title: Altered response of pendrin-positive intercalated cells in the kidney of Hoxb7-Cre;Mib1f/f mice.
abstract: The anion exchanger pendrin is exclusively expressed by non-type A intercalated cells (ICs), type B ICs and non A-non B ICs. Pendrin-positive ICs are mainly localized in the cortical collecting duct (CCD) and connecting tubule (CNT) rather than the outer medullary collecting duct (OMCD). Our previous study reported that Notch signaling is required for the specification of ureteric bud cells to the principal cells (PCs) and ICs in the medullary collecting duct. The purpose of this study was to determine whether the deletion of Mind bomb-1 (Mib1), an E3 ubiquitin ligase required for the initiation of Notch signaling, would affect the differentiation of pendrin-positive type B and non A-non B ICs in Hoxb7-Cre;Mib1f/f mice. In Hoxb7-Cre;Mib1f/f mice, there was a significant increase in the fraction of pendrin-negative/AE1-positive type A ICs not only in the OMCD (67.02±2.04% vs. 33.78±0.71%; Hoxb7-Cre;Mib1f/f vs. Mib1f/f) but also in the CCD (23.70±2.68% vs. 19.71±0.43%; Hoxb7-Cre;Mib1f/f vs. Mib1f/f) and CNT (23.70±2.68% vs. 19.71±0.43%; Hoxb7-Cre;Mib1f/f vs. Mib1f/f) as compared with Mib1f/f. In contrast, there were no significant differences in the fraction of pendrin-positive type B ICs (7.11±3.84% vs. 7.61±4.45%; Hoxb7-Cre;Mib1f/f vs. Mib1f/f) between the two groups in the cortex including CCD and CNT. Furthermore, there was a significant decrease in the fraction of non A-non B ICs (8.95±2.28% vs. 13.06±4.81%; Hoxb7-Cre;Mib1f/f vs. Mib1f/f) in these tubules in the Hoxb7-Cre;Mib1f/f mice. These results suggest that the degree of differentiation of subtypes of ICs may vary depending on the Notch signaling pathway.
authors.affiliation: Department of Anatomy and Cell Death Disease Research Center, College of Medicine, The Catholic University of Korea, and Department of Applied Veterinary Medicine, The Graduate School of Agriculture and Animal Science, Konkuk University, Seoul, Republic of Korea.
authors.forename: Sun-Ah
authors.initials: SA
authors.lastname: Nam
authors.affiliation: Department of Anatomy and Cell Death Disease Research Center, College of Medicine, The Catholic University of Korea, Seoul, Republic of Korea.
authors.forename: Wan-Young
authors.initials: WY
authors.lastname: Kim
authors.affiliation: Department of Anatomy and Cell Death Disease Research Center, College of Medicine, The Catholic University of Korea, Seoul, Republic of Korea.
authors.forename: Yu-Mi
authors.initials: YM
authors.lastname: Kim
authors.affiliation: Department of Internal Medicine, Division of Nephrology, Kangbuk Samsung Hospital, School of Medicine, Sungkyunkwan University, Seoul, Republic of Korea.
authors.forename: Hyang
authors.initials: H
authors.lastname: Kim
authors.affiliation: Department of Biological Sciences, Seoul National University, Seoul, Republic of Korea.
authors.forename: Young-Yun
authors.initials: YY
authors.lastname: Kong
authors.affiliation: Department of Applied Veterinary Medicine, The Graduate School of Agriculture and Animal Science, Konkuk University, Seoul, Republic of Korea.
authors.forename: Sang Mok
authors.initials: SM
authors.lastname: Lee
authors.affiliation: Department of Anatomy and Cell Death Disease Research Center, College of Medicine, The Catholic University of Korea, Seoul, Republic of Korea. jinkim@catholic.ac.kr.
authors.forename: Jin
authors.initials: J
authors.lastname: Kim
mesh_terms: D000818:Animals; D027321:Anion Transport Proteins / Q000378:metabolism*; D007668:Kidney / Q000166:cytology / Q000378:metabolism*; D007685:Kidney Tubules, Collecting / Q000166:cytology / Q000378:metabolism*; D051379:Mice; D008822:Mice, Transgenic; D015398:Signal Transduction / Q000235:genetics; D000076988:Sulfate Transporters; D044767:Ubiquitin-Protein Ligases / Q000235:genetics / Q000378:metabolism*
chemical_list: D027321:Anion Transport Proteins; C494849:Slc26a4 protein, mouse; D000076988:Sulfate Transporters; C470629:MIB1 protein, mouse; D044767:Ubiquitin-Protein Ligases