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.
Department of Molecular Oral Physiology, Institute of Health Biosciences, University of Tokushima Graduate School, Tokushima, Japan.
Mileva R
MR
Karabasil
Kwartarini
K
Murdiastuti
Nunuk
N
Purwanti
Ahmad
A
Azlina
Purevjav
P
Javkhlan
Takahiro
T
Hasegawa
Chenjuan
C
Yao
Tetsuya
T
Akamatsu
Kazuo
K
Hosoi
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