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Transcriptional properties of Ptx1 and Ptx2 isoforms. Paper-8395505.
A new family of G-protein regulators - the RGS proteins. Paper-956564.
Axenfeld-Rieger syndrome and spectrum of PITX2 and FOXC1 mutations. Paper-14120151.
Full-spectrum ARS is caused primarily by mutations in the PITX2 gene. Paper-11450548.
LEF-1 specifically interacts with the PITX2 C-terminal tail. Paper-10787415.
Genetic analysis of PITX2 and FOXC1 in Rieger Syndrome patients from Brazil. Paper-9365616.
We suggest that this mutation in PITX2 is the cause of typical ARS in patients. Paper-13482193.
A sequencing-based mutation screen was undertaken for the PITX2 and FOXC1 genes. Paper-9365616.
The smallest FOXC1 and PITX2 deletions were 5.4 and 1.6 kb in size, respectively. Paper-15636891.
CONCLUSIONS: FOXC1 and PITX2 genetic defects explain 40% of our large ASD cohort. Paper-15636891.
Novel mutations of FOXC1 and PITX2 in patients with Axenfeld-Rieger malformations. Paper-12197507.
CONCLUSIONS: We found a novel p.W86C mutation in PITX2 in a Chinese family with ARS. Paper-13482193.
This mutation indicates that IGDS and ARS are allelic variants of the same disorder. Paper-1677181.
Both deletions included only the PITX2 and ENPEP ( glutamyl aminopeptidase) genes. Paper-12574002.
Cellular regulation of RGS proteins: modulators and integrators of G protein signaling. Paper-9331374.
This included complete sequencing for PITX2, BARX1 and the forkhead domain of FOXC1. Paper-13258387.
In this study, we characterized the molecular defect in PITX2 in a Chinese family with ARS. Paper-13482193.
RIEG1 , the gene responsible for the 4q25 ARS phenotype, recently has been cloned. Paper-1677181.
PAWR was also found to inhibit PITX2 transcriptional activity in ocular cells. Paper-14094135.
In addition, six FOXC1 and five PITX2 deletions were found, explaining 14% (11/80) of the cases. Paper-15636891.
RESULTS: We identified four novel PITX2 genetic alterations in four unrelated families with ARS. Paper-12355135.
Cell-specific activation of the atrial natriuretic factor promoter by PITX2 and MEF2A. Paper-10616674.
Antagonistic regulation of Dlx2 expression by PITX2 and Msx2: implications for tooth development. Paper-9149037.
The PITX2 gene is a major gene encoding a major transcription factor associated with ARS. Paper-12355135.
Mutations in several chromosomal loci have been implicated in ARS, including PITX2, FOXC1 and PAX6. Paper-11450548.
The Ptx ( Pitx) family of homeobox transcription factors comprises Ptx1, Ptx2 and Ptx3. Paper-8395505.
Mutation analysis of the PAX6, FOX1, PITX2, and MYNC genes was normal as was MLPA for these genes. Paper-12720059.
Mutational analysis of the PITX2 and NKX2-5 genes in patients with idiopathic atrial fibrillation. Paper-15543426.
Of note, the patients with nonocular findings were more likely to have PITX2 defects than FOXC1 defects. Paper-12388599.
If RGS proteins were active unrestrictedly, they would completely suppress G-protein-mediated signaling. Paper-10512042.
Consistent with these results we show that the human 2.5 kb LEF-1 promoter is activated by PITX2. Paper-10787415.
RESULTS: Thirteen FOXC1 and eight PITX2 mutations were identified, accounting for 26% (21/80) of the cases. Paper-15636891.
PITX2, beta-catenin and LEF-1 interact to synergistically regulate the LEF-1 promoter. Paper-10787415.
TGFbeta enhances Foxc1 and induces Pitx2 expression in cell cultures. Paper-11280273.
The 2.5 kb LEF-1 promoter contains two regions that act to inhibit its transcription in concert with PITX2. Paper-10787415.
These data suggest PAWR is a novel PITX2-interacting protein that regulates PITX2 activity in ocular cells. Paper-14094135.
Linkage analysis was used to study one large family for which no mutations were detected in the PITX2 or FOXC1 genes. Paper-9365616.
For the first time, we present evidence that increased PITX2 activity may underlie the severe ARS ocular phenotype. Paper-9038146.
Pit-1 interaction with the Pitx2 C terminus masks the inhibitory effect and promotes increased DNA binding activity. Paper-8279496.
The coding regions of PITX2, FOXC1, CYP1B1, and GJA1 genes were completely evaluated through direct sequencing. Paper-11820122.
