A constitutively active form of CREB can activate expression of the rat prolactin promoter in non-pituitary cells

Yan, Guo-zai; Chen, Xiaohuai; Bancroft, Carter

doi:10.1016/0303-7207(94)90255-0

Cited by 16 publications

(7 citation statements)

References 23 publications

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“…1), was generated by PCR using pGL3-0.1mHK␣2 as a template. Plasmids CMV500, CREB, the dominant negative CREB mutant A-CREB (1), the constitutively active CREB mutant CREB-VP16 (25,36), and pCREBdLZ-VP16, which is identical to CREB-VP16 except that the DNAbinding and dimerization domains of CREB are deleted (25), were a gift from Dr. D. D. Ginty (Department of Neuroscience, Howard Hughes Medical Institute, The Johns Hopkins University School of Medicine, Baltimore, MD). Plasmid glutathione S-transferase (GST)-CREB-1 (10) was a gift from Dr. T. F. Osborne (Department of Biology and Biochemistry, University of California, Irvine, CA).…”

Section: Methodsmentioning

confidence: 99%

CREB trans-activates the murine H⁺-K⁺-ATPase α₂-subunit gene

Xu¹,

Zhang²,

Kone³

2004

American Journal of Physiology-Cell Physiology

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Despite its key role in potassium homeostasis, transcriptional control of the H ϩ -K ϩ -ATPase ␣2-subunit (HK␣2) gene in the collecting duct remains poorly characterized. cAMP increases H ϩ -K ϩ -ATPase activity in the collecting duct, but its role in activating HK␣2 transcription has not been explored. Previously, we demonstrated that the proximal 177 bp of the HK␣2 promoter confers basal collecting duct-selective expression. This region contains several potential cAMP/Ca 2ϩ -responsive elements (CRE). Accordingly, we examined the participation of CRE-binding protein (CREB) in HK␣2 transcriptional control in murine inner medullary collecting duct (mIMCD)-3 cells. Forskolin and vasopressin induced HK␣2 mRNA levels, and CREB overexpression stimulated the activity of HK␣2 promoter-luciferase constructs. Serial deletion analysis revealed that CREB inducibility was retained in a construct containing the proximal 100 bp of the HK␣2 promoter. In contrast, expression of a dominant negative inhibitor (A-CREB) resulted in 60% lower HK␣2 promoter-luciferase activity, suggesting that constitutive CREB participates in basal HK␣2 transcriptional activity. A constitutively active CREB mutant (CREB-VP16) strongly induced HK␣2 promoter-luciferase activity, whereas overexpression of CREBdLZ-VP16, which lacks the CREB DNA-binding domain, abolished this activation. In vitro DNase I footprinting and gel shift/supershift analysis of the proximal promoter with recombinant glutathione S-transferase (GST)-CREB-1 and mIMCD-3 cell nuclear extracts revealed sequence-specific DNA-CREB-1 complexes at Ϫ86/ Ϫ60. Mutation at three CRE-like sequences within this region abolished CREB-1 DNA-binding activity and abrogated CREB-VP16 trans-activation of the HK␣2 promoter. In contrast, mutation of the neighboring Ϫ104/Ϫ94 ␤ element did not alter CREB-VP16 transactivation of the HK␣2 promoter. Thus CREB-1, binding to one or more CRE-like elements in the Ϫ86/Ϫ60 region, trans-activates the HK␣2 gene and may represent an important link between rapid and delayed effects of cAMP on HK␣2 activity. transcription; promoter; cAMP; potassium POTASSIUM AND ACID-BASE HOMEOSTASIS must be strictly maintained and restored for the proper functioning of all eukaryotic cells. Epithelial cells of the kidney and colon play a critical role in adjusting K ϩ , Na ϩ , and acid elimination to accommodate changes in dietary intake. Physiological and molecular biological studies in animals have pointed to the H ϩ -K ϩ -ATPase ␣ 2 -subunit gene (HK␣ 2 , also termed colonic H ϩ -K ϩ -ATPase), which is principally expressed in the distal colon and renal collecting duct, as a key participant in the control of body K ϩ homeostasis (14,29,30,35). For example, mice with null mutations in this gene experience profound hypokalemia during dietary K ϩ (18) and Na ϩ restriction (31). HK␣ 2 may also play a role in HCO 3 Ϫ absorption by the kidney (20, 21) and the distal colon (18), as well as increased ammonium secretion in the inner medullary collecting duct (IMCD) during chronic hypokal...

