NDLI: Antigen Selectivity Characteristic of Polyclonal Antibodies Against Omega-Conotoxin GVIA and N-Type Voltage-Dependent Calcium Channels

Content Provider	Springer Nature Link
Author	Ichida, S. Abe, J. Sugimoto, W. Uematsu, M. Komoike, K. Imoto, K. Mori, M. Wada, T. Minami, T. Kakutani, K.
Copyright Year	2003
Abstract	The antibodies against omega-conotoxin GVIA (ω-CTX GVIA; N-type voltage-dependent calcium channel [VDCC] blocker) and B$_{1}$Nt (N-terminal segment [residues 1–13] of BI α$_{1}$ subunits of VDCCs) were prepared, and the selectivity for each antigen ω-CTX GVIA and B1Nt was investigated. For the antigen selectivity of anti–ω-CTX GVIA antibody against ω-CTX GVIA, ELISA, and immunoprecipitation were used. The reactions for ELISA and immunoprecipitation were observed except when antibody IgG purified by Protein A–Sepharose CL-4B from nonimmunized serum (purified NI-Ab) was used. The specific reactions were inhibited by 10 nM ω-CTX GVIA, but not by ω-CTX SVIB (N-type VDCC blocker), ω-CTX MVIIC (N- and P-type VDCC blocker), or ω-Aga IVA (P-type VDCC blocker). For the antigen selectivity of the anti-B1Nt antibody, analyses by ELISA, immunoprecipitation, and Western blotting were conducted. The reactions were observed except when NI-Ab was used. The ELISA and immunoprecipitation reactions were inhibited by the antigen peptide B1Nt, and the IC$_{50}$ values were about 1.2 × 1028 and 1.3 × 1028 M, respectively. The bands of 210 and 190 kD by Western blotting of crude membranes from chick brain were also inhibited by 1 μM B1Nt. These results suggest that the antibodies prepared against ω-CTX GVIA and B1Nt in this work have high selectivity for their antigen. Therefore we assume that the antibodies against ω-CTX GVIA and B1Nt are useful tools for the analyses of the function and distribution of N-type VDCCs. The anti ω-CTX GVIA antibody must also be useful for the radioimmunoassay of ω-CTX GVIA.
Starting Page	789
Ending Page	796
Page Count	8
File Format	PDF
ISSN	03643190
Journal	Neurochemical Research
Volume Number	28
Issue Number	6
e-ISSN	15736903
Language	English
Publisher	Kluwer Academic Publishers-Plenum Publishers
Publisher Date	2003-01-01
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Neurosciences Neurology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Biochemistry Cellular and Molecular Neuroscience

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Characteristics of Omega-conotoxin GVI A and MVIIC Binding to Ca$_{v}$ 2.1 and Ca$_{v}$ 2.2 Channels Captured by Anti-Ca$^{2+}$ Channel Peptide Antibodies

Calcium/Calmodulin Inhibits the Binding of Specific [125I]Omega-Conotoxin GVIA to Chick Brain Membranes

Structural Specificity for the Inhibitory Effect of Calmodulin on Specific $^{125}$I-Omega-Conotoxin GVIA Binding

Interference between two modulators of N-type (CaV2.2) calcium channel gating demonstrates that ω-conotoxin GVIA disrupts open state gating

Characteristics of the Inhibitory Effect of Calmodulin on Specific [125I]Omega-Conotoxin GVIA Binding to Crude Membranes from Chick Brain

Effects of Calmodulin and Ca$^{2+}$ Channel Blockers on ω-conotoxin GVI A Binding to Crude Membranes from α$_{1B}$ Subunit (Ca$_{v}$2.2) Expressed BHK Cells and Mice Brain Lacking the α$_{1B}$ Subunits

A Confirmation of $^{125}$I-ω-Conotoxin Labeled Sites in a Crude Membrane Fraction from Chick Brain as the α$_{1}$ Subunit of N-Type Calcium Channels

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Effects of omega-conotoxin GVIA and diltiazem on double peaked vasoconstrictor responses to periarterial electric nerve stimulation in isolated canine splenic artery.

Antigen Selectivity Characteristic of Polyclonal Antibodies Against Omega-Conotoxin GVIA and N-Type Voltage-Dependent Calcium Channels

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