Expanding the spectrum of FOXC1 and PITX2 mutations and copy number changes in patients with anterior segment malformations. Paper-15636891.
Conversely, Pitx1 or Pitx2 overexpression in GH4C1 cells leads to an enhancement of the drugs stimulatory effects. Paper-9244684.
Genotype-phenotype correlations in Axenfeld-Rieger malformation and glaucoma patients with FOXC1 and PITX2 mutations. Paper-12388599.
However, it is only modestly activated in the LS-8 tooth epithelial cell line that endogenously expresses Msx2 and Pitx2. Paper-9149037.
Intriguingly, PITX2 is also involved in left-right polarity determination, although asymmetry defects are not a feature of ARS. Paper-11450548.
A large family of regulator of G protein signaling ( RGS) proteins modulates signaling through G-protein-coupled receptors. Paper-12299957.
The purpose of this study was to evaluate PITX2, FOXC1, CYP1B1, and GJA1 gene mutations in Brazilian families with AR. Paper-11820122.
RESULTS: Two of the five families harbored mutations in the PITX2 gene, but none of the families had a detectable FOXC1 mutation. Paper-9365616.
CONCLUSION: Our results implicate the potential importance of Pitx2 as a beta-catenin downstream modulator in hair growth control. Paper-13641502.
Identification of a Wnt/Dvl/ beta-Catenin --> Pitx2 pathway mediating cell-type-specific proliferation during development. Paper-9318167.
Ocular phenotypes arise despite the deregulated expression of FOXC1- target genes through mutations in FOXC1 or PITX2. Paper-11356667.
The availability of mouse models for both PITX2 and FOXC1 has allowed detailed study of their expression and mutant phenotypes. Paper-9546396.
AR malformations are associated with mutations in two transcription factor genes ( PITX2 and FOXC1) expressed throughout eye ontogeny. Paper-9546396.
Thus, Dlx2 gene transcription is regulated by antagonistic effects between PITX2, Msx2, and factors expressed in the tooth epithelia. Paper-9149037.
Regulator of G protein signaling ( RGS) proteins are responsible for the rapid turnoff of G protein-coupled receptor signaling pathways. Paper-8363601.
RGS GAPs can modulate the frequency and duration of G-protein signaling and may constitute a new family of therapeutic targets. Paper-10512036.
Most RGS proteins are GTPase accelerating proteins (GAPs) for Gi and Gq class G protein alpha subunits, and thereby terminate signaling. Paper-8752719.
These include the transcription factors HESX1, PROP1, POU1F1, LHX3, LHX4, PITX1, PITX2, SOX2 and SOX3. Paper-12743863.
The main purpose of this study was to assess the proportion of FOXC1 and PITX2 mutations and copy number changes in 80 probands with ASD. Paper-15636891.
Furthermore, the LEF-1 promoter is differentially activated by PITX2 isoforms, which are co-expressed in dental epithelium. Paper-10787415.
One hundred twenty-six patients with ARM, representing 20 different probands, with FOXC1 and PITX2 alterations were included in the study. Paper-12388599.
Regulated exchange of HDAC1/ beta-catenin converts Pitx2 from repressor to activator, analogous to control of TCF/LEF1. Paper-9318167.
We conducted a quantitative analysis of RGS and G protein expression and devised computational models that describe their activity in vivo. Paper-10068644.
In both birds and mammals a conserved Nodal- Lefty- Pitx2 module exists that controls many aspects of asymmetric morphogenesis. Paper-13372383.
Structural assessment of PITX2, FOXC1, CYP1B1, and GJA1 genes in patients with Axenfeld-Rieger syndrome with developmental glaucoma. Paper-11820122.
Autosomal dominant cornea plana is not associated with pathogenic mutations in DCN, DSPG3, FOXC1, KERA, LUM, or PITX2. Paper-13282127.
We have examined the interaction of PITX2 isoforms with myocyte-enhancing factor 2A ( MEF2A), which is a known regulator of cardiac development. Paper-10616674.
ARS shows genetic heterogeneity and mutations of the two genes, PITX2 and FOXC1, are known to be associated with the pathogenesis. Paper-14120151.
DNA markers for candidate genes CYP1B1 on 2p22, PITX2 on 4q25, PAX6 on 11p13, MAF on 16q23 and FOXC1 on 6p25 were genotyped. Paper-13526897.
Human PRKC apoptosis WT1 regulator is a novel PITX2-interacting protein that regulates PITX2 transcriptional activity in ocular cells. Paper-14094135.
