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Article ; Online: The βγ subunit of heterotrimeric G proteins interacts with actin filaments during neuronal differentiation.

Sierra-Fonseca, Jorge A / Miranda, Manuel / Das, Siddhartha / Roychowdhury, Sukla

Biochemical and biophysical research communications

2021 Volume 549, Page(s) 98–104

Abstract: The βγ subunit of heterotrimeric G proteins, a key molecule in the G protein-coupled receptors (GPCRs) signaling pathway, has been shown to be an important factor in the modulation of the microtubule cytoskeleton. Gβγ has been shown to bind to tubulin, ... ...

Abstract	The βγ subunit of heterotrimeric G proteins, a key molecule in the G protein-coupled receptors (GPCRs) signaling pathway, has been shown to be an important factor in the modulation of the microtubule cytoskeleton. Gβγ has been shown to bind to tubulin, stimulate microtubule assembly, and promote neurite outgrowth of PC12 cells. In this study, we demonstrate that in addition to microtubules, Gβγ also interacts with actin filaments, and this interaction increases during NGF-induced neuronal differentiation of PC12 cells. We further demonstrate that the Gβγ-actin interaction occurs independently of microtubules as nocodazole, a well-known microtubule depolymerizing agent did not inhibit Gβγ-actin complex formation in PC12 cells. A confocal microscopic analysis of NGF-treated PC12 cells revealed that Gβγ co-localizes with both actin and microtubule cytoskeleton along neurites, with specific co-localization of Gβγ with actin at the distal end of these neuronal processes. Furthermore, we show that Gβγ interacts with the actin cytoskeleton in primary hippocampal and cerebellar rat neurons. Our results indicate that Gβγ serves as an important modulator of the neuronal cytoskeleton by interacting with both microtubules and actin filaments, and is likely to participate in various aspects of neuronal differentiation including axon and growth cone formation.
MeSH term(s)	Actin Cytoskeleton/drug effects ; Actin Cytoskeleton/metabolism ; Actins/metabolism ; Animals ; Axons/drug effects ; Axons/metabolism ; Cell Differentiation/drug effects ; Cytoskeleton/drug effects ; Cytoskeleton/metabolism ; GTP-Binding Protein beta Subunits/metabolism ; GTP-Binding Protein gamma Subunits/metabolism ; Hippocampus/cytology ; Models, Biological ; Nerve Growth Factor/pharmacology ; Neurons/cytology ; Neurons/drug effects ; Neurons/metabolism ; PC12 Cells ; Polymerization/drug effects ; Protein Binding/drug effects ; Rats ; Rats, Sprague-Dawley
Chemical Substances	Actins ; GTP-Binding Protein beta Subunits ; GTP-Binding Protein gamma Subunits ; Nerve Growth Factor (9061-61-4)
Language	English
Publishing date	2021-03-02
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2021.02.095
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Article ; Online: Giardial lipid rafts share virulence factors with secreted vesicles and participate in parasitic infection in mice.

Grajeda, Brian I / De Chatterjee, Atasi / Villalobos, Carmen M / Pence, Breanna C / Ellis, Cameron C / Enriquez, Vanessa / Roy, Sourav / Roychowdhury, Sukla / Neumann, Aaron K / Almeida, Igor C / Patterson, Steven E / Das, Siddhartha

Frontiers in cellular and infection microbiology

2022 Volume 12, Page(s) 974200

Abstract: ... Giardia ... ...

Abstract	Giardia lamblia
MeSH term(s)	Animals ; Cysts ; Giardia/metabolism ; Giardiasis/parasitology ; Membrane Microdomains/metabolism ; Mice ; Oseltamivir ; Proteomics ; Protozoan Proteins/metabolism ; Virulence Factors/metabolism
Chemical Substances	Protozoan Proteins ; Virulence Factors ; Oseltamivir (20O93L6F9H)
Language	English
Publishing date	2022-08-23
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2619676-1
ISSN	2235-2988 ; 2235-2988
ISSN (online)	2235-2988
ISSN	2235-2988
DOI	10.3389/fcimb.2022.974200
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Article ; Online: Alcohol self-administration and nicotine withdrawal alter biomarkers of stress and inflammation and prefrontal cortex changes in Gβ subunits.

