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Validated All-in-One™ qPCR Primer for VHL(NM_000551.3) Search again
Product ID:
HQP055454
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
HRCA1, RCA1, VHL1, pVHL
Gene Description:
von Hippel-Lindau tumor suppressor
Target Gene Accession:
NM_000551.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
Von Hippel-Lindau syndrome (VHL) is a dominantly inherited familial cancer syndrome predisposing to a variety of malignant and benign tumors. A germline mutation of this gene is the basis of familial inheritance of VHL syndrome. The protein encoded by this gene is a component of the protein complex that includes elongin B, elongin C, and cullin-2, and possesses ubiquitin ligase E3 activity. This protein is involved in the ubiquitination and degradation of hypoxia-inducible-factor (HIF), which is a transcription factor that plays a central role in the regulation of gene expression by oxygen. RNA polymerase II subunit POLR2G/RPB7 is also reported to be a target of this protein. Alternatively spliced transcript variants encoding distinct isoforms have been observed.
Gene References into function
- Expression of the von Hippel-Lindau gene protein in breast cancer tissue.
- VHL-dependent sensitization of RCC cells to TNF-alpha-mediated killing may contribute to VHL's growth-suppressive function
- Erythropoietin, tumours and the von Hippel-Lindau gene: towards identification of mechanisms and dysfunction of oxygen sensing.
- Role in regulation of cell growth.
- Inactivation of the VHL tumor suppressor gene is a genetic change in the tumorigenic pathway of clear-cell renal cell carcinoma and may occur at an early or first step in the tumorigenic pathway rather than as a late event.
- The Chuvash polycythemia gene is identified as the VHL gene with a point mutation that disrupts VHL function, causing a failure to degrade HIF-1 alpha and upregulation of downstream target genes such as EPO.
- A novel point mutation in the VHL gene (406 T-->G) was found in a patient with multiple recurrent chromaffin paragangliomas.
- structure of an HIF-1alpha-pVHL complex determined; role of hydroxyproline
- mutation in renal cell carcinoma
- VHL-mediated hypoxia regulation of cyclin D1 in renal carcinoma cells.
- molecular basis for stabilization by components of VHL ubiquitin ligase
- crystal structure and basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL
- Down regulation of HIF-1 by VHL protein is associated with tumorigenesis of clear cell carcinoma of the kidney
- Identification of cyclin D1 and other novel targets for the von Hippel-Lindau tumor suppressor gene by expression array analysis and investigation of cyclin D1 genotype as a modifier in von Hippel-Lindau disease.
- Functional analysis of the VHL tumor suppressor gene promoter sheds light on the developmental regulation of VHL expression, molecular pathology of epigenetic silencing of VHL in tumorigenesis, and suggests a link between Sp1, VHL, and nephrogenesis.
- Deletions of the entire VHL gene have occurred in von Hippel-Lindau syndrome patients from Poland.
- VHL protein has a role in protein stabilization in human kidney
- REVIEW: Molecular basis of the VHL hereditary cancer syndrome
- The binding of pVHL to HIF is governed by the enzymatic hydroxylation of conserved prolyl residues within peptidic motifs present in the HIFalpha family members.
- Review. The von Hippel-Lindau tumor suppressor protein regulates hypoxia-inducible gene transcription. It is a subunit of an E3 ubiquitin ligase targeting HIFalpha subunits.
- Direct sequencing analyses revealed that the tumors exhibited frameshift mutations and in some cases loss of heterozygosity at the VHL gene locus.
- propose that mutations of the VHL gene represent an important cause of pediatric sporadic polycythemias with an inappropriately high serum erythropoietin concentration
- P81S germline mutation in a German Von Hippel-Lindau disease type 2C family with the previously identified L188V mutation; co-segregation of these two mutations with the disease
- Von Hippel-Lindau tumor suppressor protein transforms human neuroblastoma cells into functional neuron-like cells.
- VHL regulates protein stability and the transactivation function of the hypoxia-inducible factor-1alpha
- HIF-1 binds to VHL in a specific binding site
- BRCA1 AND VHL LOH is infrequent in sporadic breast carcinoma.