BACKGROUND: Axenfeld-Rieger syndrome ( ARS) is associated with mutations in the PITX2 gene that encodes a homeobox transcription factor. Paper-12087533.
RESULTS: The frequency of mutations in the FOXC1, GJA1, PITX2, and CYP1B1 genes in this study were 25%, 12.5%, 0% and 0%, respectively. Paper-11820122.
The ocular anomaly has been linked with mutations in genes PAX6, PITX2, PITX3 and CYP1B1, but the causal factor of PpS remains unknown. Paper-11286795.
As our understanding of RGS protein structure and function has developed, so has the realisation that they play roles beyond G-protein regulation. Paper-12152186.
LEF-1 and beta-catenin interactions with PITX2 provide new mechanisms for the regulation of PITX2 transcriptional activity. Paper-10787415.
Pitx2, a beta-catenin-regulated transcription factor, regulates the differentiation of outer root sheath cells cultured in vitro. Paper-13641502.
We observed that endogenous PITX1 and PITX2 isoforms from murine LbetaT2 gonadotrope cells could bind a highly conserved proximal cis-element. Paper-14323964.
METHODS: All coding exons of the FOXC1 and PITX2 genes were amplified by PCR from genomic DNA and subjected to direct DNA sequencing. Paper-12197507.
The major mechanism whereby RGS proteins negatively regulate G proteins is via the GTPase activating protein activity of their RGS domain. Paper-8363601.
These assays would be useful for dissecting the physiological modes of action of RGS proteins in controlling G-protein-mediated signaling machinery. Paper-10512042.
Regulators of G protein signaling ( RGS) proteins accelerate the intrinsic GTPase activity of Galpha subunits, and thus terminate G protein activation. Paper-9740969.
Glaucoma in only 18% of patients with either PITX2 or FOXC1 genetic defects responded to medical or surgical treatment (used solely or in combination). Paper-12388599.
Surprisingly, Msx2 binds to the bicoid element (5'-TAATCC-3') with a high specificity and competes with PITX2 for binding to this element. Paper-9149037.
We studied the role of MYOC, CYP1B1, and PITX2 in a population (n=60) affected with juvenile or early-onset glaucoma from the greater Toronto area. Paper-9154414.
This modulation of RGS protein action underlies the characteristic "relaxation" behavior of G-protein-gated K+ channels in native cardiac myocytes. Paper-10512042.
Recently, a bicoid-related homeobox transcription factor gene called RIEG has been cloned, characterized, and proven to cause the 4q25 linked RIEG. Paper-1362288.
This study examined the two genes known to cause Rieger syndrome, PITX2 and FOXC1, for mutations in five Brazilian families with Axenfeld-Rieger syndrome. Paper-9365616.
Our results may be useful for better understanding of the spectrum of PITX2 mutations and the role of PITX2 in the development and progression of ARS. Paper-13482193.
In contrast, expression of other MLL target genes such as Pitx2 or expression of anti-apoptotic BCL-2 failed to rescue hematopoietic-colony frequency. Paper-10561549.
New findings indicate that RGS proteins act not as dedicated inhibitors but, rather, as tightly regulated modulators and integrators of G protein signaling. Paper-9331374.
We show a new mechanism where LEF-1 expression is regulated through PITX2, LEF-1 and beta-catenin direct physical interactions. Paper-10787415.
The synergism was dependent on promoter context, because it required MEF2 binding sites and was not seen with two other PITX2 target promoters. Paper-10616674.
Functional interactions between FOXC1 and PITX2 underlie the sensitivity to FOXC1 gene dose in Axenfeld-Rieger syndrome and anterior segment dysgenesis. Paper-11356667.
Absence of PITX2, BARX1, and FOXC1 mutations in De Hauwere syndrome (Axenfeld-Rieger anomaly, hydrocephaly, hearing loss): a 25-year follow up. Paper-13258387.
Pitx2 is a member of the Pitx homeobox gene family, and in both amphioxus and ascidians Pitx gene expression is predominantly left sided. Paper-9309259.
BACKGROUND: Mutations in the PITX2 homeobox gene are known to contribute to Axenfeld-Rieger syndrome ( ARS), an autosomal-dominant developmental disorder. Paper-11361337.
More than 20 RGS proteins have been isolated, and there are indications that specific RGS proteins regulate specific G protein-coupled receptor pathways. Paper-8363601.
CONCLUSION: Rieger syndrome can -- in addition to PITX2 gene mutations and abnormalities at chromosome 13q14 -- be associated with PAX6 gene abnormalities. Paper-8811362.
G protein activity is controlled by the interplay between receptor- catalyzed activation and the inhibitory regulators of G protein signaling ( RGS) proteins. Paper-8752719.
