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Article ; Online: Distinct epithelial-to-mesenchymal transitions induced by

Gjelaj, Ersa / Hamel, Paul A

2021 Volume 134, Issue 4

Abstract: ... The most ... ...

Abstract	The most common
MeSH term(s)	Class I Phosphatidylinositol 3-Kinases/genetics ; Epithelial-Mesenchymal Transition/genetics ; Humans ; Phosphatidylinositol 3-Kinase ; Phosphatidylinositol 3-Kinases/genetics ; Phosphatidylinositol 3-Kinases/metabolism ; Signal Transduction
Chemical Substances	Class I Phosphatidylinositol 3-Kinases (EC 2.7.1.137) ; PIK3CA protein, human (EC 2.7.1.137) ; PIK3CB protein, human (EC 2.7.1.137) ; Phosphatidylinositol 3-Kinase (EC 2.7.1.137)
Language	English
Publishing date	2021-02-17
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.248294
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Article ; Online: Nonsynonymous Mutations in Intellectual Disability and Autism Spectrum Disorder Gene PTCHD1 Disrupt

Xie, Connie T Y / Pastore, Stephen F / Vincent, John B / Frankland, Paul W / Hamel, Paul A

Cells

2024 Volume 13, Issue 2

Abstract: ... ...

Abstract	PTCHD1
MeSH term(s)	Humans ; Intellectual Disability/genetics ; Autism Spectrum Disorder/genetics ; Glycosylation ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mutation/genetics ; Protein Stability
Chemical Substances	Membrane Proteins ; PTCHD1 protein, human
Language	English
Publishing date	2024-01-21
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells13020199
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Article ; Online: Neuronal transcription of autism gene PTCHD1 is regulated by a conserved downstream enhancer sequence.

Pastore, Stephen F / Muhammad, Tahir / Stan, Cassandra / Frankland, Paul W / Hamel, Paul A / Vincent, John B

Scientific reports

2023 Volume 13, Issue 1, Page(s) 20391

Abstract: Patched domain-containing 1 (PTCHD1) is a well-established susceptibility gene for autism spectrum disorder (ASD) and intellectual disability (ID). Previous studies have suggested that alterations in the dosage of PTCHD1 may contribute to the etiology of ...

Abstract	Patched domain-containing 1 (PTCHD1) is a well-established susceptibility gene for autism spectrum disorder (ASD) and intellectual disability (ID). Previous studies have suggested that alterations in the dosage of PTCHD1 may contribute to the etiology of both ASD and ID. However, there has not yet been a thorough investigation regarding mechanisms that regulate PTCHD1 expression. We sought to characterize the Ptchd1 promoter in a mouse neuronal model, as well as to identify and validate cis regulatory elements. We defined specific regions of the Ptchd1 promoter essential for robust expression in P19-induced neurons. Evolutionarily-conserved putative transcription factor binding sites within these regions were subsequently identified. Using a pairwise comparison of chromatin accessibility between mouse forebrain and liver tissues, a candidate regulatory region, ~ 9.1 kbp downstream of the Ptchd1 stop codon was defined. This region harbours two ENCODE-predicted enhancer cis-regulatory elements. Further, using DNase footprint analysis, a putative YY1-binding motif was also identified. Genomic deletion of the entire 8 kbp downstream open chromatin region attenuated Ptchd1 transcription by over 60% in our neuronal model, corroborating its predicted regulatory function. This study provides mechanistic insights related to the expression of PTCHD1, and provides important context to interpret genetic and genomic variation at this locus which may influence neurodevelopment.
MeSH term(s)	Animals ; Mice ; Autistic Disorder/genetics ; Autism Spectrum Disorder/genetics ; Membrane Proteins/metabolism ; Neurons/metabolism ; Conserved Sequence ; Enhancer Elements, Genetic ; Chromatin/genetics
Chemical Substances	Membrane Proteins ; Chromatin ; Ptchd1 protein, mouse
Language	English
Publishing date	2023-11-21
Publishing country	England
Document type	Journal Article
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-023-46673-0
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Article ; Online: The protein-specific activities of the transmembrane modules of Ptch1 and Ptch2 are determined by their adjacent protein domains.

Fleet, Andrew J / Hamel, Paul A

The Journal of biological chemistry

2018 Volume 293, Issue 43, Page(s) 16583–16595

Abstract: Signaling through the Hedgehog (Hh) pathway is mediated by the Patched (Ptch) family of proteins. Although the vertebrate Ptch proteins Ptch1 and Ptch2 harbor two closely related transmembrane modules related to sterol-sensing domains (SSDs), the role of ...

