gi-/[beta][gamma] dimers. Importantly, subthreshold concentrations of DOR or CB1 agonists with D2 agonists, which ate without effect when added separately, together activate cAMP/PKA signaling synergistically. There is also synergy between DOR of CB1 with ethanol, another addicting agent. In all instances, synergy requires adenosine activation of adenosine A2 receptors and is mediated by [beta][gamma] dimers. Synergy by this molecular mechanism appears to confer hypersensitivity to opioids and cannabinoids while simultaneously increasing the sensitivity of D2 signaling when receptors are expressed on the same cells. This mechanism may account, in part, for drug-induced activation of medium spiny neurons in the nucleus accumbens.

Published
2003

17. Betagamma dimers mediate synergy of dopamine D2 and adenosine A2 receptor-stimulated PKA signaling and regulate ethanol consumption

Author

Yao, Lina, Arolfo, Maria Pia, Dohrman, Douglas P., Jiang, Zhan, Fan, Peidong, Fuchs, Sara, Janak, Patricia H., Gordon, Adrienne S., and Diamond, Ivan

Subjects
Dopamine receptors -- Genetic aspects, Cellular signal transduction -- Analysis, Protein kinases -- Analysis, Genetic transcription -- Regulation, Biological sciences
Abstract

Results show that the dopamine-D2 receptor agonist NPA enhances cAMP concentration causing translocation of PKA C-alpha leading to increases CRE-mediated gene expression. Further, the NPA and ethanol synergistically induce PKC C-alpha translocation with free betagamma subunits of the G proteins meidating the synergistic response reducing alcohol consumption by rats.

Published
2002

20. Discovery of Potent and Selective MTH1 Inhibitors for Oncology: Enabling Rapid Target (In)Validation

Author

Farand, Julie, primary, Kropf, Jeffrey E., additional, Blomgren, Peter, additional, Xu, Jianjun, additional, Schmitt, Aaron C., additional, Newby, Zachary E., additional, Wang, Ting, additional, Murakami, Eisuke, additional, Barauskas, Ona, additional, Sudhamsu, Jawahar, additional, Feng, Joy Y., additional, Niedziela-Majka, Anita, additional, Schultz, Brian E., additional, Schwartz, Karen, additional, Viatchenko-Karpinski, Serge, additional, Kornyeyev, Dmytro, additional, Kashishian, Adam, additional, Fan, Peidong, additional, Chen, Xiaowu, additional, Lansdon, Eric B., additional, Ports, Michael O., additional, Currie, Kevin S., additional, Watkins, William J., additional, and Notte, Gregory T., additional

Published
2019
Full Text
View/download PDF

27. Targeting LOXL2 for cardiac interstitial fibrosis and heart failure treatment

Author

Yang, Jin, primary, Savvatis, Konstantinos, additional, Kang, Jong Seok, additional, Fan, Peidong, additional, Zhong, Hongyan, additional, Schwartz, Karen, additional, Barry, Vivian, additional, Mikels-Vigdal, Amanda, additional, Karpinski, Serge, additional, Kornyeyev, Dmytro, additional, Adamkewicz, Joanne, additional, Feng, Xuhui, additional, Zhou, Qiong, additional, Shang, Ching, additional, Kumar, Praveen, additional, Phan, Dillon, additional, Kasner, Mario, additional, López, Begoña, additional, Diez, Javier, additional, Wright, Keith C., additional, Kovacs, Roxanne L., additional, Chen, Peng-Sheng, additional, Quertermous, Thomas, additional, Smith, Victoria, additional, Yao, Lina, additional, Tschöpe, Carsten, additional, and Chang, Ching-Pin, additional

Published
2016
Full Text
View/download PDF

29. Dominant negative down-regulation of endotoxin-induced tumor necrosis factor [Alpha] production by [Lps.sup.d]/Ran

Author

Yuan, Quan, Zhao, Fangping, Chung, Siu-Wah, Fan, Peidong, Sultzer, Barnet M., Kan, Y. W., and Wong, Peter M. C.

Subjects
Septic shock -- Analysis, Tumor necrosis factor -- Measurement, Genetic engineering -- Research, DNA damage -- Analysis, Science and technology
Abstract