We have identified a functional link between FOXC1 and PITX2 which we propose underpins the similar Axenfeld-Rieger phenotype caused by mutations of these genes. Paper-11356667.
A four-marker panel including PITX2, BMP4, FGF4, and C20orf55 was identified that resulted in improvement of outcome prediction compared with PITX2 alone. Paper-13561685.
In order to better understand the occurrence of glaucoma in ARS patients, we studied the PITX2 gene expression in human embryonic and fetal ocular tissue sections. Paper-12355135.
CONCLUSIONS: The results indicate that the PITX2 C-terminal domain has inhibitory activity and support the notion that ARS may also be caused by gain-of-function mutations. Paper-11361337.
To investigate the roles of RGS proteins during cartilage development, we overexpressed RGS4, RGS5, RGS7, and RGS10 in the chondrogenic cell line ATDC5. Paper-11310394.
Msx2 represses the Dlx2 promoter in CHO cells and coexpression of both PITX2 and Msx2 resulted in transcriptional antagonism of the Dlx2 promoter. Paper-9149037.
METHODS: The patients were examined for FOXC1 and PITX2 copy number changes and mutations using MLPA (multiplex ligation-dependent probe amplification) and direct sequencing. Paper-15636891.
Three recently described proteins, Ptx1, Ptx2, and Ptx3, define a new family of transcription factors, the Ptx subfamily, within the paired-like class of homeodomain factors. Paper-1887273.
Regulators of the G protein signalling ( RGS) pathway have been implicated in the control of a diverse array of cellular functions, including conidiation in filamentous fungi. Paper-12468478.
PITX2, beta-catenin and lymphoid enhancer factor ( LEF-1) are required for the inductive formation of several epithelial-derived organs, including teeth. Paper-10787415.
PURPOSE: To determine the prevalence of FOXC1 and PITX2 mutations and to assess clinical phenotypes in a cohort of German patients with Axenfeld-Rieger malformations. Paper-12197507.
The exact functions of these proteins remain mostly elusive, but RGS proteins such as RGS4 are involved in the regulation of G(i)-protein betagamma-subunit-gated K(+) channels. Paper-9666967.
Regulator of G protein signaling ( RGS) proteins increases the intrinsic GTPase activity of Galpha-subunits and are widely regarded as negative regulators of G protein signaling. Paper-13735023.
Because Pitx2, Msx2, and Dlx2 are expressed in the dental epithelium, we examined the transcriptional activity of PITX2 in concert with Msx2 and the Dlx2 promoter. Paper-9149037.
Haplotypic analysis of three Rieger syndrome regions in a large family with Axenfeld-Rieger syndrome excluded linkage to the 4q25 ( PITX2), 6p25 ( FOXC1), and 13q14 (RIEG2) regions. Paper-9365616.
Of these, eight showed highly significant hypermethylation in tumor tissue (p < 0.0001): GDNF, MTHFR, OPCML, TNFRSF25, TCF21, PAX8, PTPRN2 and PITX2. Paper-12945727.
In the present study, the expression of the Ptx1, Ptx2, and Ptx3 genes was characterized in the normal human pituitary and in the different types of human pituitary adenomas. Paper-1887273.
Our analysis indicates that the homeodomain and the adjacent inhibitory domain in PITX2 interact with the C-terminal leucine zipper domain of PAWR. Paper-14094135.
The PITX2 gene, on chromosome 4q25, and the FOXC1 gene, on chromosome 6p25, have been implicated in the different phenotypes of the syndrome through mutational events. Paper-11820122.
We conclude that increased activity of one PITX2 allele may be as physiologically disruptive as a mutation that nullifies a PITX2 allele, with either condition resulting in ARS. Paper-9038146.
Here we identify the paired-like homeobox transcription factors Pitx1 and Pitx2 as factors functionally activating the proximal human prolactin promoter (hPRL-164luc). Paper-9244684.
Deletion of a distal 800 bp segment of the LEF-1 promoter resulted in enhanced PITX2 activation, and increased synergistic activation in the presence of LEF-1. Paper-10787415.
In mice, Ptx1 and Ptx2 gene expression has been detected in the area of the pituitary primordium and is maintained throughout development in Rathke pouch and adult pituitary. Paper-1887273.
PITX2 activated while Msx2 unexpectedly repressed transcription of a TK-Bicoid luciferase reporter in a tooth epithelial cell line (LS-8) and CHO cell line. Paper-9149037.
In addition, the expression of Pitx2, a bicoid-type homeodomain transcription factor, was also increased by overexpression of beta-catenin in ORS cells cultured in vitro. Paper-13641502.