Abstract	Signaling through the Hedgehog (Hh) pathway is mediated by the Patched (Ptch) family of proteins. Although the vertebrate Ptch proteins Ptch1 and Ptch2 harbor two closely related transmembrane modules related to sterol-sensing domains (SSDs), the role of these closely related receptors in the Hh pathway are not equivalent. Ptch1 is essential for development and appears to be the principal receptor mediating responses to Hh ligands, whereas Ptch2 is nonessential, and its role in Hh-signaling remains ambiguous. We hypothesized that the SSDs of the Ptch proteins function as generic modules whose protein-specific activities are determined by the adjacent cytoplasmic and luminal domains. We first showed that individual N-terminal and C-terminal halves of Ptch1 associated noncovalently to mediate ligand-dependent regulation of Hh signaling. The analogous regions of Ptch2 also interacted noncovalently but did not repress the Hh pathway. However, the SSD of Ptch2 were capable of repressing Hh signaling, as determined using chimeric proteins where the SSDs of Ptch1 were replaced by those from Ptch2. Replacement of the SSDs of Ptch1 with the analogous regions from the cholesterol transporter NPC1 failed to produce a chimeric protein capable of Hh repression. Further refinement of the specific regions in Ptch1 and Ptch2 revealed that specific cytoplasmic domains of Ptch1 were necessary but not sufficient for repression of Hh signaling and that the two principal luminal domains of Ptch1 and Ptch2 were interchangeable. These data support a model where the SSDs of the Ptch family proteins exhibit generic activities and that the adjacent cytoplasmic and luminal domains determine their protein-specific activities.
MeSH term(s)	Animals ; Cell Membrane/genetics ; Cell Membrane/metabolism ; Hedgehog Proteins/genetics ; Hedgehog Proteins/metabolism ; Humans ; Mice ; Mice, Knockout ; Patched-1 Receptor/chemistry ; Patched-1 Receptor/genetics ; Patched-1 Receptor/metabolism ; Patched-2 Receptor/chemistry ; Patched-2 Receptor/genetics ; Patched-2 Receptor/metabolism ; Protein Binding ; Protein Domains ; Signal Transduction
Chemical Substances	Hedgehog Proteins ; Patched-1 Receptor ; Patched-2 Receptor ; Ptch1 protein, mouse ; Ptch2 protein, mouse
Language	English
Publishing date	2018-08-30
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA118.004478
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Article ; Online: PTCHD1

Pastore, Stephen F / Ko, Sangyoon Y / Frankland, Paul W / Hamel, Paul A / Vincent, John B

Genes

2022 Volume 13, Issue 3

Abstract: Over the last one and a half decades, copy number variation and whole-genome sequencing studies have illuminated the considerable genetic heterogeneity that underlies the etiologies of autism spectrum disorder (ASD) and intellectual disability (ID). ... ...

Abstract	Over the last one and a half decades, copy number variation and whole-genome sequencing studies have illuminated the considerable genetic heterogeneity that underlies the etiologies of autism spectrum disorder (ASD) and intellectual disability (ID). These investigations support the idea that ASD may result from complex interactions between susceptibility-related genetic variants (single nucleotide variants or copy number variants) and the environment. This review outlines the identification and neurobiological characterization of two such genes located in Xp22.11, Patched domain-containing 1 (
MeSH term(s)	Animals ; Autism Spectrum Disorder/genetics ; DNA Copy Number Variations ; Humans ; Intellectual Disability/genetics ; Membrane Proteins/genetics ; Mice ; Quality of Life
Chemical Substances	Membrane Proteins ; PTCHD1 protein, human ; Ptchd1 protein, mouse
Language	English
Publishing date	2022-03-17
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2527218-4
ISSN	2073-4425 ; 2073-4425
ISSN (online)	2073-4425
ISSN	2073-4425
DOI	10.3390/genes13030527
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Article: PTCHD1: Identification and Neurodevelopmental Contributions of an Autism Spectrum Disorder and Intellectual Disability Susceptibility Gene

Pastore, Stephen F. / Ko, Sangyoon Y. / Frankland, Paul W. / Hamel, Paul A. / Vincent, John B.