Cruz, Bryan / Castañeda, Karen / Aranda, Michelle / Hinojosa, Cecilia A / Castro-Gutierrez, Roberto / Flores, Rodolfo J / Spencer, Charles T / Vozella, Valentina / Roberto, Marisa / Gadad, Bharathi S / Roychowdhury, Sukla / O'Dell, Laura E

The American journal of drug and alcohol abuse

2022 Volume 49, Issue 3, Page(s) 321–332

Abstract: Background: ...

Abstract	Background:
MeSH term(s)	Rats ; Male ; Animals ; Nicotine/adverse effects ; Leptin/metabolism ; Leptin/pharmacology ; Leptin/therapeutic use ; Corticosterone/metabolism ; Corticosterone/pharmacology ; Corticosterone/therapeutic use ; Rats, Wistar ; Substance Withdrawal Syndrome/drug therapy ; Prefrontal Cortex ; Ethanol/adverse effects
Chemical Substances	Nicotine (6M3C89ZY6R) ; Leptin ; Corticosterone (W980KJ009P) ; Ethanol (3K9958V90M)
Language	English
Publishing date	2022-10-07
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	193086-2
ISSN	1097-9891 ; 0095-2990
ISSN (online)	1097-9891
ISSN	0095-2990
DOI	10.1080/00952990.2022.2121656
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Article ; Online: Activation of β- and α2-adrenergic receptors stimulate tubulin polymerization and promote the association of Gβγ with microtubules in cultured NIH3T3 cells.

Sierra-Fonseca, Jorge A / Bracamontes, Christina / Saldecke, Jessica / Das, Siddhartha / Roychowdhury, Sukla

Biochemical and biophysical research communications

2018 Volume 503, Issue 1, Page(s) 102–108

Abstract: Microtubules (MTs) constitute a crucial part of the cytoskeleton and are essential for cell division and differentiation, cell motility, intracellular transport, and cell morphology. Precise regulation of MT assembly and dynamics is essential for the ... ...

Abstract	Microtubules (MTs) constitute a crucial part of the cytoskeleton and are essential for cell division and differentiation, cell motility, intracellular transport, and cell morphology. Precise regulation of MT assembly and dynamics is essential for the performance of these functions. Although much progress has been made in identifying and characterizing the cellular factors that regulate MT assembly and dynamics, signaling events in this process is not well understood. Gβγ, an important component of the G protein-coupled receptor (GPCR) signaling pathway, has been shown to promote MT assembly in vitro and in cultured NIH3T3 and PC12 cells. Using the MT depolymerizing agent nocodazole, it has been demonstrated that the association of Gβγ with polymerized tubulin is critical for MT assembly. More recently, Gβγ has been shown to play a key role in NGF-induced neuronal differentiation of PC12 cells through its interaction with tubulin/MTs and modulation of MT assembly. Although NGF is known to exert its effect through tyrosine kinase receptor TrkA, the result suggests a possible involvement of GPCRs in this process. The present study was undertaken to determine whether agonist activation of GPCR utilizes Gβγ to promote MT assembly. We used isoproterenol and UK 14,304, agonists for two different GPCRs (β- and α2-adrenergic receptors, respectively) known to activate Gs and Gi respectively, with an opposing effect on production of cAMP. The results demonstrate that the agonist activation of β- and α2-adrenergic receptors promotes the association of Gβγ with MTs and stimulates MT assembly in NIH3T3 cells. Interestingly, the effects of these two agonists were more prominent when the cellular level of MT assembly was low (30% or less). In contrast to MT assembly, actin polymerization was not affected by isoproterenol or UK 14, 304 indicating that the effects of these agonists are limited to MTs. Thus, it appears that, upon cellular demand, GPCRs may utilize Gβγ to promote MT assembly. Stimulation of MT assembly appears to be a novel function of G protein-mediated signaling.
MeSH term(s)	Adrenergic alpha-2 Receptor Agonists/pharmacology ; Adrenergic beta-Agonists/pharmacology ; Animals ; Cell Differentiation ; GTP-Binding Protein beta Subunits/metabolism ; GTP-Binding Protein gamma Subunits/metabolism ; Mice ; Microtubules/metabolism ; NIH 3T3 Cells ; Neurons/cytology ; Neurons/drug effects ; Neurons/metabolism ; PC12 Cells ; Polymerization ; Protein Multimerization ; Rats ; Receptors, Adrenergic, alpha-2/metabolism ; Receptors, Adrenergic, beta/metabolism ; Signal Transduction ; Tubulin/chemistry ; Tubulin/metabolism
Chemical Substances	Adrenergic alpha-2 Receptor Agonists ; Adrenergic beta-Agonists ; GTP-Binding Protein beta Subunits ; GTP-Binding Protein gamma Subunits ; Receptors, Adrenergic, alpha-2 ; Receptors, Adrenergic, beta ; Tubulin
Language	English
Publishing date	2018-06-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2018.05.188
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Article: Activation of β- and α2-adrenergic receptors stimulate tubulin polymerization and promote the association of Gβγ with microtubules in cultured NIH3T3 cells