We found that a nodal/ lefty/ pitx2 gene cassette regulates left-right asymmetry in the sea urchin but that intriguingly, the expression of these genes is reversed compared to vertebrates. Paper-12669034.
Axenfeld-Rieger ocular dysgenesis is associated with mutations of the human PITX2 and FOXC1 genes, which encode transcription factors of the homeodomain and forkhead types, respectively. Paper-11356667.
As in patients carrying mutations in PITX2 and FOXC1, TGFbeta signal inactivation in NC cells leads to ocular defects characteristic of the human disorder Axenfeld-Rieger's anomaly. Paper-11280273.
Blocking N-cadherin function randomizes heart looping and alters the expression of Snail and Pitx2, later components of the molecular cascade that regulate left-right asymmetry. Paper-8490838.
Mutations in the homeobox transcription factor PITX2 result in Axenfeld-Rieger syndrome ( ARS), which is associated with anterior segment dysgenesis and an increased risk of glaucoma. Paper-14094135.
CONCLUSIONS: The findings in the present study clearly demonstrate that FOXC1 and PITX2 mutations are responsible for a significant proportion of Axenfeld-Rieger malformations in Germany. Paper-12197507.
I discuss the molecular mechanisms by which these phenomena might be explained including specific interactions between the RGS and G-protein coupled receptor, G-protein and effector. Paper-12152185.
Regulators of G-protein signalling ( RGS) proteins are a large and diverse family initially identified as GTPase activating proteins (GAPs) of heterotrimeric G-protein Galpha-subunits. Paper-12152186.
The first biochemical studies of RGS proteins have shown that they accelerate the GTPase activities of G-protein alpha subunits, thus driving G proteins into their inactive GDP-bound forms. Paper-956564.
Deletion analysis of Pitx2 revealed that the C-terminal 39-amino-acid tail represses DNA binding activity and is required for Pitx2- Pit-1 interaction and Pit-1 synergism. Paper-8279496.
In addition, no pathogenic sequence variations were found in DCN, DSPG3, LUM, PITX2 and FOXC1, which have also been implicated in corneal and anterior segment dysgenesis. Paper-13282127.
LEF-1 cannot autoregulate LEF-1 expression; however co-transfection of PITX2 and LEF-1 result in a synergistic activation of the 2.5 kb LEF-1 promoter. Paper-10787415.
In this study, we will attempt to give a brief review of the clinical features and the relevant diagnostic approaches, together with a detailed review of published PITX2 and FOXC1 mutations. Paper-14120151.
Exclusion of a PAX6, FOXC1, PITX2, and MYCN mutation in another patient with apple peel intestinal atresia, ocular anomalies and microcephaly and review of the literature. Paper-12720059.
INTRODUCTION: ARS is a multisystem, autosomal dominant disorder characterized by specific ocular and non-ocular anomalies sometimes caused by mutations in the transcription factor gene, PITX2. Paper-10326219.
In the present study, current medical therapies do not successfully lower intraocular pressure or prevent progression of glaucoma in patients with ARM who have FOXC1 or PITX2 alterations. Paper-12388599.
Opioids exert their physiologic effects via complex G protein-coupled receptor-signaling mechanisms, and RGS proteins are now known to tightly regulate the G protein signaling cycle. Paper-10748399.
Nkx2-5 may function locally as part of the laterality cascade, downstream of nodal and Pitx2, or it may direct asymmetric morphogenesis after laterality has been determined. Paper-2115758.
Structural and mutational analyses have characterized the RGS/G alpha interaction in detail, explaining the molecular mechanisms of the GTPase activating protein activity of RGS proteins. Paper-8363601.
FOXC1 and PITX2A physically interact, and this interaction requires crucial functional domains on both proteins: the C-terminal activation domain of FOXC1 and the homeodomain of PITX2. Paper-11356667.
Among these are a highly conserved Arp1 protein (likely part of a conserved dynactin complex), and Arp4 and Arp6 homologues (subunits of the chromatin-remodeling machinery). Paper-11153049.
Ultimately, PITX2 loss of function mutations have a compound effect: the reduced expression of PITX2- target genes coupled with the extensive activation of FOXC1-regulated targets. Paper-11356667.
Interplay between PITX2 and FOXC1 in the development of different anterior segment tissues may partly explain the phenotypic variability and the genetic heterogeneity characteristic of ASD. Paper-12567039.
These results demonstrate a promoter- and cell-specific functional interaction between PITX2 and MEF2A and suggest the possibility of coordinate control by these factors in the oral epithelium. Paper-10616674.
