Skip to main content
Mijn bibliotheek
Ga naar:
Nieuws Boeken Tijdschriften Toetsvragen Web-tv Video Audio
Tips voor Mijn BSL
BSL Shop
Inloggen

Welkom bij THIM Hogeschool voor Fysiotherapie & Bohn Stafleu van Loghum

THIM Hogeschool voor Fysiotherapie heeft ervoor gezorgd dat je Mijn BSL eenvoudig en snel kunt raadplegen. Je kunt je links eenvoudig registreren. Met deze gegevens kun je thuis, of waar ook ter wereld toegang krijgen tot Mijn BSL. Heb je een vraag, neem dan contact op met helpdesk@thim.nl.

» Andere revante producten voor THIM studenten en medewerkers.

Registreer

Om ook buiten de locaties van THIM, thuis bijvoorbeeld, van Mijn BSL gebruik te kunnen maken, moet je jezelf eenmalig registreren. Dit kan alleen vanaf een computer op een van de locaties van THIM.

Eenmaal geregistreerd kun je thuis of waar ook ter wereld onbeperkt toegang krijgen tot Mijn BSL.

Login

Als u al geregistreerd bent, hoeft u alleen maar in te loggen om onbeperkt toegang te krijgen tot Mijn BSL.

Inloggen
Top
Tijdschrift voor Kindergeneeskunde
Gepubliceerd in:

01-04-2006 | Artikelen

De rol van polycystine-1 en polycystine-2 in de pathofysiologie van cystennieren

Auteur: dr. D. J. M. Peters

Gepubliceerd in: Tijdschrift voor Kindergeneeskunde | Uitgave 2/2006

Log in om toegang te krijgen
share
DELEN

Deel dit onderdeel of sectie (kopieer de link)

  • Optie A:
    Klik op de rechtermuisknop op de link en selecteer de optie “linkadres kopiëren”
  • Optie B:
    Deel de link per e-mail
    Link delen
publish
Publiceer nu