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Section: Methodsmentioning

confidence: 99%

CREB trans-activates the murine H⁺-K⁺-ATPase α₂-subunit gene

Xu¹,

Zhang²,

Kone³

2004

American Journal of Physiology-Cell Physiology

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“…We thus examined the effects of suppression and activation of CREB on VAMP2-EGFP punctum formation using A-CREB as a dominantnegative inhibitor of CREB (Ahn et al, 1998) and VP16-CREB as a constitutively active CREB (Yan et al, 1994), respectively. The A-CREB and VP16-CREB genes were placed in the effector-reporter cassette to yield Pomp-VG-ACREB and Pomp-VG-VP16CREB, respectively (Fig.…”

Section: Creb Regulates Vamp2-egfp Punctum Formation In Axon Terminalsmentioning

confidence: 99%

Distinct Roles of Calcineurin-Nuclear Factor of Activated T-Cells and Protein Kinase A-cAMP Response Element-Binding Protein Signaling in Presynaptic Differentiation

Yoshida¹,

Mishina²

2005

J. Neurosci.

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Synaptic vesicle accumulation and morphological changes are characteristic features of axon terminal differentiation during synaptogenesis. To investigate the regulatory mechanism that orchestrates synaptic molecules to form mature presynaptic terminals, we visualized a single axon terminal of zebrafish olfactory sensory neurons in vivo and examined the effects of the neuron-specific gene manipulations on the axon terminal differentiation. Synaptic vesicles visualized with vesicle-associated membrane protein 2 (VAMP2)-enhanced green fluorescent protein (EGFP) fusion protein gradually accumulated in axon terminals, whereas the axon terminals visualized with GAP43 fused with EGFP remodeled from complex shapes with filopodia to simple shapes without filopodia from 50 h postfertilization (hpf) to 84 hpf. Expression of dominant-negative protein kinase A (PKA) or cAMP response element-binding protein (CREB) suppressed the VAMP2-EGFP punctum formation in axon terminals during synaptogenesis. Consistently, constitutively active PKA or CREB stimulated VAMP2-EGFP puncta formation. On the other hand, cyclosporine A treatment or suppression of nuclear factor of activated T cells (NFAT) activation prevented the axon terminal remodeling from complex to simple shapes during synaptogenesis. Consistently, expression of constitutively active calcineurin accelerated the axon terminal remodeling. These results suggest that calcineurin-NFAT signaling regulates axon terminal remodeling, and PKA-CREB signaling controls synaptic vesicle accumulation.

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“…Gene Transfer-The expression vector used was pSV2-CREB-VP16 (a generous gift from Dr. C. Bancroft, Mount Sinai School of Medicine, New York, NY), which encodes a chimera protein where CREB-(1-341) is fused to the transcription activator region of VP16, thus generating a constitutively active CREB protein (40). Neuronal gene transfer was performed as reported previously, using polyethyleneimine 25 kDa (PEI 25K, Sigma) as DNA carrier (41).…”

Section: Materials-polyornithinementioning

confidence: 99%

Amyloid Precursor Protein Family-induced Neuronal Death Is Mediated by Impairment of the Neuroprotective Calcium/Calmodulin Protein Kinase IV-dependent Signaling Pathway