- role for pVHL in the regulation of microtubule dynamics and potentially provide a link between this function of pVHL and the pathogenesis of haemangioblastoma and phaeochromocytoma in the context of VHL disease
- models for function of this protein and Hippel-Lindau disease
- identification of complex with E3 ligase as target of splice variants of HIF-3 alpha locus
- mutation not a common means of VHL inactivation in non-small-cell lung cancer
- TNF-alpha mRNA was a target of translational repression by pVHL through the TNF-alpha 3'-untranslated region in renal cell carcinoma cells
- Mutations in Von Hippel-Lindau gene product are associated with malignant transformation of pheochromocytomas
- demonstrate that the KRAB-A domain in VHLaK mediates pVHL binding and functions as a transcriptional repression module; findings provide a novel mechanism for the modulation of hypoxia-inducible factor-1alpha (HIF-1alpha) transactivation by pVHL
- Germline mutation of the VHL gene and loss of heterozygosity on the VHL gene locus in 3p were detected in a meningioma in VHL disease associated with multiple cerebellar hemangioblastomas
- Methylation inactivation of vhl is associated with oral cancer
- To better understand the role of VHL in the hypoxia signaling pathways of tumor cells, we used serial analysis of gene expression (SAGE) to investigate hypoxia-regulated gene expression in renal carcinoma cells (786-0), with and without VHL
- We conclude that, in vivo, folding of VHL requires the cooperation of Hsp70 and TRiC and that Hsp70 acts to promote substrate binding to TRiC.
- Loss of this protein causes cell density dependent deregulation of CyclinD1 expression through hypoxia-inducible factor.
- Downregulation of Cap43 gene by von Hippel-Lindau protein in renal cancer cells.
- role for VHL mutations promoting conventional clear cell renal cell carcinoma development by an impairment of HIF-1alpha proteolysis
- Data show that hypoxia-inducible factor 1 alpha was stabilized in the von Hippel-Lindau gene product-deficient cell line 786-0 treated with a proteasome inhibitor or cobalt ion.
- the subcellular localization of VHL plays a role in its tumor suppressor properties
- Promoter hypermethylation of this gene is demonstrated in esophageal squamous cell carcinoma.
- report seven additional congenital polycythemic patients with VHL mutations in both alleles
- hsRB7 is identified as a subunit of RNA polymerase II and a target of VHL.
- Nuclear and cytoplasmic pVHL expression was associated with low histological grade, early tumor stage, and better prognosis. Alteration of subcellular pVHL trafficking is of potential relevance for biological behavior of clear-cell renal-cell carcinoma.
- The von Hippel-Lindau tumour suppressor protein pVHL negatively regulates CXCR4 expression owing to its capacity to target hypoxia-inducible factor (HIF) for degradation under normoxic conditions
- role in regulating transcription of HIF-proline hydroxylase genes in response to low oxygen
- pVHL has a role in elevating p53 expression
- role of VHL protein level and intracellular localization in renal tumorigenesis in humans.
- contribution of tat-binding protein-1 to E3 ubiquitin ligase function
- Data show that chaperonin TRiC binding is specified by two short hydrophobic beta strands in the von Hippel-Lindau protein that, upon folding, become buried within the native structure.
- HIF2alpha has a role in regulating pVHL-defective tumor growth
- In Von Hippel-Lindau disease the association of clear cell renal carcinoma development with a relatively high loss of structural stability in pVHL missense-mutants was consistent.
- study of the phenotype of VHL 598C>T homozygosity reveals that Chuvash polycythemia is a distinct VHL syndrome manifested by thrombosis, vascular abnormalities, and intact hypoxic regulation despite increased basal expression of hypoxia-regulated genes
- We identified a missense mutation of VHL gene, 695 G --> A (R161Q), in a Japanese kindred with type 2A VHL syndrome. We analysed 16 members of this family and detected the same mutation in 8 individuals.