We recently showed that adenoviral transfer and expression of the [Lps.sup.d]/Ran gene isolated from endotoxin-resistant C3H/HeJ mice could protect endotoxin-sensitive mice from endotoxic shock. Elevation of proinflammatory cytokines, such as tumor necrosis factor [Alpha] (TNF-[Alpha]), is thought to be essential for the development of septic shock. To investigate the extent to which [Lps.sup.d]/Ran affects TNF-[Alpha] production, we transduced primary macrophages from endotoxin-sensitive and -resistant mice with adenoviral vectors expressing the wild-type and the mutant Lps/Ran cDNAs and other control genes, and compared the amount of TNF-[Alpha] produced by these various transduced macrophages. Successful transfer and expression of [Lps.sup.d]/Ran cDNA in endotoxin-sensitive C3H/HeOuJ macrophages reduced TNF-[Alpha] production upon lipopolysaccharide (LPS) stimulation, as compared with macrophages transduced with vectors expressing the wild-type [Lps.sup.n]/Ran cDNA, the green fluorescent protein gene, or the lacZ gene. On the other hand, successful transfer and expression of the wild-type [Lps.sup.n]/Ran cDNA in primary macrophages from endotoxin-resistant C3H/HeJ mice failed to induce TNF-[Alpha] production to any significant extent unless a very high LPS concentration was used. Given our previous demonstration that [Lps.sup.n]/Ran functions effectively in restoring LPS responsiveness in B cells from C3H/HeJ mice, we conclude that Lps/Ran is involved in a CD14-independent signal transduction pathway. This dominant negative down-regulation by [Lps.sup.d]/Ran on TNF-[Alpha] production by macrophages and probably other innate immune responses may be key to the development of an effective gene therapy for endotoxic or septic shock. gene therapy | septic shock | Ran GTPase | adenovirus

Published
2000

30. [Lps.sup.d]/Ran of endotoxin-resistant C3H/HeJ mice is defective in mediating lipopolysaccharide endotoxin responses

Author

WONG, PETER M. C., KANG, ANTHONY, CHEN, HONG, YUAN, QUAN, FAN, PEIDONG, SULTZER, BARNET M., KAN, YUET WAI, and CHUNG, SIU-WAH

Subjects
Endotoxins -- Physiological aspects, Genetic markers -- Analysis, Adenoviruses -- Research, Cellular recognition -- Research, Science and technology
Abstract

C3H/HeJ inbred mice are defective in that they are highly resistant to endotoxic shock as compared with normal responder mice. Their B cells and macrophages do not respond significantly when exposed to lipopolysaccharide (LPS), whereas cells from the responder mice do. Using a functional assay, we previously isolated a cDNA, which encodes for Ran/TC4 GTPase. We now show that this gene is mutated in C3H/HeJ mice, which accounts for their resistance to endotoxin stimulation. Sequence analysis of independent mutant [Lps.sup.d]/Ran cDNAs isolated from splenic B cells of C3H/HeJ mice reveals a consistent single base substitution at position 870, where a thymidine is replaced with a cytidine. In situ hybridization maps the [Lps.sup.d]/Ran cDNA to mouse chromosome 4. By retroviral gene transfer, the wild-type [Lps.sup.n]/Ran cDNA but not the mutant [Lps.sup.d]/Ran cDNA can restore LPS responsiveness of C3H/HeJ cells. Adenoviral gene transfer in vivo with the mutant [Lps.sup.d]/Ran cDNA but not the wild-type [Lps.sup.n]/Ran cDNA rescues endotoxin-sensitive mice from septic shock. Thus Lps/Ran is an important target for LPS-mediated signal transduction, and the [Lps.sup.d]/Ran gene may be useful as a therapeutic sequence in gene therapy for endotoxemia and septic shock.

Published
1999

32. Thioredoxin-2 Inhibits Mitochondrial Reactive Oxygen Species Generation and Apoptosis Stress Kinase-1 Activity to Maintain Cardiac Function

Author

Huang, Qunhua, primary, Zhou, Huanjiao Jenny, additional, Zhang, Haifeng, additional, Huang, Yan, additional, Hinojosa-Kirschenbaum, Ford, additional, Fan, Peidong, additional, Yao, Lina, additional, Belardinelli, Luiz, additional, Tellides, George, additional, Giordano, Frank J., additional, Budas, Grant R., additional, and Min, Wang, additional

Published
2015
Full Text
View/download PDF

33. Intracellular Na+ overload causes oxidation of CaMKII and leads to Ca2+ mishandling in isolated ventricular myocytes

Author

Viatchenko-Karpinski, Serge, primary, Kornyeyev, Dmytro, additional, El-Bizri, Nesrine, additional, Budas, Grant, additional, Fan, Peidong, additional, Jiang, Zhan, additional, Yang, Jin, additional, Anderson, Mark E., additional, Shryock, John C., additional, Chang, Ching-Pin, additional, Belardinelli, Luiz, additional, and Yao, Lina, additional

Published
2014
Full Text
View/download PDF

34. Dopamine and Ethanol Cause Translocation of εPKC Associated with εRACK: Cross-talk Between PKA and PKC Signaling Pathways

Author

Yao, Lina, Fan, Peidong, Jiang, Zhan, Gordon, Adrienne, Mochly-Rosen, Daria, and Diamond, Ivan