Axenfeld-Rieger syndrome ( ARS) and iridogoniodysgenesis syndrome ( IGDS) are clinically related autosomal dominant disorders which affect the anterior segment of the eye as well as non-ocular structures. Paper-1677181.
Here we confirm through targeted mutagenesis of RGS7 that these ET-identified residues are critical for RGS domain regulation and are likely to function as global determinants of RGS function. Paper-8695690.
In this review we discuss the classical experiments in the light of recent advances in the molecular understanding of left-right development, with a focus on the mediator role of the homeobox gene Pitx2. Paper-8276117.
Further structural and biochemical studies are needed for understanding the wide spectrum of clinical phenotypes caused by the increasing number of new PITX2 mutations found in ARS affected patients. Paper-12355135.
METHODS: Six members of a five-generation family with PA were extensively phenotyped and linkage analysis of candidate genes, namely, PAX6, PITX2, FOXC1, CYP1B1 and MAF, was performed. Paper-13526897.
This work ties both proteins into a common pathway and offers an explanation of why increased FOXC1 gene dosage produces a phenotype resembling that of PITX2 deletions and mutations. Paper-11356667.
In this review we discuss what has been learned so far about the role of RGS proteins in regulating G protein-coupled receptor signaling and point out areas that may be fruitful for future research. Paper-8363601.
G protein-coupled biological processes are important for an ever-increasing number of human diseases and require fine-tuning through accessory molecules such as the regulators of G protein signaling ( RGS). Paper-13577067.
Although we detected a number of variants, our candidate gene approach did not result in identification of mutations associated with AF in the coding regions of PITX2 or NKX2-5 in our well characterized AF cohort. Paper-15543426.
In addition, an alternative approach using transgenic animals expressing RGS-resistant G protein alpha subunits now highlights the contributions of RGS proteins to distinct signalling pathways in the heart. Paper-12462553.
Ptx1 and Ptx2 are expressed in the stomodeum and its derivatives including the pituitary, as well as in mesodermal derivatives, whereas Ptx3 is expressed in one neuronal lineage of the brain and in the eyes. Paper-8395505.
Yeast two-hybrid screening was performed using a cDNA library from a human trabecular meshwork primary cell line to detect novel PITX2- interacting proteins and study their role in ARS pathogenesis. Paper-14094135.
PURPOSE: To improve the understanding of Axenfeld-Rieger Malformation (ARM)-associated glaucoma and to determine the best glaucoma treatment for patients with ARM who have known genetic defects in FOXC1 or PITX2. Paper-12388599.
They share a 120 amino acid homology domain ( RGS domain), which exhibits GTPase accelerating activity for alpha-subunits of heterotrimeric G-proteins, and thus, are negative regulators of G-protein-mediated signalling. Paper-9666967.
Studies in animal models have shown that laterality decisions are mediated by a cascade of genes that lead to the asymmetric expression of Nodal, LEFTA, LEFTB and PITX2 in the lateral plate mesoderm. Paper-12045865.
Screening of DCN, DSPG3, FOXC1, KERA, LUM, and PITX2 revealed 12 previously described single nucleotide polymorphisms, 2 previously described duplications, and 1 previously described insertion. Paper-13282127.
In this review, the role of the ASD genes, PITX2 and FOXC1, is considered in relation to the embryology of the anterior segment, the biochemical function of these proteins, and their role in development and disease aetiology. Paper-12567039.
DNA was obtained from affected and unaffected subjects for the performance of a genome-wide linkage analysis as well as PCR amplification and sequencing of DCN, DSPG3, FOXC1, KERA, LUM, and PITX2. Paper-13282127.
RESULTS: A novel PITX2 mutation, c.840G>T, was identified in all affected members of the family with ARS that causes an amino acid substitution from tryptophan to cysteine at codon 86. Paper-13482193.
Msx1, Pax9, and Axin2 are involved in non-syndromic hypodontia, while genes such as Shh, Pitx2, Irf6, and p63 are considered to participate in syndromic genetic disorders, which include tooth agenesis. Paper-12849414.
Molecular phylogenetics show PitxA is most closely related to the Pitx1 and Pitx2 genes of jawed vertebrates, however resolution in the trees is insufficient to determine if PitxA is orthologous to a specific jawed vertebrate gene. Paper-9604202.
We isolated the first member of this family, Ptxl ( pituitary homeobox 1), through its DNA binding properties whereas a second related gene, Ptx2 ( RIEG), was identified by positional cloning as the causative gene for Rieger's syndrome. Paper-1599715.
