Role of polycystins in renal tubulogenesis
作者： Alessandra Boletta , Gregory G Germino
DOI: 10.1016/S0962-8924(03)00169-7
关键词:
摘要: Every day, human renal tubules process 140 l of glomerular filtrate into 1 urine. They accomplish this by the coordinated function distinct cell types occupying specific positions along tubules. This precisely defined structure requires tight regulation morphogenesis. A group disorders termed polycystic kidney disease (PKD) is characterized altered tubular morphology. Mutating genes involved in PKD results that either fail to form properly or 'forget' how maintain their 'correct' diameter. Study proteins will elucidate morphogenesis and guide development therapies. Here, we focus on insights provided study most common PKD, autosomal dominant PKD.
unirioja.es
elsevier.com
sci-hub.se 参考文章(76)
Robert W. Tucker, Arthur B. Pardee, Keigi Fujiwara, Centriole ciliation is related to quiescence and DNA synthesis in 3T3 cells Cell. ,vol. 17, pp. 527- 535 ,(1979) , 10.1016/0092-8674(79)90261-7
Toshio Mochizuki, Guanqing Wu, Tomohito Hayashi, Stavroulla L Xenophontos, Barbera Veldhuisen, Jasper J Saris, David M Reynolds, Yiqiang Cai, Patricia A Gabow, Alkis Pierides, William J Kimberling, Martijn H Breuning, C Constantinou Deltas, Dorien JM Peters, Stefan Somlo, None, PKD2, a Gene for Polycystic Kidney Disease That Encodes an Integral Membrane Protein Science. ,vol. 272, pp. 1339- 1342 ,(1996) , 10.1126/SCIENCE.272.5266.1339
F. Lin, T. Hiesberger, K. Cordes, A. M. Sinclair, L. S. B. Goldstein, S. Somlo, P. Igarashi, Kidney-specific inactivation of the KIF3A subunit of kinesin-II inhibits renal ciliogenesis and produces polycystic kidney disease Proceedings of the National Academy of Sciences of the United States of America. ,vol. 100, pp. 5286- 5291 ,(2003) , 10.1073/PNAS.0836980100
R. Montesano, G. Schaller, L. Orci, Induction of epithelial tubular morphogenesis in vitro by fibroblast-derived soluble factors. Cell. ,vol. 66, pp. 697- 711 ,(1991) , 10.1016/0092-8674(91)90115-F
L. Tsiokas, T. Arnould, C. Zhu, E. Kim, G. Walz, V. P. Sukhatme, Specific association of the gene product of PKD2 with the TRPC1 channel Proceedings of the National Academy of Sciences of the United States of America. ,vol. 96, pp. 3934- 3939 ,(1999) , 10.1073/PNAS.96.7.3934
S. Gonzalez-Perrett, K. Kim, C. Ibarra, A. E. Damiano, E. Zotta, M. Batelli, P. C. Harris, I. L. Reisin, M. A. Arnaout, H. F. Cantiello, Polycystin-2, the protein mutated in autosomal dominant polycystic kidney disease (ADPKD), is a Ca2+-permeable nonselective cation channel Proceedings of the National Academy of Sciences of the United States of America. ,vol. 98, pp. 1182- 1187 ,(2001) , 10.1073/PNAS.98.3.1182
Feng Qian, F. Joseph Germino, Yiqiang Cai, Xiangbin Zhang, Stefan Somlo, Gregory G. Germino, PKD1 interacts with PKD2 through a probable coiled-coil domain Nature Genetics. ,vol. 16, pp. 179- 183 ,(1997) , 10.1038/NG0697-179
Luc Baert, Hereditary polycystic kidney disease (adult form): A microdissection study of two cases at an early stage of the disease Kidney International. ,vol. 13, pp. 519- 525 ,(1978) , 10.1038/KI.1978.75
C. Montell, Physiology, Phylogeny, and Functions of the TRP Superfamily of Cation Channels Science Signaling. ,vol. 2001, ,(2001) , 10.1126/STKE.2001.90.RE1
Stephen C. Parnell, Brenda S. Magenheimer, Robin L. Maser, Carolyn A. Rankin, Abdelkrim Smine, Takashi Okamoto, James P. Calvet, The Polycystic Kidney Disease-1 Protein, Polycystin-1, Binds and Activates Heterotrimeric G-Proteinsin Vitro Biochemical and Biophysical Research Communications. ,vol. 251, pp. 625- 631 ,(1998) , 10.1006/BBRC.1998.9514