Short-time effects of neuroactive steroids on rat cortical Ca2+-ATPase activity

Żylińska, Ludmiła; Gromadzińska, Ewa; Lachowicz, Lilla

doi:10.1016/s1388-1981(99)00015-3

Cited by 36 publications

(20 citation statements)

References 39 publications

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“…These include a single study that demonstrates 17␤-estradiol-mediated stimulation of Ca 2ϩ efflux from porcine coronary arterial smooth muscle cells (13). This is consistent with reports that 17␤-estradiol stimulates plasma membrane Ca 2ϩ ATPase (PMCA) of both excitable (rat cortical synaptosomes) (39,40) and non-excitable (human erythrocytes) cells (40).…”

supporting

confidence: 83%

17β-Estradiol Elevates cGMP and, via Plasma Membrane Recruitment of Protein Kinase GIα, Stimulates Ca2+ Efflux from Rat Hepatocytes

Stratton

Squires

Green

2010

Journal of Biological Chemistry

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Rapid non-genomic effects of 17␤-estradiol, the principal circulating estrogen, have been observed in a wide variety of cell types. Here we investigate rapid signaling effects of 17␤-estradiol in rat hepatocytes. We show that, above a threshold concentration of 1 nM, 17␤-estradiol, but not 17␣-estradiol, stimulates particulate guanylyl cyclase to elevate cGMP, which through activation and plasma membrane recruitment of protein kinase G isoform I␣, stimulates plasma membrane Ca 2؉ -ATPase-mediated Ca 2؉ efflux from rat hepatocytes. These effects are extremely rapid in onset and are mimicked by a membrane-impermeant 17␤-estradiol-BSA conjugate, suggesting that 17␤-estradiol acts at the extracellular face of the plasma membrane. We also show that 17␤-estradiol binds specifically to the intact hepatocyte plasma membrane through an interaction that is competed by an excess of atrial natriuretic peptide but also shows many similarities to the pharmacological characteristics of the putative ␥-adrenergic receptor. We, therefore, propose that the observed rapid signaling effects of 17␤-estradiol are mediated either through the guanylyl cyclase A receptor for atrial natriuretic peptide or through the ␥-adrenergic receptor, which is either itself a transmembrane guanylyl cyclase or activates a transmembrane guanylyl cyclase through cross-talk signaling.

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supporting

confidence: 83%

17β-Estradiol Elevates cGMP and, via Plasma Membrane Recruitment of Protein Kinase GIα, Stimulates Ca2+ Efflux from Rat Hepatocytes

Stratton

Squires

Green

2010

Journal of Biological Chemistry

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“…A few studies consider the effects of hormones on ATPase activity. For example, the demonstration that physiologically relevant concentrations of estradiol increased the hydrolytic activity of rat cortical Ca 2ϩ -ATPase (56) supports the idea that this plasma membrane calcium pump is a nongenomic steroid target (56). Menkes-and Wilson-ATPases have been implicated in human disorders of copper homeostasis.…”

Section: An Atypical Nuclear P-type Atpase Is a Rfbp 3645mentioning

confidence: 90%

Cloning and Characterization of an Atypical Type IV P-type ATPase That Binds to the RING Motif of RUSH Transcription Factors