RESULTS: We investigate the expression of conserved gene networks (involving bmp2, bmp4, eda, edar, fgf8, pax9, pitx2, runx2, shh and wnt7b) known to pattern iterative structures and teeth in other vertebrates. Paper-12899065.
METHODS: Clinical data were collected from patients with diagnosed ARM, in whom we had previously identified disease-causing mutations in either the FOXC1 or PITX2 genes, by examination of patient records and use of clinical questionnaires. Paper-12388599.
Sella turcica anomalies in association with craniofacial and dental aberrations, such as maxillary retrognathia, skeletal Class III relationship and hypoplasia of teeth, might be important indicators for ARS caused by PITX2 mutation. Paper-12994169.
Here, we present direct evidence for an earlier proposal [7] that Nodal signalling specifically represses expression of SnR in left lateral mesoderm, and thus ensures its normal confinement to the right, while activating Pitx2 on the left. Paper-1904925.
The entire coding sequences, including intron-exon boundaries, of the genes PITX2 and NKX2-5 were screened for genetic variants by means of initial polymerase chain reaction followed by DNA sequencing in 96 patients with idiopathic AF. Paper-15543426.
In the anterior eye, TGFbeta2 released from the lens is required for the expression of transcription factors Pitx2 and Foxc1 in the NC-derived cornea and in the chamber-angle structures of the eye that control intraocular pressure. Paper-11280273.
New findings in yeast, however, demonstrate a major role for a DEP domain in mediating the interaction of an RGS protein to the C-terminal tail of a GPCR, thus placing RGS in close proximity with its substrate G protein alpha subunit. Paper-12247952.
Recent data show that the 519-amino acid RGS3, the only RGS protein with an additional G protein betagamma dimer binding domain, largely alters the signalling of G(i) proteins to the monomeric GTPases Rac1 and RhoA in cardiomyocytes. Paper-12462553.
This quantitative real-time polymerase chain reaction method is established for the 19 reported mouse RGS genes and is used to study the tissue distribution of the R4 family of RGS genes and the diurnal regulation of RGS16 in mouse liver. Paper-10512036.
Here, we report that the bicoid-related transcription factor Pitx2 is rapidly induced by the Wnt/Dvl/ beta-catenin pathway and is required for effective cell-type-specific proliferation by directly activating specific growth-regulating genes. Paper-9318167.
We also show that synergistic activation of hPRL-164luc by Pitx2 and Pit-1 requires the integrity of the B2 Pitx binding site, and at least one of the P1 and P2 Pit-1 response elements. Paper-9244684.
By a combination of single-strand conformation polymorphism and direct cycle sequencing, MYOC mutations were detected in 8 (13.3%) of the 60 individuals, CYP1B1 mutations were detected in 3 (5%) of the 60 individuals, and no PITX2 mutations were detected. Paper-9154414.
We have previously shown that Pitx2 (also called Ptx2 and RIEG) transactivates a reporter gene containing a bicoid enhancer and synergistically transactivates the prolactin promoter in the presence of the POU homeodomain protein Pit-1. Paper-8279496.
Endogenous PAWR and PITX2 were found to be located in the nucleus of ocular cells and to co-localize in the mesenchyme of the iridocorneal angle of the developing mouse eye, consistent with a role in the development of the anterior segment of the eye. Paper-14094135.
In somatolactotroph GH4C1 cells, basal proximal hPRL promoter activity was inhibited by a Pitx2 dominant-negative form in a dose-dependent manner, whereas binding disruptive mutations in the Pitx sites significantly reduced basal activity of the promoter. Paper-9244684.
Control of chondrocyte differentiation is attained, in part, through G-protein signaling, but the functions of the RGS family of genes, well known to control G-protein signaling at the Galpha subunit, have not been studied extensively in chondrogenesis. Paper-11310394.
The development of this asymmetry is controlled by a molecular pathway that includes the signalling molecule Nodal and the transcription factor Pitx2, proteins encoded by genes that are predominantly expressed on the left side of all vertebrate embryos studied to date. Paper-9309259.
CONCLUSIONS: Patients with FOXC1 mutations have the mildest prognosis for glaucoma development, whereas patients with PITX2 defects and patients with FOXC1 duplication have a more severe prognosis for glaucoma development than do patients with FOXC1 mutations. Paper-12388599.
Our in situ hybridization results obtained on human embryonic and fetal ocular tissue sections constitute the first molecular histological data providing an explanation for the occurrence of precocious glaucoma in human patients affected by ARS caused by PITX2 mutations. Paper-12355135.