Sierra-Fonseca, Jorge A / Bracamontes, Christina / Saldecke, Jessica / Das, Siddhartha / Roychowdhury, Sukla

Biochemical and biophysical research communications. 2018 Sept. 03, v. 503, no. 1

2018

Abstract	Microtubules (MTs) constitute a crucial part of the cytoskeleton and are essential for cell division and differentiation, cell motility, intracellular transport, and cell morphology. Precise regulation of MT assembly and dynamics is essential for the performance of these functions. Although much progress has been made in identifying and characterizing the cellular factors that regulate MT assembly and dynamics, signaling events in this process is not well understood. Gβγ, an important component of the G protein-coupled receptor (GPCR) signaling pathway, has been shown to promote MT assembly in vitro and in cultured NIH3T3 and PC12 cells. Using the MT depolymerizing agent nocodazole, it has been demonstrated that the association of Gβγ with polymerized tubulin is critical for MT assembly. More recently, Gβγ has been shown to play a key role in NGF-induced neuronal differentiation of PC12 cells through its interaction with tubulin/MTs and modulation of MT assembly. Although NGF is known to exert its effect through tyrosine kinase receptor TrkA, the result suggests a possible involvement of GPCRs in this process. The present study was undertaken to determine whether agonist activation of GPCR utilizes Gβγ to promote MT assembly. We used isoproterenol and UK 14,304, agonists for two different GPCRs (β- and α2-adrenergic receptors, respectively) known to activate Gs and Gi respectively, with an opposing effect on production of cAMP. The results demonstrate that the agonist activation of β- and α2-adrenergic receptors promotes the association of Gβγ with MTs and stimulates MT assembly in NIH3T3 cells. Interestingly, the effects of these two agonists were more prominent when the cellular level of MT assembly was low (30% or less). In contrast to MT assembly, actin polymerization was not affected by isoproterenol or UK 14, 304 indicating that the effects of these agonists are limited to MTs. Thus, it appears that, upon cellular demand, GPCRs may utilize Gβγ to promote MT assembly. Stimulation of MT assembly appears to be a novel function of G protein-mediated signaling.
Keywords	actin ; agonists ; alpha-2 adrenergic receptors ; cell division ; cell movement ; cyclic AMP ; isoproterenols ; microtubules ; neurons ; physiological transport ; polymerization ; signal transduction ; tubulin ; United Kingdom
Language	English
Dates of publication	2018-0903
Size	p. 102-108.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2018.05.188
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Article ; Online: The assembly of GM1 glycolipid- and cholesterol-enriched raft-like membrane microdomains is important for giardial encystation.