Subjects
Time Factors, Ethanol, Dopamine, Receptors, Cell Surface, Protein Kinase C-epsilon, Receptors for Activated C Kinase, Cyclic AMP-Dependent Protein Kinases, Models, Biological, Article, Rats, Enzyme Activation, Protein Transport, Type C Phospholipases, Animals, Signal Transduction
Abstract

We found previously that neural responses to ethanol and the dopamine D2 receptor (D2) agonist 2,10,11-trihydroxy-N-propylnorapomorphine hydrobromide (NPA) involve both epsilon protein kinase C (epsilonPKC) and cAMP-dependent protein kinase A (PKA). However, little is known about the mechanism underlying ethanol- and D2-mediated activation of epsilonPKC and the relationship to PKA activation. In the present study, we used a new epsilonPKC antibody, 14E6, that selectively recognized active epsilonPKC when not bound to its anchoring protein epsilonRACK (receptor for activated C-kinase), and PKC isozyme-selective inhibitors and activators to measure PKC translocation and catalytic activity. We show here that ethanol and NPA activated epsilonPKC and induced translocation of both epsilonPKC and its anchoring protein, epsilonRACK to a new cytosolic site. The selective epsilonPKC agonist, pseudo-epsilonRACK, activated epsilonPKC but did not cause translocation of the epsilonPKC/epsilonRACK complex to the cytosol. These data suggest a step-wise activation and translocation of epsilonPKC after NPA or ethanol treatment, where epsilonPKC first translocates and binds to its RACK and subsequently the epsilonPKC/epsilonRACK complex translocates to a new subcellular site. Direct activation of PKA by adenosine-3',5'-cyclic monophosphorothioate, Sp-isomer (Sp-cAMPS), prostaglandin E1, or the adenosine A2A receptor is sufficient to cause epsilonPKC translocation to the cytosolic compartment in a process that is dependent on PLC activation and requires PKA activity. These data demonstrate a novel cross-talk mechanism between epsilonPKC and PKA signaling systems. PKA and PKC signaling have been implicated in alcohol rewarding properties in the mesolimbic dopamine system. Cross-talk between PKA and PKC may underlie some of the behaviors associated with alcoholism.

Published
2008

36. Response to Letter Regarding Article, “Late Sodium Current Inhibition Reverses Electromechanical Dysfunction in Human Hypertrophic Cardiomyopathy”

Author

Coppini, Raffaele, primary, Ferrantini, Cecilia, additional, Del Lungo, Martina, additional, Stillitano, Francesca, additional, Sartiani, Laura, additional, Tosi, Benedetta, additional, Suffredini, Silvia, additional, Tesi, Chiara, additional, Poggesi, Corrado, additional, Cerbai, Elisabetta, additional, Mugelli, Alessandro, additional, Yao, Lina, additional, Fan, Peidong, additional, Belardinelli, Luiz, additional, Yacoub, Magdi, additional, and Olivotto, Iacopo, additional

Published
2013
Full Text
View/download PDF

37. Late Sodium Current Inhibition Reverses Electromechanical Dysfunction in Human Hypertrophic Cardiomyopathy

Author

Coppini, Raffaele, primary, Ferrantini, Cecilia, additional, Yao, Lina, additional, Fan, Peidong, additional, Del Lungo, Martina, additional, Stillitano, Francesca, additional, Sartiani, Laura, additional, Tosi, Benedetta, additional, Suffredini, Silvia, additional, Tesi, Chiara, additional, Yacoub, Magdi, additional, Olivotto, Iacopo, additional, Belardinelli, Luiz, additional, Poggesi, Corrado, additional, Cerbai, Elisabetta, additional, and Mugelli, Alessandro, additional

Published
2013
Full Text
View/download PDF

42. Addendum: Inhibition of aldehyde dehydrogenase-2 suppresses cocaine seeking by generating THP, a cocaine use–dependent inhibitor of dopamine synthesis

Author

Yao, Lina, primary, Fan, Peidong, additional, Arolfo, Maria, additional, Jiang, Zhang, additional, Olive, M Foster, additional, Zablocki, Jeff, additional, Sun, Hai-Ling, additional, Chu, Nancy, additional, Lee, Jeongrim, additional, Kim, Hee-Yong, additional, Leung, Kwan, additional, Shryock, John, additional, Blackburn, Brent, additional, and Diamond, Ivan, additional

Published
2011
Full Text
View/download PDF

48. Dopamine and Ethanol Cause Translocation of PKC Associated with RACK: Cross-Talk between cAMP-Dependent Protein Kinase A and Protein Kinase C Signaling Pathways

Author

Yao, Lina, Fan, Peidong, Jiang, Zhan, Gordon, Adrienne, Mochly-Rosen, Daria, and Diamond, Ivan