The experimental strategies developed in kinetic studies of interactions between RGS9 isoforms with G proteins of the Gi subfamily provide a useful framework for conducting similar studies with essentially any regulator of G-protein signaling ( RGS) protein-G-protein pair. Paper-10857727.
These disease/gene matches include the oculorenal syndrome and PAX2; aniridia and PAX6; Rieger syndrome and RIEG1/ PITX2; cyclopia and Sonic hedgehog; cone-rod dystrophy, Leber's congenital amaurosis and CRX; and recessive septooptic dysplasia and HESX1. Paper-8266460.
Regulator of G protein signalling ( RGS) proteins are GTPase- activating proteins for heterotrimeric G protein alpha subunits, and are therefore physiologically and pathophysiologically important negative regulators of G-protein-coupled receptor signalling in the cardiovascular system. Paper-12462553.
An emphasis is placed on heterotrimeric G protein signaling with a discussion of the specific heterotrimeric G-proteins involved in lymphocyte chemotaxis and motility and the role of regulator of G protein signaling ( RGS) proteins in controlling the activation of downstream effectors. Paper-12080248.
Here, we present results from a multicenter study investigating whether PITX2 and other candidate DNA methylation markers predict outcome in node-positive, estrogen receptor-positive, HER-2-negative breast cancer patients who received adjuvant anthracycline-based chemotherapy. Paper-13561685.
There have been more than 20 RGS proteins reported in the literature, and multiple RGS proteins have been shown to negatively regulate G protein-mediated opioid signaling, facilitate opioid receptor desensitization and internalization, and affect the rate at which opioid tolerance develops. Paper-10748399.
Furthermore, beta-catenin in combination with PITX2 synergistically activates the LEF-1 promoter and this activation is independent of the Wnt-responsive element. beta-catenin directly interacts with PITX2 to synergistically regulate LEF-1 expression. Paper-10787415.
An article in this issue of Molecular Pharmacology (Yost et al., p. 812) describes the use of an innovative fluorescent cell imaging technique to study interactions of the G protein beta(5) subunit with a panel of Ggamma subunits as well as regulator of G protein signaling ( RGS) proteins that contain a Ggamma-like subdomain. Paper-12498262.
The current spectrum of intragenic FOXC1 and PITX2 mutations was extended considerably, the identified copy number changes were fine mapped, the smallest FOXC1 and PITX2 deletions reported so far were identified, and the need for dedicated copy number screening of the FOXC1 and PITX2 genomic landscape was emphasized. Paper-15636891.
Promising DNA methylation biomarkers include the use of methylated GSTP1 for aiding the early diagnosis of prostate cancer, methylated PITX2 for predicting outcome in lymph node-negative breast cancer patients and methylated MGMT in predicting benefit from alkylating agents in patients with glioblastomas. Paper-13606396.
These synonyms are used for gene PITX2 (paired-like homeodomain 2): Solurshin, RS, RIEG bicoid-related homeobox transcription factor, RIEG1, RIEG, RGS, PTX2, Pituitary homeobox 2, Paired-like homeodomain transcription factor 2, Otlx2, MGC20144, MGC111022, IRID2, IHG2, IGDS2, IGDS, IDG2, Homeobox protein PITX2, Brx1, ARP1, ALL1-responsive protein ARP1.
These accession numbers are used for gene PITX2: Q3KQX9 (UNIPROT__AC), O60578 (UNIPROT__AC), BX380370 (NCBI_GENBANK__AC), BP372081 (NCBI_GENBANK__AC).
PITX2 is a homologue of unc-30 (UNCoordinated) from Caenorhabditis elegans.
PITX2 is a homologue of Ptx1 (CG1447 gene product from transcript CG1447-RC) from Drosophila melanogaster.
PITX2 is a homologue of PITX2 (paired-like homeodomain 2) from Pan troglodytes.
PITX2 is a homologue of PITX2 (paired-like homeodomain 2) from Canis lupus familiaris.
PITX2 is a homologue of PITX2 (paired-like homeodomain 2) from Bos taurus.
PITX2 is a homologue of PITX2 (paired-like homeodomain 2) from Gallus gallus.
PITX2 is a homologue of Pitx2 (paired-like homeodomain transcription factor 2) from Mus musculus.
PITX2 is a homologue of Pitx2 (paired-like homeodomain 2) from Rattus norvegicus.
PITX2 is a homologue of pitx2 (paired-like homeodomain transcription factor 2) from Danio rerio.
PITX2 is a homologue of AgaP_AGAP000190 (AGAP000190-PA) from Anopheles gambiae str. PEST.
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iHOP - Information Hyperlinked over Proteins .
Concept & Implementation by Robert Hoffmann.