De Chatterjee, Atasi / Mendez, Tavis L / Roychowdhury, Sukla / Das, Siddhartha

Infection and immunity

2015 Volume 83, Issue 5, Page(s) 2030–2042

Abstract: Although encystation (or cyst formation) is an important step of the life cycle of Giardia, the cellular events that trigger encystation are poorly understood. Because membrane microdomains are involved in inducing growth and differentiation in many ... ...

Abstract	Although encystation (or cyst formation) is an important step of the life cycle of Giardia, the cellular events that trigger encystation are poorly understood. Because membrane microdomains are involved in inducing growth and differentiation in many eukaryotes, we wondered if these raft-like domains are assembled by this parasite and participate in the encystation process. Since the GM1 ganglioside is a major constituent of mammalian lipid rafts (LRs) and known to react with cholera toxin B (CTXB), we used Alexa Fluor-conjugated CTXB and GM1 antibodies to detect giardial LRs. Raft-like structures in trophozoites are located in the plasma membranes and on the periphery of ventral discs. In cysts, however, they are localized in the membranes beneath the cyst wall. Nystatin and filipin III, two cholesterol-binding agents, and oseltamivir (Tamiflu), a viral neuraminidase inhibitor, disassembled the microdomains, as evidenced by reduced staining of trophozoites with CTXB and GM1 antibodies. GM1- and cholesterol-enriched LRs were isolated from Giardia by density gradient centrifugation and found to be sensitive to nystatin and oseltamivir. The involvement of LRs in encystation could be supported by the observation that raft inhibitors interrupted the biogenesis of encystation-specific vesicles and cyst production. Furthermore, culturing of trophozoites in dialyzed medium containing fetal bovine serum (which is low in cholesterol) reduced raft assembly and encystation, which could be rescued by adding cholesterol from the outside. Our results suggest that Giardia is able to form GM1- and cholesterol-enriched lipid rafts and these raft domains are important for encystation.
MeSH term(s)	Cholesterol/metabolism ; G(M1) Ganglioside/metabolism ; Giardia/growth & development ; Giardia/metabolism ; Membrane Microdomains/metabolism ; Spores, Protozoan/growth & development ; Spores, Protozoan/metabolism
Chemical Substances	G(M1) Ganglioside (37758-47-7) ; Cholesterol (97C5T2UQ7J)
Language	English
Publishing date	2015-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	218698-6
ISSN	1098-5522 ; 0019-9567
ISSN (online)	1098-5522
ISSN	0019-9567
DOI	10.1128/IAI.03118-14
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Article: Submembraneous microtubule cytoskeleton: regulation of microtubule assembly by heterotrimeric Gproteins.

Roychowdhury, Sukla / Rasenick, Mark M

The FEBS journal

2008 Volume 275, Issue 19, Page(s) 4654–4663

Abstract: Heterotrimeric Gproteins participate in signal transduction by transferring signals from cell surface receptors to intracellular effector molecules. Gproteins also interact with microtubules and participate in microtubule-dependent centrosome/chromosome ... ...

Abstract	Heterotrimeric Gproteins participate in signal transduction by transferring signals from cell surface receptors to intracellular effector molecules. Gproteins also interact with microtubules and participate in microtubule-dependent centrosome/chromosome movement during cell division, as well as neuronal differentiation. In recent years, significant progress has been made in our understanding of the biochemical/functional interactions between Gprotein subunits (alpha and betagamma) and microtubules, and the molecular details emerging from these studies suggest that alpha and betagamma subunits of Gproteins interact with tubulin/microtubules to regulate the assembly/dynamics of microtubules, providing a novel mechanism for hormone- or neurotransmitter-induced rapid remodeling of cytoskeleton, regulation of the mitotic spindle for centrosome/chromosome movements in cell division, and neuronal differentiation in which structural plasticity mediated by microtubules is important for appropriate synaptic connections and signal transmission.
MeSH term(s)	Cell Differentiation ; Cell Division ; Cytoskeleton/metabolism ; GTP-Binding Protein alpha Subunits, Gi-Go/physiology ; GTP-Binding Protein alpha Subunits, Gs/physiology ; GTP-Binding Protein beta Subunits/physiology ; GTP-Binding Protein gamma Subunits/physiology ; Heterotrimeric GTP-Binding Proteins/physiology ; Microtubules/physiology ; Neurons/cytology ; Signal Transduction ; Spindle Apparatus/physiology ; Spindle Apparatus/ultrastructure ; Tubulin/physiology
Chemical Substances	GTP-Binding Protein beta Subunits ; GTP-Binding Protein gamma Subunits ; Tubulin ; GTP-Binding Protein alpha Subunits, Gi-Go (EC 3.6.5.1) ; GTP-Binding Protein alpha Subunits, Gs (EC 3.6.5.1) ; Heterotrimeric GTP-Binding Proteins (EC 3.6.5.1)
Language	English
Publishing date	2008-08-27
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/j.1742-4658.2008.06614.x
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Article: Arachidonic Acid Induces the Migration of MDA-MB-231 Cells by Activating Raft-associated Leukotriene B4 Receptors.

