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Title: The binding property of a monoclonal antibody against the extracellular domains of aquaporin-4 directs aquaporin-4 toward endocytosis

Authors:
; ; ; ; ; ; ; ; ; ; ; ;
Publication Date:
Sponsoring Org.:
USDOE Office of Electricity Delivery and Energy Reliability (OE), Power Systems Engineering Research and Development (R&D) (OE-10)
OSTI Identifier:
1254670
Grant/Contract Number:
A151TR
Resource Type:
Journal Article: Published Article
Journal Name:
Biochemistry and Biophysics Reports
Additional Journal Information:
Journal Volume: 7; Journal Issue: C; Related Information: CHORUS Timestamp: 2017-09-18 10:33:58; Journal ID: ISSN 2405-5808
Publisher:
Elsevier
Country of Publication:
Netherlands
Language:
English

Citation Formats

Huang, Ping, Takai, Yoshiki, Kusano-Arai, Osamu, Ramadhanti, Julia, Iwanari, Hiroko, Miyauchi, Takayuki, Sakihama, Toshiko, Han, Jing-Yan, Aoki, Masashi, Hamakubo, Takao, Fujihara, Kazuo, Yasui, Masato, and Abe, Yoichiro. The binding property of a monoclonal antibody against the extracellular domains of aquaporin-4 directs aquaporin-4 toward endocytosis. Netherlands: N. p., 2016. Web. doi:10.1016/j.bbrep.2016.05.017.
Huang, Ping, Takai, Yoshiki, Kusano-Arai, Osamu, Ramadhanti, Julia, Iwanari, Hiroko, Miyauchi, Takayuki, Sakihama, Toshiko, Han, Jing-Yan, Aoki, Masashi, Hamakubo, Takao, Fujihara, Kazuo, Yasui, Masato, & Abe, Yoichiro. The binding property of a monoclonal antibody against the extracellular domains of aquaporin-4 directs aquaporin-4 toward endocytosis. Netherlands. doi:10.1016/j.bbrep.2016.05.017.
Huang, Ping, Takai, Yoshiki, Kusano-Arai, Osamu, Ramadhanti, Julia, Iwanari, Hiroko, Miyauchi, Takayuki, Sakihama, Toshiko, Han, Jing-Yan, Aoki, Masashi, Hamakubo, Takao, Fujihara, Kazuo, Yasui, Masato, and Abe, Yoichiro. 2016. "The binding property of a monoclonal antibody against the extracellular domains of aquaporin-4 directs aquaporin-4 toward endocytosis". Netherlands. doi:10.1016/j.bbrep.2016.05.017.
@article{osti_1254670,
title = {The binding property of a monoclonal antibody against the extracellular domains of aquaporin-4 directs aquaporin-4 toward endocytosis},
author = {Huang, Ping and Takai, Yoshiki and Kusano-Arai, Osamu and Ramadhanti, Julia and Iwanari, Hiroko and Miyauchi, Takayuki and Sakihama, Toshiko and Han, Jing-Yan and Aoki, Masashi and Hamakubo, Takao and Fujihara, Kazuo and Yasui, Masato and Abe, Yoichiro},
abstractNote = {},
doi = {10.1016/j.bbrep.2016.05.017},
journal = {Biochemistry and Biophysics Reports},
number = C,
volume = 7,
place = {Netherlands},
year = 2016,
month = 9
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record at 10.1016/j.bbrep.2016.05.017

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  • The properties of (/sup 125/I)beta h-endorphin-binding sites from rat brain membranes and membranes from the NG108-15 cell line were compared using a monoclonal antibody directed against the opioid receptor and opioid peptides as probes. The binding of (/sup 125/I)beta h-endorphin to both rat brain and NG108-15 membranes yielded linear Scatchard plots with Kd values of 1.2 nM and 1.5 nM, respectively, and Bmax values of 865 fmol/mg rat brain membrane protein and 1077 fmol/mg NG108-15 membrane protein. A monoclonal antibody, OR-689.2.4, capable of inhibiting mu and delta binding but not kappa binding to rat brain membranes, noncompetitively inhibited the bindingmore » of 1 nM (/sup 125/I)beta h-endorphin to rat brain and NG108-15 membranes with an IC50 value of 405 nM for rat brain membranes and 543 nM for NG108-15 membranes. The monoclonal antibody also inhibited the binding of 3 nM (/sup 3/H) (D-penicillamine2, D-penicillamine5) enkephalin to NG108-15 membranes with an IC50 value of 370 nM. In addition to blocking the binding of (/sup 125/I)beta h-endorphin to brain membranes, the antibody also displaced (/sup 125/I)beta h-endorphin from membranes. Site-specific opioid peptides had large variations in their IC50 values depending on whether they were inhibiting (/sup 125/I)beta h-endorphin binding to rat brain or the NG108-15 membranes. When the peptides were tested with the monoclonal antibody for their combined ability to inhibit (/sup 125/I)beta h-endorphin binding to both membrane preparations, the peptides and antibody blocked binding as though they were acting at allosterically coupled sites, not two totally independent sites. These studies suggest that mu-, delta-, and beta-endorphin-binding sites share some sequence homology with the 35,000-dalton protein that the antibody is directed against.« less
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