Genes. 2022 Mar. 17, v. 13, no. 3

2022

Abstract	Over the last one and a half decades, copy number variation and whole-genome sequencing studies have illuminated the considerable genetic heterogeneity that underlies the etiologies of autism spectrum disorder (ASD) and intellectual disability (ID). These investigations support the idea that ASD may result from complex interactions between susceptibility-related genetic variants (single nucleotide variants or copy number variants) and the environment. This review outlines the identification and neurobiological characterization of two such genes located in Xp22.11, Patched domain-containing 1 (PTCHD1), and its antisense lncRNA PTCHD1-AS. Animal models of Ptchd1 disruption have recapitulated a subset of clinical symptoms related to ASD as well as to ID. Furthermore, these Ptchd1 mouse knockout studies implicate the expression of Ptchd1 in both the thalamic and the hippocampal brain regions as being crucial for proper neurodevelopment and cognitive function. Altered kynurenine metabolic signalling has been postulated as a disease mechanism in one of these animal studies. Additionally, ASD patient-derived induced pluripotent stem cells (iPSCs) carrying a copy number loss impacting the antisense non-coding RNA PTCHD1-AS have been used to generate 2D neuronal cultures. While copy number loss of PTCHD1-AS does not affect the transcription of PTCHD1, the neurons exhibit diminished miniature excitatory postsynaptic current frequency, supporting its role in ASD etiology. A more thorough understanding of risk factor genes, such as PTCHD1 and PTCHD1-AS, will help to clarify the intricate genetic and biological mechanisms that underlie ASD and ID, providing a foundation for meaningful therapeutic interventions to enhance the quality of life of individuals who experience these conditions.
Keywords	autism ; brain ; cognition ; copy number variation ; etiology ; genes ; genetic heterogeneity ; kynurenine ; mice ; neurodevelopment ; neurons ; non-coding RNA
Language	English
Dates of publication	2022-0317
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2527218-4
ISSN	2073-4425
ISSN	2073-4425
DOI	10.3390/genes13030527
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Article ; Online: Oestrogen receptor-alpha regulates non-canonical Hedgehog-signalling in the mammary gland.

Okolowsky, Nadia / Furth, Priscilla A / Hamel, Paul A

Developmental biology

2014 Volume 391, Issue 2, Page(s) 219–229

Abstract: Mesenchymal dysplasia (mes) mice harbour a truncation in the C-terminal region of the Hh-ligand receptor, Patched-1 (mPtch1). While the mes variant of mPtch1 binds to Hh-ligands with an affinity similar to that of wild type mPtch1 and appears to normally ...

Abstract	Mesenchymal dysplasia (mes) mice harbour a truncation in the C-terminal region of the Hh-ligand receptor, Patched-1 (mPtch1). While the mes variant of mPtch1 binds to Hh-ligands with an affinity similar to that of wild type mPtch1 and appears to normally regulate canonical Hh-signalling via smoothened, the mes mutation causes, among other non-lethal defects, a block to mammary ductal elongation at puberty. We demonstrated previously Hh-signalling induces the activation of Erk1/2 and c-src independently of its control of smo activity. Furthermore, mammary epithelial cell-directed expression of an activated allele of c-src rescued the block to ductal elongation in mes mice, albeit with delayed kinetics. Given that this rescue was accompanied by an induction in estrogen receptor-alpha (ERα) expression and that complex regulatory interactions between ERα and c-src are required for normal mammary gland development, it was hypothesized that expression of ERα would also overcome the block to mammary ductal elongation at puberty in the mes mouse. We demonstrate here that conditional expression of ERα in luminal mammary epithelial cells on the mes background facilitates ductal morphogenesis with kinetics similar to that of the MMTV-c-src(Act) mice. We demonstrate further that Erk1/2 is activated in primary mammary epithelial cells by Shh-ligand and that this activation is blocked by the inhibitor of c-src, PP2, is partially blocked by the ERα inhibitor, ICI 182780 but is not blocked by the smo-inhibitor, SANT-1. These data reveal an apparent Hh-signalling cascade operating through c-src and ERα that is required for mammary gland morphogenesis at puberty.
MeSH term(s)	Animals ; Cell Line ; Enzyme Activation ; Epithelial Cells ; Estradiol/analogs & derivatives ; Estradiol/pharmacology ; Estrogen Antagonists/pharmacology ; Estrogen Receptor alpha/antagonists & inhibitors ; Estrogen Receptor alpha/physiology ; Extracellular Signal-Regulated MAP Kinases/metabolism ; Female ; Fibrocystic Breast Disease/genetics ; Fulvestrant ; HEK293 Cells ; Hedgehog Proteins/metabolism ; Humans ; Mammary Glands, Animal/cytology ; Mammary Glands, Animal/growth & development ; Mammary Glands, Animal/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Morphogenesis ; Patched Receptors ; Patched-1 Receptor ; Piperazines/pharmacology ; Proto-Oncogene Proteins pp60(c-src)/antagonists & inhibitors ; Pyrazoles/pharmacology ; Pyrimidines/pharmacology ; Receptors, Cell Surface/genetics ; Receptors, G-Protein-Coupled/antagonists & inhibitors ; Receptors, G-Protein-Coupled/physiology ; Signal Transduction/genetics ; Smoothened Receptor
Chemical Substances	AG 1879 ; Estrogen Antagonists ; Estrogen Receptor alpha ; Hedgehog Proteins ; PTCH1 protein, human ; Patched Receptors ; Patched-1 Receptor ; Piperazines ; Ptch1 protein, mouse ; Pyrazoles ; Pyrimidines ; Receptors, Cell Surface ; Receptors, G-Protein-Coupled ; SANT-1 compound ; Shh protein, mouse ; Smo protein, mouse ; Smoothened Receptor ; Fulvestrant (22X328QOC4) ; Estradiol (4TI98Z838E) ; Proto-Oncogene Proteins pp60(c-src) (EC 2.7.10.2) ; Extracellular Signal-Regulated MAP Kinases (EC 2.7.11.24)
Language	English
Publishing date	2014-04-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1114-9
ISSN	1095-564X ; 0012-1606
ISSN (online)	1095-564X
ISSN	0012-1606
DOI	10.1016/j.ydbio.2014.04.007
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Article: Oestrogen receptor-alpha regulates non-canonical Hedgehog-signalling in the mammary gland