- von Hippel-Lindau tumor suppressor protein is a molten globule under native conditions
- deregulation of hypoxia-inducible genes in VHL-/- cells can be attributed mainly to deregulation of HIF and validate HIF as a therapeutic anticancer drug target
- In VHL disease, inactivation of the VHL wild-type allele appears necessary, but not sufficient, for the formation of tumor that produces symptoms and neurological disability.
- VHL appears to regulate the stability of other proteins that might be involved in various steps of oncogenic processes (review)
- The incidence of renal involvement & renal cell carcinoma was greater in VHL families with truncating mutations or large rearrangement, vs missense changes. 2 mutation cluster regions associated with renal lesions & RCC: codons 74-90 & codons 130-136.
- VHL appears to be a critical gatekeeper with respect to the development of renal cell carcinoma. (Review)
- To determine the germline mutation in an extended family in which 1 member was diagnosed clinically with von Hippel-Lindau (VHL) disease and to investigate 3 generations of the family.The mutation was identified as IVS1 + 1 G-->T
- directly measured VHL-induced subcellular changes in microtubule dynamics; induction of VHL in cells resulted in a decrease of tubulin turnover at the cell periphery, while minimally influencing microtubule dynamics around the centrosome
- presence of wild-type VHL protein (pVHL) increased mitochondrial DNA and respiratory chain protein contents and permitted the cells to rely on their mitochondrial ATP production to grow in the absence of glucose
- A DNA sequence analysis of vhl tumor suppressor gene revealed the L163R mutation. This new mutation may be specifically associated with the von Hippel-Lindau type 2C disease phenotype.
- Renal cell carcinoma patients who express VHL are likely to respond to bortezomib.
- specific association between pVHL and the hydroxylated HIF-alpha requires both the L1 and L7 loops to coordinate dynamic coupling among distant pVHL regions
- loss of heterozygosity of VHL gene is an important genetic event in Chinese sporadic renal carcinoma, and the LOH frequency is 41.4%. VHL LOH has no influence on stage and grade of RCC.
- von Hippel-Lindau tumour suppressor protein regulates HIF-1alpha and its oxygen-regulated transactivation domains at high cell density.
- IRP2 degradation involving 2-oxoglutarate-dependent oxygenase does not require the E3 ubiquitin ligase activity of pVHL
- Tid-1(L) may play a critical role in pVHL-mediated tumor suppression by modulating the pVHL-dependent HIF-1alpha stability.
- Therapeutic and prognostic implication of somatic VHL alteration in renal cell carcinoma may be different according to the mutational subtype and the Pro582Ser change in HIF-1alpha may contribute to the development of metastases.
- phosphorylation of the acidic domain of VHL plays a role in the regulation of proper fibronectin matrix deposition and may be relevant for the development of VHL-associated malignancies
- mechanisms of VHL tumour suppressor function and novel hypoxia-responsive genes that might be implicated in tumorigenesis in both VHL disease and in other cancers
- The interplay between the functional pVHL and carbonic anhydrase IX/CA XII in colorectal tumors seems rather complex and is not evident merely at the expression levels.
- Loss of expression of von Hippel-Lindau tumor suppressor protein associated with improved survival in patients with early-stage clear cell renal cell carcinoma
- A new heterozygous VHL gene mutation (430G->A;Gly144Arg)ws found in a man with polycythemia and high erythropoietin levels.
- Hippel-Lindau gene mutations may have a role in sporadic renal cell carcinoma
- pVHL itself is induced in prolonged hypoxia in a kinetic that parallels the observed downregulation of hypoxia-inducible factor 1, alpha protein under such conditions
- von Hippel Lindau tumor suppressor has a role in iron homeostasis in renal carcinoma cells
- Expression of p53 in renal carcinoma cells is independent of VHL.
- VHL loss drives NF-kappaB activation by resulting in hypoxia-inducible factor alpha accumulation
- analysis of Von Hippel-Lindau mutations in Korean patients with von Hippel-Lindau disease, pheochromocytomas and paragangliomas
- Review of overall findings demonstrates the essential role of the hypoxia/VHL/hypoxia-inducible factor-1 alpha pathway in endochondral bone development.