Chatterjee, Atasi De / Roy, Debarshi / Guevara, Priscilla / Pal, Rituraj / Naryan, Mahesh / Roychowdhury, Sukla / Das, Siddhartha

Clinical cancer drugs

2017 Volume 5, Issue 1, Page(s) 28–41

Abstract: Background: The migration of tumor cells is critical in spreading cancers through the lymphatic nodes and circulatory systems. Although arachidonic acid (AA) and its soluble metabolites have been shown to induce the migration of breast and colon cancer ... ...

Abstract	Background: The migration of tumor cells is critical in spreading cancers through the lymphatic nodes and circulatory systems. Although arachidonic acid (AA) and its soluble metabolites have been shown to induce the migration of breast and colon cancer cells, the mechanism by which it induces such migration has not been fully understood. Objective: The effect of AA on migratory responses of the MDA-MB-231 cell line (a triple-negative breast cancer cell) was examined and compared with MCF-7 (estrogen-receptor positive) breast cancer cells to elucidate the mechanism of AA-induced migration. Methods: Migrations of breast cancer cells were examined with the help of wound-healing assays. AA-induced eicosanoid synthesis was monitored by RP-HPLC. Cellular localizations of lipoxygenase and lipid rafts were assessed by immunoblot and confocal microscopy. Results: AA treatment stimulated the synthesis of leukotriene B4 (LTB Conclusion: Our results suggest that AA treatment activates the BLT1 receptor (present in membrane microdomains) and stimulates the synthesis of LTB
Language	English
Publishing date	2017-07-12
Publishing country	United Arab Emirates
Document type	Journal Article
ISSN	2212-697X
ISSN	2212-697X
DOI	10.2174/2212697X05666180418145601
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Article: Submembraneous microtubule cytoskeleton: regulation of microtubule assembly by heterotrimeric G proteins

Roychowdhury, Sukla / Rasenick, Mark M

FEBS journal. 2008 Oct., v. 275, no. 19

2008

Abstract: Heterotrimeric G proteins participate in signal transduction by transferring signals from cell surface receptors to intracellular effector molecules. G proteins also interact with microtubules and participate in microtubule-dependent centrosome/ ... ...

Abstract	Heterotrimeric G proteins participate in signal transduction by transferring signals from cell surface receptors to intracellular effector molecules. G proteins also interact with microtubules and participate in microtubule-dependent centrosome/chromosome movement during cell division, as well as neuronal differentiation. In recent years, significant progress has been made in our understanding of the biochemical/functional interactions between G protein subunits (α and βγ) and microtubules, and the molecular details emerging from these studies suggest that α and βγ subunits of G proteins interact with tubulin/microtubules to regulate the assembly/dynamics of microtubules, providing a novel mechanism for hormone- or neurotransmitter-induced rapid remodeling of cytoskeleton, regulation of the mitotic spindle for centrosome/chromosome movements in cell division, and neuronal differentiation in which structural plasticity mediated by microtubules is important for appropriate synaptic connections and signal transmission.
Language	English
Dates of publication	2008-10
Size	p. 4654-4663.
Publisher	Blackwell Publishing Ltd
Publishing place	Oxford, UK
Document type	Article
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/j.1742-4658.2008.06614.x
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Article ; Online: Nerve growth factor induces neurite outgrowth of PC12 cells by promoting Gβγ-microtubule interaction.

