| PRKCSH serves as a potential immunological and prognostic biomarker in pan-cancer. | PRKCSH serves as a potential immunological and prognostic biomarker in pan-cancer.
Wang Q, Wang X, Li J, Yin T, Wang Y, Cheng L., Free PMC Article | 02/1/2024 |
| Potential role of PRKCSH in lung cancer: bioinformatics analysis and a case study of Nano ZnO. | Potential role of PRKCSH in lung cancer: bioinformatics analysis and a case study of Nano ZnO.
Lei R, Zhou M, Zhang S, Luo J, Qu C, Wang Y, Guo P, Huang R. | 04/2/2022 |
| Results suggest that loss of PRKCSH and SEC63 leads to general defects in ciliogenesis, while quenching of the Wnt signaling cascade is cholangiocyte-restricted. | Liver cyst gene knockout in cholangiocytes inhibits cilium formation and Wnt signaling.
Wills ES, Te Morsche RHM, van Reeuwijk J, Horn N, Geomini I, van de Laarschot LFM, Mans DA, Ueffing M, Boldt K, Drenth JPH, Roepman R. | 03/24/2018 |
| This study demonstrated that Large copy number variations on germline level are not present in patients with a clinical diagnosis of Severe Polycystic Liver Disease. | Severe Polycystic Liver Disease Is Not Caused by Large Deletions of the PRKCSH Gene.
Cnossen WR, Maurits JS, Salomon J, Te Morsche RH, Waanders E, Drenth JP., Free PMC Article | 04/1/2017 |
| Polycystic liver disease is recessive at the cellular level, and loss of functional PRKCSH is an important step in cystogenesis. | Secondary, somatic mutations might promote cyst formation in patients with autosomal dominant polycystic liver disease.
Janssen MJ, Waanders E, Te Morsche RH, Xing R, Dijkman HB, Woudenberg J, Drenth JP. | 02/11/2012 |
| The induction of autophagy by hepatocystin deficiency is mediated through mammalian target of rapamycin (mTOR). | Deficiency of hepatocystin induces autophagy through an mTOR-dependent pathway.
Yang J, Zhao Y, Ma K, Jiang FJ, Liao W, Zhang P, Zhou J, Tu B, Wang L, Kampinga HH, Xie Z, Zhu WG. | 10/8/2011 |
| Results provide evidence that mutations at the coding PRKCSH GAG repeat are a target of MSI and are selectively associated with the MSI-H phenotype in gastric carcinomas. | PRKCSH GAG trinucleotide repeat is a mutational target in gastric carcinomas with high-level microsatellite instability.
Palmirotta R, Guadagni F, Savonarola A, Ludovici G, De Marchis ML, Palli D, Falchetti M, Ottini L. | 07/23/2011 |
| The common SNPs tested in DDOST, PRKCSH and LGALS3 do not seem to be associated with diabetic micro- or macrovascular complications or with type 1 diabetes in Finnish patients. | DDOST, PRKCSH and LGALS3, which encode AGE-receptors 1, 2 and 3, respectively, are not associated with diabetic nephropathy in type 1 diabetes.
Hoverfelt A, Sallinen R, Söderlund JM, Forsblom C, Pettersson-Fernholm K, Parkkonen M, Groop PH, Wessman M, FinnDiane Study Group, Hoverfelt A, Sallinen R, Söderlund JM, Forsblom C, Pettersson-Fernholm K, Parkkonen M, Groop PH, Wessman M, FinnDiane Study Group. | 11/6/2010 |
| identified a total of 26 novel mutations in PRKCSH (n = 14) and SEC63 (n = 12), including four splice site mutations, eight insertions/ deletions, six non-sense mutations, and eight missense mutations | Secondary and tertiary structure modeling reveals effects of novel mutations in polycystic liver disease genes PRKCSH and SEC63.
Waanders E, Venselaar H, te Morsche RH, de Koning DB, Kamath PS, Torres VE, Somlo S, Drenth JP., Free PMC Article | 10/23/2010 |
| Our results suggest that PRKCSH gene is not a major genetic cause of PCLD and there may be at least another locus responsible for the disease in Taiwan. | PRKCSH genetic mutation was not found in Taiwanese patients with polycystic liver disease.
Yang AM, Shih SC, Chu CH, Wang TE, Yang WS, Yang AM, Shih SC, Chu CH, Wang TE, Yang WS. | 03/15/2010 |
| PRKCSH functions as a chaperone-like molecule, which prevents endoplasmic reticulum-associated degradation of TRPP2. | PRKCSH/80K-H, the protein mutated in polycystic liver disease, protects polycystin-2/TRPP2 against HERP-mediated degradation.