Abstract

We found previously that neural responses to ethanol and the dopamine D2 receptor (D2) agonist 2,10,11-trihydroxy-N-propylnorapomorphine hydrobromide (NPA) involve both protein kinase C (PKC) and cAMP-dependent protein kinase A (PKA). However, little is known about the mechanism underlying ethanol- and D2-mediated activation of PKC and the relationship to PKA activation. In the present study, we used a new PKC antibody, 14E6, that selectively recognized active PKC when not bound to its anchoring protein RACK (receptor for activated C-kinase), and PKC isozyme-selective inhibitors and activators to measure PKC translocation and catalytic activity. We show here that ethanol and NPA activated PKC and induced translocation of both PKC and its anchoring protein, RACK to a new cytosolic site. The selective PKC agonist, pseudo-RACK, activated PKC but did not cause translocation of the PKC/RACK complex to the cytosol. These data suggest a step-wise activation and translocation of PKC after NPA or ethanol treatment, where PKC first translocates and binds to its RACK and subsequently the PKC/RACK complex translocates to a new subcellular site. Direct activation of PKA by adenosine-3',5'-cyclic monophosphorothioate, Sp-isomer (Sp-cAMPS), prostaglandin E1, or the adenosine A2A receptor is sufficient to cause PKC translocation to the cytosolic compartment in a process that is dependent on PLC activation and requires PKA activity. These data demonstrate a novel cross-talk mechanism between PKC and PKA signaling systems. PKA and PKC signaling have been implicated in alcohol rewarding properties in the mesolimbic dopamine system. Cross-talk between PKA and PKC may underlie some of the behaviors associated with alcoholism.

Published
2008

49. Nicotine and Ethanol Activate Protein Kinase A Synergistically via Gi beta{gamma} Subunits in Nucleus Accumbens/Ventral Tegmental Cocultures: The Role of Dopamine D1/D2 and Adenosine A2A Receptors.

Author

Inoue, Yuichiro, Yao, Lina, Hopf, F Woodward, Fan, Peidong, Jiang, Zhan, Bonci, Antonello, and Diamond, Ivan

Abstract

Tobacco and alcohol are the most commonly used drugs of abuse and show the most serious comorbidity. The mesolimbic dopamine system contributes significantly to nicotine and ethanol reinforcement, but the underlying cellular signaling mechanisms are poorly understood. Nicotinic acetylcholine (nACh) receptors are highly expressed on ventral tegmental area (VTA) dopamine neurons, with relatively low expression in nucleus accumbens (NAcb) neurons. Because dopamine receptors D(1) and D(2) are highly expressed on NAcb neurons, nicotine could influence NAcb neurons indirectly by activating VTA neurons to release dopamine in the NAcb. To investigate this possibility in vitro, we established primary cultures containing neurons from VTA or NAcb separately or in cocultures. Nicotine increased cAMP response element-mediated gene expression only in cocultures; this increase was blocked by nACh or dopamine D(1) or D(2) receptor antagonists. Furthermore, subthreshold concentrations of nicotine with ethanol increased gene expression in cocultures, and this increase was blocked by nACh, D(2) or adenosine A(2A) receptor antagonists, Gbetagamma or protein kinase A (PKA) inhibitors, and adenosine deaminase. These results suggest that nicotine activated VTA neurons, causing the release of dopamine, which in turn stimulated both D(1) and D(2) receptors on NAcb neurons. In addition, subthreshold concentrations of nicotine and ethanol in combination also activated NAcb neurons through synergy between D(2) and A(2A) receptors. These data provide a novel cellular mechanism, involving Gbetagamma subunits, A(2A) receptors, and PKA, whereby combined use of tobacco and alcohol could enhance the reinforcing effect in humans as well as facilitate long-term neuroadaptations, increasing the risk for developing coaddiction.

Published
2007
Full Text
View/download PDF

50. Inhibition of aldehyde dehydrogenase-2 suppresses cocaine seeking by generating THP, a cocaine use-dependent inhibitor of dopamine synthesis.

Author

Yao, Lina, Fan, Peidong, Arolfo, Maria, Jiang, Zhang, Olive, M Foster, Zablocki, Jeff, Sun, Hai-Ling, Chu, Nancy, Lee, Jeongrim, Kim, Hee-Yong, Leung, Kwan, Shryock, John, Blackburn, Brent, and Diamond, Ivan

Subjects
*ALDEHYDE dehydrogenase
Abstract

A correction to the article "Inhibition of aldehyde dehydrogenase-2 suppresses cocaine seeking by generating THP, a cocaine use-dependent inhibitor of dopamine synthesis" that was published in the previous issue.

Published
2011
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results