Summary

In recent years, our knowledge on the pathophysiology of polycystic kidney disease expanded dramatically. An increasing number of genes mutated in renal cystic diseases in humans or rodents have been identified and most of them encode proteins that localise in the primary cilium, a mechanosensor that regulates intracellular [Ca2+]i levels. Polycystin-1 and polycystin-2, the proteins encoded by the genes mutated in patients with autosomal dominant polycystic kidney disease (adpkd), seem to play a crucial role in this regulation. The polycystins belong to a novel subclass of transient receptor potential (trp) channels, the transient receptor potential polycystins (trpp's). Increased knowledge on altered signaling in polycystic kidney disease and the availability of a variety of animal models are now providing the opportunities to test therapeutic interventions.
vorige artikel De ziekte van Dent
volgende artikel Aquaporines in de nier en hun rol in nefrogene diabetes insipidus
Literatuur
Gabow PA. Autosomal dominant polycystic kidney disease: More than a renal disease. Am J Kidney Dis 1990;16:403-13.PubMed
Peters DJM, Sandkuijl LA. In: Breuning MH, Devoto M, Romeo G, eds. Contributions to nephrology, vol. 97: Polycystic kidney disease. Basel: Karger, 1992. p. 128-39.
The European Polycystic Kidney Disease Consortium. The polycystic kidney disease 1 gene encodes a 14 kb transcript and lies within a duplicated region on chromosome 16. Cell 1992; 77:881-94.
The American PKD1 Consortium. Analysis of the genomic sequence for the autosomal dominant polycystic kidney disease (PKD1) gene predicts the presence of a leucine-rich repeat. Hum Mol Genet 1995;4:575-82.
Hughes J, Ward CJ, Peral B, et al. The polycystic kidney disease 1 (PKD1) gene encodes a novel protein with multiple cell recognition domains. Nat Genet 1995;10:151-60.CrossRefPubMed
Rossetti S, Chauveau D, Walker D, et al. A complete mutation screen of the ADPKD genes by DHPLC. Kidney Int 2002;61:1588-99.CrossRefPubMed
Hateboer N, Dijk MA, Coto E, et al. Comparison of phenotypes of polycystic kidney disease types 1 and 2. Lancet 1999; 353:103-7.CrossRefPubMed
Watnick T, Phakdeekitcharoen B, Johnson A, et al. Mutation detection of PKD1 identifies a novel mutation common to three families with aneurysms and/or very-early-onset disease. Am J Hum Genet 1999;65:1561-71.CrossRefPubMed
Rossetti S, Chauveau D, Kubly V, et al. Association of mutation position in polycystic kidney disease 1 (PKD1) gene and development of a vascular phenotype. Lancet 2003;361:2196-201.CrossRefPubMed
Rossetti S, Burton S, Strmecki L, et al. The position of the polycystic kidney disease 1 (PKD1) gene mutation correlates with the severity of renal disease. J Am Soc Nephrol 2002; 13:1230-7.CrossRefPubMed
Magistroni R, He N, Wang K, et al. Genotype-renal function correlation in type 2 autosomal dominant polycystic kidney disease. J Am Soc Nephrol 2003;14:1164-74.CrossRefPubMed
Fain PR, McFann KK, Taylor MR, et al. Modifier genes play a significant role in the phenotypic expression of PKD1. Kidney Int 2005;67:1256-67.CrossRefPubMed
Paterson AD, Magistroni R, He N, et al. Progressive loss of renal function is an age-dependent heritable trait in type 1 autosomal dominant polycystic kidney disease. J Am Soc Nephrol 2005;16(3):755-62.CrossRefPubMed
Qian F, Germino FJ, Cai Y, et al. PKD1 interacts with PKD2 through a probable coiled-coil domain. Nat Genet 1997;16: 179-83.CrossRefPubMed
Mochizuki T, Wu G, Hayashi T, et al. PKD2, a gene for polycystic kidney disease that encodes an integral membrane protein. Science 1996;272:1339-42.CrossRefPubMed
Foggensteiner L, Bevan AP, Thomas R, et al. Cellular and subcellular distribution of polycystin-2, the protein product of the PKD2 gene. J Am Soc Nephrol 2000;11:814-27.PubMed
Peters DJM, Wal A van de, Spruit L, et al. Cellular localization and tissue distribution of polycystin-1. J Pathol 1999; 188:439-46.CrossRefPubMed
Lu W, Peissel B, Babakhanlou H, et al. Perinatal lethality with kidney and pancreas defects, in mice with a targetted pkd1 mutation. Nat Genet 1997;17:179-81.CrossRefPubMed
Lantinga-van Leeuwen IS, Dauwerse JG, Baelde HJ, et al. Lowering of Pkd1 expression is sufficient to cause polycystic kidney disease. Hum Mol Genet 2004;13:3069-77.CrossRefPubMed