Gao H, Wang Y, Wegierski T, Skouloudaki K, Pütz M, Fu X, Engel C, Boehlke C, Peng H, Kuehn EW, Kim E, Kramer-Zucker A, Walz G. | 03/15/2010 |
| Observational study of gene-disease association. (HuGE Navigator) | See all PubMed (3) articlesDDOST, PRKCSH and LGALS3, which encode AGE-receptors 1, 2 and 3, respectively, are not associated with diabetic nephropathy in type 1 diabetes.
Hoverfelt A, Sallinen R, Söderlund JM, Forsblom C, Pettersson-Fernholm K, Parkkonen M, Groop PH, Wessman M, FinnDiane Study Group, Hoverfelt A, Sallinen R, Söderlund JM, Forsblom C, Pettersson-Fernholm K, Parkkonen M, Groop PH, Wessman M, FinnDiane Study Group. Patients with isolated polycystic liver disease referred to liver centres: clinical characterization of 137 cases.
Van Keimpema L, De Koning DB, Van Hoek B, Van Den Berg AP, Van Oijen MG, De Man RA, Nevens F, Drenth JP. PRKCSH genetic mutation was not found in Taiwanese patients with polycystic liver disease.
Yang AM, Shih SC, Chu CH, Wang TE, Yang WS, Yang AM, Shih SC, Chu CH, Wang TE, Yang WS. | 04/8/2009 |
| 80K-H is a novel regulator of IP3R1 activity, and it may contribute to neuronal functions. | 80K-H interacts with inositol 1,4,5-trisphosphate (IP3) receptors and regulates IP3-induced calcium release activity.
Kawaai K, Hisatsune C, Kuroda Y, Mizutani A, Tashiro T, Mikoshiba K. | 01/21/2010 |
| the majority of cysts from PRKCSH mutation carriers did not express hepatocystin | Cysts of PRKCSH mutated polycystic liver disease patients lack hepatocystin but express Sec63p.
Waanders E, Croes HJ, Maass CN, te Morsche RH, van Geffen HJ, van Krieken JH, Fransen JA, Drenth JP. | 01/21/2010 |
| These results indicate that insulin induces dynamic associations between PKCzeta, 80K-H, and munc18c and that 80K-H may act as a key signaling link between PKCzeta and munc18c in live cells. | 80K-H acts as a signaling bridge in intact living cells between PKCzeta and the GLUT4 translocation regulator Munc18c.
Smithers NP, Hodgkinson CP, Cuttle M, Sale GJ. | 01/21/2010 |
| Hepatocystin is not secreted in liver cyst fluids of autosomal dominant polycystic liver disease patients, suggesting that mutant hepatocystin is either not produced or degraded intracellularly. | Hepatocystin is not secreted in cyst fluid of hepatocystin mutant polycystic liver patients.
Waanders E, Lameris AL, Op den Camp HJ, Pluk W, Gloerich J, Strijk SP, Drenth JP. | 01/21/2010 |
| Observational study of genotype prevalence and gene-disease association. (HuGE Navigator) | Extensive mutational analysis of PRKCSH and SEC63 broadens the spectrum of polycystic liver disease.
Waanders E, te Morsche RH, de Man RA, Jansen JB, Drenth JP. | 03/13/2008 |
| germline mutations in PRKCSH as the probable cause of autosomal dominant polycystic liver disease | Germline mutations in PRKCSH are associated with autosomal dominant polycystic liver disease.
Drenth JP, te Morsche RH, Smink R, Bonifacino JS, Jansen JB. | 01/21/2010 |
| Mutations in this protein cause isolated autosomal dominant polycystic liver disease. | Mutations in PRKCSH cause isolated autosomal dominant polycystic liver disease.
Li A, Davila S, Furu L, Qian Q, Tian X, Kamath PS, King BF, Torres VE, Somlo S., Free PMC Article | 01/21/2010 |
| autosomal dominant polycystic liver disease is genetically heterogeneous | Abnormal hepatocystin caused by truncating PRKCSH mutations leads to autosomal dominant polycystic liver disease.
Drenth JP, Tahvanainen E, te Morsche RH, Tahvanainen P, Kääriäinen H, Höckerstedt K, van de Kamp JM, Breuning MH, Jansen JB. | 01/21/2010 |
| role of hepatocystin in carbohydrate processing and quality control of newly synthesized glycoproteins in the endoplasmic reticulum | Molecular characterization of hepatocystin, the protein that is defective in autosomal dominant polycystic liver disease.
Drenth JP, Martina JA, Te Morsche RH, Jansen JB, Bonifacino JS. | 01/21/2010 |
| results identify 80K-H as a new player involved in GLUT4 vesicle transport and identify a link between a kinase involved in the insulin signalling cascade, PKCzeta, and a known component of the GLUT4 vesicle trafficking pathway, munc18c | Identification of 80K-H as a protein involved in GLUT4 vesicle trafficking.
Hodgkinson CP, Mander A, Sale GJ., Free PMC Article | 01/21/2010 |