- the association of the elongin-binding domain of the tumor suppressor protein vin Hippel Landau (VHL) with a specific RNA-binding domain of HuR (RRM1) is important for the destabilizing function of VHL on VPF/VEGF mRNA
- Mutation IN Von Hippel Lindau tumor suppressor is associated with polycythemia
- type 2A but not type 2B mutant VHL proteins retained significant ubiquitin ligase activity towards HIF-1alpha in vitro
- in pancreatic cancer cells, the p38-mediated phosphorylation of HIF-1alpha contributed to the inhibition of HIF-1alpha and von Hippel-Lindau tumor suppressor protein interaction during ischemia
- Germline mutation on the VHL gene was present in patients with pheochromocytoma or functional paraganglioma.
- VHL forms a self-associated complex in vivo. Coexpression of 2 VHL missense mutants (1 in the alpha domain & the other in the beta domain)restores HIF-mediated gene expression. VHL homotypic complexes target HIFalpha for ubiquitin-mediated proteolysis.
- Although no evidence for a classic tumor suppressor role for VHL in NB could be obtained, a strong correlation was observed between reduced levels of VHL mRNA and low patient survival probability.
- pVHL does not directly promote the degradation of PKCd nor does it inhibit catalytic activity in cells, indicating that distinctive signalling role(s) for the cellular complex characterize this interaction
- These results suggest that the tumor suppressor pVHL has an unexpected function to upregulate the tumor suppressor p53.
- somatic VHL gene alterations may not play a major role in tumorigenesis of MEN2A-associated medullary thyroid carcinoma
- A hypomorphic VHL allele causes a generalised abnormality in VHL-HIF signalling. VHL plays a major role in the calibration & homeostasis of the respiratory & cardiovascular systems, most likely through its central role in the regulation of HIF.
- Ectopic expression of VHL in RCC(VHL-) cells induced increased polarization and primary cilium formation.
- Mnk2 can interact with CBC(VHL) complex, and is probably one of the new substrates of the CBC(VHL) complex.
- P25L is a benign variant of the VHL protein in von Hippel-Lindau (VHL) disease.
- Treatment of the VHL-deficient a human renal tumor cell line with the hydroxamic HDAC inhibitor LAQ824 resulted in an dependent of HIF-1 alpha protein via a VHL-independent mechanism and reduction of HIF-1 alpha transcriptional activity
- Reconstitution of VHL expression in renal cell carcinoma (RCC) cells repressed hepatocyte growth factor (HGF)-stimulated beta-catenin tyrosyl phosphorylation, cytoplasmic beta-catenin accumulation, and reporter gene transactivation.
- analysis of two sequence variants of the VHL gene
- VHL promotes E2 box-dependent E-cadherin transcription by HIF-mediated regulation of SIP1 and snail
- In transfected cells and KSHV-infected B lymphoma cells, KSHV-encoded latency-associated nuclear antigen (LANA) expression stimulates degradation of tumor suppressors von Hippel-Lindau and p53.
- von Hippel-Lindau (VHL) protein (pVHL) is a ciliary protein that controls ciliogenesis in kidney cells.
- VHL protein exerts its tumor suppressor action, at least partially, via inhibition of p22phox-based Nox4/Nox1 NADPH oxidase-dependent reactive oxygen species generation
- This review highlights recent evidence uncovering the transcriptional regulation of E-cadherin, a cell adhesion molecule with anti-invasive properties in epithelial-derived cancers, via the von Hippel-Lindau (VHL)-hypoxia-inducible factor (HIF) pathway.
- von Hippel-Lindau tumor suppressor protein has a role in clear cell renal carcinoma
- The VHL mutation genotype may be used to predict the prevalence and outcome of ocular VHL disease and to guide ophthalmic follow-up.
- The germ line mutations in Chinese kindreds with von Hippel-Lindau syndrome consisted of 4 missense mutations, 1 nonsense mutation and 1 deletion, of which 4 mutations existed in exon 1, 1 in exon 2 and 1 in exon 3.
- VHL tumour-suppressor gene mutation is involved in clear cell carcinoma in association with long-term dialysis. Mutation of VHL gene was not found in any dialysis-specific renal cell carcinomas studied herein.