Wu G, D'Agati V, Cai Y, et al. Somatic inactivation of Pkd2 results in polycystic kidney disease. Cell 1998;93:177-88.CrossRefPubMed
Qian FJ, Watnick TJ, Onuchic LF, Germino GG. The molecular basis of focal cyst formation in human autosomal dominant polycystic kidney disease. Cell 1996;87:979-87.CrossRefPubMed
Montell C. Physiology, phylogeny, and functions of the TRP superfamily of cation channels. Sci STKE 2001;90:RE1.
Parnell SC, Magenheimer BS, Rankin CA, et al. The polycystic kidney disease-1 protein, polycystin-1, binds and activates heterotrimeric G-proteins in vitro. Biochem Biophys Res Commun 1998;251:625-31.CrossRefPubMed
Kim E, Arnould T, Sellin L, et al. Interaction between RGS7 and polycystin. Proc Natl Acad Sci USA 1999;96:6371-6.CrossRefPubMed
Bhunia AK, Piontek K, Boletta A, et al. PKD1 induces p21(waf1) and regulation of the cell cycle via direct activation of the JAK-STAT signaling pathway in a process requiring PKD2. Cell 2002;109:157-68.CrossRefPubMed
Qian F, Boletta A, Bhunia AK, et al. Cleavage of polycystin-1 requires the receptor for egg jelly domain and is disrupted by human autosomal-dominant polycystic kidney disease 1-associated mutations. Proc Natl Acad Sci USA 2002;99:16981-6.CrossRefPubMed
Chauvet V, Tian X, Husson H, et al. Mechanical stimuli induce cleavage and nuclear translocation of the polycystin-1 C terminus. J Clin Invest 2004;114:1433-43.PubMed
Kottgen M, Benzing T, Simmen T, et al. Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation. EMBO J 2005;24(4):705-16.CrossRefPubMed
Hanaoka K, Qian F, Boletta A, et al. Co-assembly of polycystin-1 and -2 produces unique cation-permeable currents. Nature 2000;408:990-4.CrossRefPubMed
Delmas P, Padilla F, Osorio N, et al. Polycystins, calcium signaling, and human diseases. Biochem Biophys Res Commun 2004;322:1374-83.CrossRefPubMed
Pazour GJ, Rosenbaum JL. Intraflagellar transport and cilia-dependent diseases. Trends Cell Biol 2002;12:551-5.CrossRefPubMed
Yoder BK, Hou X, Guay-Woodford LM. The polycystic kidney disease proteins, polycystin-1, polycystin-2, polaris, and cystin, are co-localized in renal cilia. J Am Soc Nephrol 2002; 13:2508-16.CrossRefPubMed
Praetorius HA, Spring KR. Bending the MDCK cell primary cilium increases intracellular calcium. J Membr Biol 2001;184:71-9.CrossRefPubMed
Nauli SM, Alenghat FJ, LuoY, et al. Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells. Nat Genet 2003;33:129-37.CrossRefPubMed
Delmas P, Nomura H, Li X, et al. Constitutive activation of G-proteins by polycystin-1 is antagonized by polycystin-2. J Biol Chem 2002;277:11276-83.CrossRefPubMed
Yamaguchi T, Wallace DP, Magenheimer BS, et al. Calcium restriction allows cAMP activation of the B-Raf/ERK pathway, switching cells to a cAMP-dependent growth-stimulated phenotype. J Biol Chem 2004;279:40419-30.CrossRefPubMed
Tao Y, Kim J, Schrier RW, Edelstein CL. Rapamycin markedly slows disease progression in a rat model of polycystic kidney disease. J Am Soc Nephrol 2005;16:46-51.CrossRefPubMed
Muto S, Aiba A, Saito Y, et al. Pioglitazone improves the phenotype and molecular defects of a targeted Pkd1 mutant. Hum Mol Genet 2002;11:1731-42.CrossRefPubMed
Dijk MA van, Breuning MH, Duiser R, et al. No effect of enalapril on progression in autosomal dominant polycystic kidney disease. Nephrol Dial Transplant 2003;18:2314-20.CrossRefPubMed
Pazour GJ, Dickert BL, Vucica Y, et al. Chlamydomonas IFT88 and its mouse homologue, polycystic kidney disease gene tg737, are required for assembly of cilia and flagella. J Cell Biol 200;151:709-18.CrossRef
Metagegevens
Titel
De rol van polycystine-1 en polycystine-2 in de pathofysiologie van cystennieren
Auteur
dr. D. J. M. Peters
Publicatiedatum
01-04-2006
Uitgeverij
Bohn Stafleu van Loghum
Gepubliceerd in
Tijdschrift voor Kindergeneeskunde / Uitgave 2/2006
Print ISSN: 0376-7442
Elektronisch ISSN: 1875-6840
DOI
https://doi.org/10.1007/BF03061609

Andere artikelen Uitgave 2/2006

Een kwestie van komen en gaan: neurologische aandoeningen ten gevolge van ionkanaalmutaties

  • Artikelen

Het lange qt-syndroom: een cardiale ionkanaalziekte

  • Artikelen

Fenotype-genotype correlaties bij cystische fibrose

  • Artikelen

Aquaporines in de nier en hun rol in nefrogene diabetes insipidus

  • Artikelen

De ziekte van Dent

  • Artikelen

Een bijzondere vorm van het syndroom van Bartter: een gestoorde functie van het romk-kaliumkanaal

  • Artikelen