Sierra-Fonseca, Jorge A / Najera, Omar / Martinez-Jurado, Jessica / Walker, Ellen M / Varela-Ramirez, Armando / Khan, Arshad M / Miranda, Manuel / Lamango, Nazarius S / Roychowdhury, Sukla

BMC neuroscience

2014 Volume 15, Page(s) 132

Abstract: Background: Assembly and disassembly of microtubules (MTs) is critical for neurite outgrowth and differentiation. Evidence suggests that nerve growth factor (NGF) induces neurite outgrowth from PC12 cells by activating the receptor tyrosine kinase, TrkA. ...

Abstract	Background: Assembly and disassembly of microtubules (MTs) is critical for neurite outgrowth and differentiation. Evidence suggests that nerve growth factor (NGF) induces neurite outgrowth from PC12 cells by activating the receptor tyrosine kinase, TrkA. G protein-coupled receptors (GPCRs) as well as heterotrimeric G proteins are also involved in regulating neurite outgrowth. However, the possible connection between these pathways and how they might ultimately converge to regulate the assembly and organization of MTs during neurite outgrowth is not well understood. Results: Here, we report that Gβγ, an important component of the GPCR pathway, is critical for NGF-induced neuronal differentiation of PC12 cells. We have found that NGF promoted the interaction of Gβγ with MTs and stimulated MT assembly. While Gβγ-sequestering peptide GRK2i inhibited neurite formation, disrupted MTs, and induced neurite damage, the Gβγ activator mSIRK stimulated neurite outgrowth, which indicates the involvement of Gβγ in this process. Because we have shown earlier that prenylation and subsequent methylation/demethylation of γ subunits are required for the Gβγ-MTs interaction in vitro, small-molecule inhibitors (L-28 and L-23) targeting prenylated methylated protein methyl esterase (PMPMEase) were tested in the current study. We found that these inhibitors disrupted Gβγ and ΜΤ organization and affected cellular morphology and neurite outgrowth. In further support of a role of Gβγ-MT interaction in neuronal differentiation, it was observed that overexpression of Gβγ in PC12 cells induced neurite outgrowth in the absence of added NGF. Moreover, overexpressed Gβγ exhibited a pattern of association with MTs similar to that observed in NGF-differentiated cells. Conclusions: Altogether, our results demonstrate that βγ subunit of heterotrimeric G proteins play a critical role in neurite outgrowth and differentiation by interacting with MTs and modulating MT rearrangement.
MeSH term(s)	Animals ; Carboxylic Ester Hydrolases/antagonists & inhibitors ; Carboxylic Ester Hydrolases/metabolism ; Cell Enlargement ; Cells, Cultured ; Cerebellum/cytology ; Cerebellum/physiology ; GTP-Binding Protein beta Subunits/metabolism ; GTP-Binding Protein gamma Subunits/metabolism ; Hippocampus/cytology ; Hippocampus/physiology ; Microtubules/metabolism ; Nerve Growth Factor/metabolism ; Neurites/physiology ; Neurogenesis/physiology ; Neurons/cytology ; Neurons/physiology ; PC12 Cells ; Rats ; Rats, Sprague-Dawley ; Tubulin/metabolism
Chemical Substances	GTP-Binding Protein beta Subunits ; GTP-Binding Protein gamma Subunits ; Tubulin ; Nerve Growth Factor (9061-61-4) ; Carboxylic Ester Hydrolases (EC 3.1.1.-) ; prenylated methylated protein methyl esterase, rat (EC 3.1.1.-)
Language	English
Publishing date	2014-12-31
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2041344-0
ISSN	1471-2202 ; 1471-2202
ISSN (online)	1471-2202
ISSN	1471-2202
DOI	10.1186/s12868-014-0132-4
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