Okolowsky, Nadia / Furth, Priscilla A / Hamel, Paul A

Developmental biology. 2014 July 15, v. 391, no. 2

2014

Abstract	Mesenchymal dysplasia (mes) mice harbour a truncation in the C-terminal region of the Hh-ligand receptor, Patched-1 (mPtch1). While the mes variant of mPtch1 binds to Hh-ligands with an affinity similar to that of wild type mPtch1 and appears to normally regulate canonical Hh-signalling via smoothened, the mes mutation causes, among other non-lethal defects, a block to mammary ductal elongation at puberty. We demonstrated previously Hh-signalling induces the activation of Erk1/2 and c-src independently of its control of smo activity. Furthermore, mammary epithelial cell-directed expression of an activated allele of c-src rescued the block to ductal elongation in mes mice, albeit with delayed kinetics. Given that this rescue was accompanied by an induction in estrogen receptor-alpha (ERα) expression and that complex regulatory interactions between ERα and c-src are required for normal mammary gland development, it was hypothesized that expression of ERα would also overcome the block to mammary ductal elongation at puberty in the mes mouse. We demonstrate here that conditional expression of ERα in luminal mammary epithelial cells on the mes background facilitates ductal morphogenesis with kinetics similar to that of the MMTV-c-srcAct mice. We demonstrate further that Erk1/2 is activated in primary mammary epithelial cells by Shh-ligand and that this activation is blocked by the inhibitor of c-src, PP2, is partially blocked by the ERα inhibitor, ICI 182780 but is not blocked by the smo-inhibitor, SANT-1. These data reveal an apparent Hh-signalling cascade operating through c-src and ERα that is required for mammary gland morphogenesis at puberty.
Keywords	alleles ; epithelial cells ; epithelium ; estrogens ; mammary development ; mammary glands ; mice ; morphogenesis ; mutation ; puberty
Language	English
Dates of publication	2014-0715
Size	p. 219-229.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1114-9
ISSN	1095-564X ; 0012-1606
ISSN (online)	1095-564X
ISSN	0012-1606
DOI	10.1016/j.ydbio.2014.04.007
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Article ; Online: Wnt-signalling in the embryonic mammary gland.

Boras-Granic, Kata / Hamel, Paul A

Journal of mammary gland biology and neoplasia

2013 Volume 18, Issue 2, Page(s) 155–163

Abstract: The first member of the Wnt-family ligands was identified 30 years ago as a factor in mouse mammary tumours whose expression was deregulated due to the promoter activity emanating from the proximal integration of the Mouse Mammary Tumour Virus genome ( ... ...