- pVHL and GSK3beta function together in a ciliary-maintenance signalling network, disruption of which enhances the vulnerability of cells to lose their cilia, thereby promoting cyst formation.
- VHL inactivation leads to IGF1R upregulation, contributing to renal tumorigenesis and potentially also to chemoresistance.
- Quantitative differences with respect to HIF deregulation are sufficient to account for the differential risks of kidney cancer linked to VHL mutations.
- although LOH at the VHL gene locus was frequent in ovarian carcinomas, there is no significant correlation between LOH & loss of VHL expression; in 22 clear cell carcinomas, VHL expression showed negative correlation with nuclear expression of HIF-1alpha
- HIF-1alpha stabilization correlates with down-regulation of the tumour suppressor von Hippel-Lindau protein (pVHL.
- study found frequency of germline VHL mutations was very high in classic VHL cases, lower in non-classic cases that have limited VHL manifestations or single-organ involvement & low in cases not meeting current diagnostic VHL criteria
- The novel VHL gene mutation detected in the kindred may be the causative gene of nonsyndromic pheochromocytoma.
- Alterations in this hydrophobic region of the core beta domain of the VHL protein have a variety of phenotypic consequences, and there also variations in severity of von Hippel Lindau disease.
- An elevated number of circulating endothelial progenitor cells is related to high erythropoietin production in renal cell carcinoma with novel double somatic mutations of the VHL gene.
- VHL exerts inhibitory effects on the invasive and migratory capacity of breast cancer cells in vitro.
- microtubule-dependent functions of pVHL are influenced by kinesin-2
- Ours may be the first report of retinal hemangioblastoma unassociated with a VHL mutation.
- Invasion through Matrigel and migration in wound-healing assays are significantly greater in VHL mutant renal cell carcinoma compared with wild-type cells
- there is an aberrant nuclear localization of E-cadherin in CC-RCC harboring VHL mutations, suggesting potential prognostic value of VHL and E-cadherin in CC-RCC.
- ciliary assembly and mechanotransduction is rapidly restored in VHL-/- cells upon ectopic reconstitution of wild-type - but not variant alleles of - VHL
- in Renal cell Carcinoma patients 22 vhl gene mutations were detected: changes in protein functional domains in conserved regions; 72.7% were considered capable of compromising the VHL protein suppressor function
- Data show that pVHL acts as an adaptor to promote the inhibitory phosphorylation of the NF-kappaB agonist Card9 by casein kinase 2.
- Two cancer-free dysmorphic patients with karyotypes that confer susceptibility to familial Adenomatous polyposis and von-Hippel-Lindau syndrome.
- identify a novel nuclear export motif, further highlight the role of nuclear-cytoplasmic shuttling of E3 ligases in degradation of nuclear substrates, and provide evidence that disease-causing mutations can target subcellular trafficking
- This publication focuses on studies published over the past 2 years related to pVHL.
- A wide range of deletions in 3p, including at the VHL gene, may play a role in the development of tongue cancer.
- pVHL participates in the hypoxia-mediated degradation of plasma membrane Na-K-ATPase in a HIF-independent manner.
- Clusterin shows possible important functions in tumor suppression by the von Hippel-Lindau disease (VHL) gene product. May provide better understanding of retinal hemangioblastoma associated with VHL disease.
- study's findings demonstrate that the VHL-HIF signalling pathway, which is so central to intracellular oxygen sensing, also regulates the organ systems upon which cellular oxygen delivery ultimately depends
- DNA methylation of the von Hippel-Lindau gene is associated with acute myeloid leukaemia and myelodysplastic syndromes
- S100P and pVHL are a pair of sensitive and specific markers for identifying primary pancreatic ductal adenocarcinoma and pancreatic intraepithelial neoplasia
- Increased expression of CTGF and CYR61 proteins correlatets with the loss of VHL protein expression in renal cell carcinoma.
- Among VHL598C>T homozygotes, homocysteine was elevated with low and normal folate concentrations, consistent with a possible defect in the remethylation pathway
- (Epi)genetic alterations in the VHL gene do not have prognostic value in renal cancer prognosis.