Mansharamani

Hewetson

Chilton³

2001

Journal of Biological Chemistry

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RUSH proteins are SWI/SNF-related transcription factors with RING finger signatures near their COOH termini. Long suspected of mediating protein-protein interactions, the RING motif was used to clone a binding partner. The RING finger binding protein (RFBP) is a Type IV P-type ATPase, a putative phospholipid pump, with conserved sequences for two loop segments, an ATP-binding site, a phosphorylation domain, and transmembrane passes potentially involved in substrate binding and translocation. However, RFBP differs from all other Type IV P-type ATPases in three ways. It has only three of four highly conserved NH 2 -terminal transmembrane passes, it is located in the inner nuclear membrane, and it binds the RING domain. Topographically the orientation of the adjacent hydrophilic domains and the determinants of transport specificity are altered. As a result, the small, hydrophilic loop extends into the perinuclear space that is contiguous with the lumen of the endoplasmic reticulum. The large, conformationally flexible loop extends into the nucleoplasm to contact euchromatin. Competitive reverse transcriptasepolymerase chain reaction and high performance liquid chromatography analysis revealed that endometrial RFBP mRNA expression is hormonally regulated. The physical association of a hormone-dependent RING finger-binding protein with transcriptionally active chromatin supports the speculation that RFBP plays a role in the subnuclear trafficking of transcription factors with RING motifs.RUSH is an acronym for proteins with RING finger motifs that bind to the uteroglobin promoter (1); RUSH nucleophosphoproteins contain regions of homology with members of the SWI/SNF superfamily of DNA-dependent helicases/ATPases. The expression of RUSH-1␣ (1005-amino acids, 113 kDa) and RUSH-1␤ (836 amino acids, 95 kDa) is regulated by a steroiddependent alternative splicing mechanism (2) in which ␣ is the progesterone-dependent splice variant, and ␤ is the estrogendependent splice variant. Thus, the acronym acknowledges that in a changing hormonal milieu transcription is bypassed by alternative splicing, and the response of individual target genes is accelerated or "RUSHed."Sequence alignment of homologs from rabbit, human, rodent, and plant (3) showed that all RUSH proteins contain the RING finger motif (C 3 HC 4 or RING-HC), which binds two zinc ions in a unique cross-braced system (4). RING fingers can be associated with other motifs to form larger, conserved domains such as the RING finger-B box-␣-helical coiled-coil (RBCC) domain (4). Some changes have occurred in the RING such that RING-H2 (C 3 H 2 C 3 ) designates a subclass in which a histidine residue was substituted for the fourth cysteine residue. The U-box (UFD2 homology domain) is a degenerate version of the RING motif that lacks the signature metal-chelating residues (5, 6). Unlike the authentic RING finger that is stabilized by binding zinc ions, it has been inferred from the PROMODII model that the U-box is maintained by a system of salt bridges and hydrogen bonds (6...

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“…Testosterone appears to increase the activity of both Na/K-ATPase and Ca 2+ -ATPase [57]. Acute T treatment causes a dose-dependent increase in the hydrolytic ability of Ca 2+ -ATPase purified from synaptosomal membranes of rat cortex [51].…”

Section: Androgen Induces Changes In Membrane "Flexibility"mentioning

confidence: 97%

“…Androgen metabolites have been found to acquire additional charges from sulfate residues and in turn achieve the necessary charge to penetrate into the lipid/protein complex of the cell membrane, thereby decreasing the membrane flexibility and modulating the actions of enzymes required for ATP hydrolysis [51]. For example, Verbist et al (1991) demonstrated a direct interaction of negatively charged phospholipids with membrane ATPase calcium pumps via fluorescent resonance energy transfer [52].…”

Section: Androgen Induces Changes In Membrane "Flexibility"mentioning

confidence: 99%

Non-genomic actions of androgens

Foradori

Weiser

Handa

2008

Frontiers in Neuroendocrinology

412

244

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Previous work in the endocrine and neuroendocrine fields has viewed androgen receptors (AR) as a transcription factor activated by testosterone or one of its many metabolites. The bound androgen receptor acts as transcription factor and binds to specific DNA response elements in target gene promoters, causing activation or repression of transcription and subsequently protein synthesis. Over the past two decades evidence has begun to accumulate to implicate androgens, dependent or independent of the AR, in rapid actions at the cellular and organism level. Androgen's rapid time course of action; effects in the absence or inhibition of the cellular machinery necessary for transcription/translation; and/or the effects of androgens not able to translocate to the nucleus suggest a method of androgen action not initially dependent on genomic mechcanisms (i.e. non-genomic in nature). In the present paper the non-genomic effects of androgens are reviewed, along with a discussion of the possible role non-genomic androgen actions have on animal physiology and behavior.

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Short-time effects of neuroactive steroids on rat cortical Ca2+-ATPase activity

Cited by 36 publications

References 39 publications

17β-Estradiol Elevates cGMP and, via Plasma Membrane Recruitment of Protein Kinase GIα, Stimulates Ca2+ Efflux from Rat Hepatocytes

17β-Estradiol Elevates cGMP and, via Plasma Membrane Recruitment of Protein Kinase GIα, Stimulates Ca2+ Efflux from Rat Hepatocytes

Cloning and Characterization of an Atypical Type IV P-type ATPase That Binds to the RING Motif of RUSH Transcription Factors

Non-genomic actions of androgens

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