Mbebi¹,

Sée²,

Mercken³

et al. 2002

Journal of Biological Chemistry

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The aberrant metabolism of ␤-amyloid precursor protein (APP) and the progressive deposition of its derived fragment ␤-amyloid peptide are early and constant pathological hallmarks of Alzheimer's disease. Because APP is able to function as a cell surface receptor, we investigated here whether a disruption of the normal function of APP may contribute to the pathogenic mechanisms in Alzheimer's disease. To this aim, we generated a specific chicken polyclonal antibody directed against the extracellular domain of APP, which is common with the ␤-amyloid precursor-like protein type 2. Exposure of cultured cortical neurons to this antibody (APP-Ab) induced cell death preceded by neurite degeneration, oxidative stress, and nuclear condensation. Interestingly, caspase-3-like protease was not activated in this neurotoxic action suggesting a different mode of cell death than classical apoptosis. Further analysis of the molecular mechanisms revealed a calpain-and calcineurindependent proteolysis of the neuroprotective calcium/ calmodulin-dependent protein kinase IV and its nuclear target protein cAMP responsive element binding protein. These effects were abolished by the G protein inhibitor pertussis toxin, strongly suggesting that APP binding operates via a GTPase-dependent pathway to cause neuronal death. Alzheimer's disease (AD)1 is a devastating neurodegenerative disorder characterized by deposition of ␤-amyloid (A␤) plaques, accumulation of intracellular neurofibrillary tangles, and neuronal cell loss (1). A␤ peptide is generated by proteolysis of the amyloid precursor protein (APP), which is the product of a gene located on human chromosome 21 and on mouse chromosome 16. APP is expressed in most mammalian tissues (2, 3) and is present in at least 10 different spliced variants (4). In the brain, the major isoform generating A␤ is a peptide consisting of 695 residues that contains a single transmembrane domain (5). Although the physiological role of APP is still unclear, several studies have suggested that it is implicated in important physiological functions of neurons, such as neurite outgrowth, synaptogenesis, cell substrate adhesion and neuronal survival (for review see Ref. 6).Up to now, most of the research has been focused on the toxicity of A␤ peptide related to AD. A␤ has been reported to exert a variety of toxic effects on neurons both in vitro (7,8) and in vivo (9). However, it has been reported that mice overproducing A␤1-42 extracellularly showed no neuronal loss (10), thus suggesting that A␤ peptide seems not to be the only constituent in neurotoxicity associated to AD. Previous studies have demonstrated that overexpression of full-length APP induced degeneration of postmitotic neurons derived from embryonal carcinoma cells (11). Moreover, intracellular accumulation of wild-type APP in the rat hippocampus caused a specific type of neuronal degeneration in vivo in the absence of extracellular A␤ deposition (12), and viral vector-mediated overexpression of wild-type APP induced apoptosis-like death of neurons...

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A constitutively active form of CREB can activate expression of the rat prolactin promoter in non-pituitary cells

Cited by 16 publications

References 23 publications

CREB trans-activates the murine H⁺-K⁺-ATPase α₂-subunit gene

CREB trans-activates the murine H⁺-K⁺-ATPase α₂-subunit gene

Distinct Roles of Calcineurin-Nuclear Factor of Activated T-Cells and Protein Kinase A-cAMP Response Element-Binding Protein Signaling in Presynaptic Differentiation

Amyloid Precursor Protein Family-induced Neuronal Death Is Mediated by Impairment of the Neuroprotective Calcium/Calmodulin Protein Kinase IV-dependent Signaling Pathway

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A constitutively active form of CREB can activate expression of the rat prolactin promoter in non-pituitary cells

Cited by 16 publications

References 23 publications

CREB trans-activates the murine H+-K+-ATPase α2-subunit gene

CREB trans-activates the murine H+-K+-ATPase α2-subunit gene

Distinct Roles of Calcineurin-Nuclear Factor of Activated T-Cells and Protein Kinase A-cAMP Response Element-Binding Protein Signaling in Presynaptic Differentiation

Amyloid Precursor Protein Family-induced Neuronal Death Is Mediated by Impairment of the Neuroprotective Calcium/Calmodulin Protein Kinase IV-dependent Signaling Pathway

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CREB trans-activates the murine H⁺-K⁺-ATPase α₂-subunit gene

CREB trans-activates the murine H⁺-K⁺-ATPase α₂-subunit gene