Abstract:
BACKGROUND INFORMATION:The results of water permeability measurements suggest the presence of an AQP (aquaporin) in the membrane of the CV (contractile vacuole) in Amoeba proteus [Nishihara, Shimmen and Sonobe (2004) Cell Struct. Funct. 29, 85-90]. RESULTS:In the present study, we cloned an AQP gene from A. proteus [ApAQP (A. proteus AQP)] that encodes a 295-amino-acid protein. The protein has six putative TMs (transmembrane domains) and two NPA (Asn-Pro-Ala) motifs, which are conserved among various AQPs and are thought to be involved in the formation of water channels that span the lipid bilayer. Using Xenopus oocytes, we have demonstrated that the ApAQP protein product can function as a water channel. Immunofluorescence microscopy with anti-ApAQP antibody revealed that ApAQP is detected on the CV membrane and on the vesicles around the CV. The presence of V-ATPase (vacuolar H+-ATPase) on the vesicle membrane around the CV was also detected. CONCLUSIONS:Our data on ApAQP allow us to provide the first informed explanation of the high water permeability of the CV membrane in amoeba. Moreover, the results suggest that vesicles possessing V-ATPase are involved in generating an osmotic gradient. Based on our findings, we propose a new hypothesis for the mechanism of CV function.
journal_name
Biol Celljournal_title
Biology of the cellauthors
Nishihara E,Yokota E,Tazaki A,Orii H,Katsuhara M,Kataoka K,Igarashi H,Moriyama Y,Shimmen T,Sonobe Sdoi
10.1042/BC20070091subject
Has Abstractpub_date
2008-03-01 00:00:00pages
179-88issue
3eissn
0248-4900issn
1768-322Xpii
BC20070091journal_volume
100pub_type
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