- through this novel pathway involving P1465 hydroxylation and Ser5 phosphorylation of Rbp1, pVHL may regulate tumor growth
- VHL controls gene expression of TGFBI (BIGH3) and its transactivator KLF10 in renal clear cell carcinoma and other tumors.
- Inactivation of the VHL gene in sporadic clear cell renal cancer
- Establishing correlations between the genotype of the von Hippel-Lindau mutation and the phenotype of eye disease may inform us as to how ocular von Hippel-Lindau disease arises, and help guide molecular interventions in ocular von Hippel-Lindau disease.
- study reports a large Hungarian VHL type 2 family consisting of 32 members in whom a disease-causing AGT80AAT (Ser80Ile) c.239G>A, p.Ser80Ile mutation, but not the concurrent CCT25CTT (Pro25Leu) c.74C>T, p.Pro25Leu variant co-segregated with the disease
- Report two cases of endolymphatic sac tumor (aggressive papillary tumor of middle ear and temporal bone)with analysis of the VHL gene.
- COP9/signalosome increases the efficiency of von Hippel-Lindau protein ubiquitin ligase-mediated hypoxia-inducible factor-alpha ubiquitination
- Nitric oxide donor, (+/-)-S-nitroso-N-acetylpenicillamine, stabilizes transactive HIF1-alpha by inhibiting VHL and asparagine hydroxylation.
- Spectrum of VHL germline mutations in a Chinese population is similar to that observed in Western population, and genetic testing can be powerful in diagnosis and clinical management of von Hippel Lindau disease.
- VHL mutation alone is insufficient for tumor formation; study shows that epididymal cystadenomas from VHL patients frequently also lack expression of the PTEN tumor suppressor and display activation of phosphatidylinositol 3-kinase pathway signaling.
- a role for FHIT (in addition to VHL) in renal tumorigenesis.
- partial loss of function of VHL in endothelium may be a contributing factor in tumor angiogenesis through a HIF-VEGF-independent mechanism
- Genetic and epigenetic alterations of the VHL gene may be not involved in the development or progression of gastric cancers
- There was no statistically significant increase in response to vascular endothelial growth factor targeted agents with VHL inactivation.
- analysis of von Hippel-Lindau gene alterations in clear cell renal tumors
- The authors report the presence of a second missense G546T mutation in a patient with von Hippel-Lindau disease in Kuwait.
- analysis of of degradation of HIF-1alpha at normoxia that involves pVHL but is not mediated by PHDs 1-3 or by degradation boxes surrounding Pro(402) and Pro(563)
- E2-EPF UCP expression induced by growth factors or serum increased HIF-1alpha protein level under non-hypoxic conditions, suggesting that the Egr-1/SRF-UCP-VHL pathway is in part responsible for the increased HIF-1alpha protein level
- The pVHL tumour suppressor and the Wnt tumorigenesis pathway are therefore directly linked through Jade-1.
- Results suggest that STAT3 decreases the pVHL-mediated ubiquitination of HIF-1alpha through competition with pVHL for binding to HIF-1 alpha, and then stabilizes HIF-1alpha protein levels.
- genetic variants of HIF1A (Hypoxia-inducible factor 1-alpha )and VHL(von Hippel-Lindau tumor suppressor protein) are not associated with acute mountain sickness symptoms that occur in Sherpas at extremely high altitudes
- Mxi1 is an important downstream target of HIF that contributes to pVHL-deficient renal cancer tumorigenesis
- HIF-alpha effects on c-Myc distinguish two subtypes of sporadic VHL-deficient clear cell renal carcinoma
- A nonsignificant inverse association was observed between alcohol and renal cell cancer. No statistical significant heterogeneity by VHL mutation or methylation status.
- report of a family with hereditary head and neck paraganglioma with metastatic dissemination in the liver and the spine; evidence supports the absence of mutations in SDH, RET and VHL genes
- Activin B is a key mediator of VHL/HIF-induced transformation in renal cell carcinomas.