Effects of natural point mutation of rat aquaporin 5 expressed in vitro on its capacity of water permeability and membrane trafficking.
In the colony of Sprague-Dawley (SD) strain, we found that there were rats expressing a mutant AQP5, which has a point mutation at nt 308 (G308A), leading to a replacement of (103)Gly with (103)Asp in the 3rd transmembrane domain. The mutant molecule scarcely expressed in the acinar cells, probably because of ineffective trafficking. The mutant molecule, however, showed normal water permeability when assessed by the oocyte system.
Karabasil
Mileva R
MR
Department of Molecular Oral Physiology, Institute of Health Biosciences, University of Tokushima Graduate School, Tokushima, Japan.
Murdiastuti
Kwartarini
K
Purwanti
Nunuk
N
Azlina
Ahmad
A
Javkhlan
Purevjav
P
Hasegawa
Takahiro
T
Yao
Chenjuan
C
Akamatsu
Tetsuya
T
Hosoi
Kazuo
K
D000595:Amino Acid Sequence; D000818:Animals; D051402:Aquaporin 5 / Q000032:analysis / Q000235:genetics* / Q000502:physiology*; D001692:Biological Transport / Q000502:physiology; D002463:Cell Membrane Permeability / Q000502:physiology*; D005260:Female; D023421:Models, Animal; D008969:Molecular Sequence Data; D009865:Oocytes / Q000166:cytology / Q000378:metabolism; D017354:Point Mutation / Q000235:genetics*; D051381:Rats; D017207:Rats, Sprague-Dawley; D013363:Submandibular Gland / Q000378:metabolism; D014867:Water / Q000378:metabolism*; D014982:Xenopus laevis
C496040:Aqp5 protein, rat; D051402:Aquaporin 5; D014867:Water