Abstract	The first member of the Wnt-family ligands was identified 30 years ago as a factor in mouse mammary tumours whose expression was deregulated due to the promoter activity emanating from the proximal integration of the Mouse Mammary Tumour Virus genome (Nusse and Varmus, Embo J 31:2670-84, 2012). The Wnt-ligands invoke a number of molecular-genetic signalling cascades fundamental to the patterning of developing tissues and organs during embryogenesis as well as during postnatal development. The Wnt-signalling cascade that controls the activities of β-catenin and the T-cell Factor (Tcf)/Lympoid enhancer factor (Lef1) plays a fundamental role in control of all stages of embryonic mammary gland development. We provide here a brief overview of the known aspects of Wnt-signalling activities in the embryonic mammary gland and its interactions with other signalling cascades in this developing tissue.
MeSH term(s)	Animals ; Female ; Gene Expression Regulation, Developmental ; Humans ; Mammary Glands, Animal/embryology ; Mammary Glands, Animal/metabolism ; Mammary Glands, Human/embryology ; Mammary Glands, Human/metabolism ; Wnt Proteins/genetics ; Wnt Proteins/metabolism ; Wnt Signaling Pathway/physiology
Chemical Substances	Wnt Proteins
Language	English
Publishing date	2013-05-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1327345-0
ISSN	1573-7039 ; 1083-3021
ISSN (online)	1573-7039
ISSN	1083-3021
DOI	10.1007/s10911-013-9280-x
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Article ; Online: Distinct effects of the mesenchymal dysplasia gene variant of murine Patched-1 protein on canonical and non-canonical Hedgehog signaling pathways.

Harvey, Malcolm C / Fleet, Andrew / Okolowsky, Nadia / Hamel, Paul A

The Journal of biological chemistry

2014 Volume 289, Issue 15, Page(s) 10939–10949

Abstract: Hedgehog (Hh) signaling requires regulation of the receptor Patched-1 (Ptch1), which, in turn, regulates Smoothened activity (canonical Hh signaling) as well as other non-canonical signaling pathways. The mutant Ptch1 allele mesenchymal dysplasia (mes), ... ...

Abstract	Hedgehog (Hh) signaling requires regulation of the receptor Patched-1 (Ptch1), which, in turn, regulates Smoothened activity (canonical Hh signaling) as well as other non-canonical signaling pathways. The mutant Ptch1 allele mesenchymal dysplasia (mes), which truncates the Ptch1 C terminus, produces a limited spectrum of developmental defects in mice as well as deregulation of canonical Hh signaling in some, but not all, affected tissues. Paradoxically, mes suppresses canonical Hh signaling and binds to Hh ligands with an affinity similar to wild-type mouse Ptch1 (mPtch1). We characterized the distinct activities of the mes variant of mPtch1 mediating Hh signaling through both canonical and non-canonical pathways. We demonstrated that mPtch1 bound c-src in an Hh-regulated manner. Stimulation with Sonic Hedgehog (Shh) of primary mammary mesenchymal cells from wild-type and mes animals activated Erk1/2. Although Shh activated c-src in wild-type cells, c-src was constitutively activated in mes mesenchymal cells. Transient assays showed that wild-type mPtch1, mes, or mPtch1 lacking the C terminus repressed Hh signaling in Ptch1-deficient mouse embryo fibroblasts and that repression was reversed by Shh, revealing that the C terminus was dispensable for mPtch1-dependent regulation of canonical Hh signaling. In contrast to these transient assays, constitutively high levels of mGli1 but not mPtch1 were present in primary mammary mesenchymal cells from mes mice, whereas the expression of mPtch1 was similarly induced in both mes and wild-type cells. These data define a novel signal transduction pathway involving c-src that is activated by the Hh ligands and reveals the requirement for the C terminus of Ptch in regulation of canonical and non-canonical Hh signaling pathways.
MeSH term(s)	Animals ; CSK Tyrosine-Protein Kinase ; Cell Line, Tumor ; Cells, Cultured ; Culture Media, Conditioned ; Gene Expression Regulation, Enzymologic ; HEK293 Cells ; Hedgehog Proteins/metabolism ; Humans ; Ligands ; Mice ; Mice, Inbred C57BL ; Patched Receptors ; Patched-1 Receptor ; Phosphorylation ; Protein Binding ; Protein Structure, Tertiary ; Receptors, Cell Surface/metabolism ; Signal Transduction ; src-Family Kinases/metabolism
Chemical Substances	Culture Media, Conditioned ; Hedgehog Proteins ; Ligands ; PTCH1 protein, human ; Patched Receptors ; Patched-1 Receptor ; Ptch1 protein, mouse ; Receptors, Cell Surface ; CSK Tyrosine-Protein Kinase (EC 2.7.10.2) ; src-Family Kinases (EC 2.7.10.2) ; CSK protein, human (EC 2.7.10.23)
Language	English
Publishing date	2014-02-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M113.514844
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