BRAIN ALPHA-BUNGAROTOXIN BINDING-PROTEIN CDNAS AND MABS REVEAL SUBTYPES OF THIS BRANCH OF THE LIGAND-GATED ION CHANNEL GENE SUPERFAMILY
BRAIN ALPHA-BUNGAROTOXIN BINDING-PROTEIN CDNAS AND MABS REVEAL SUBTYPES OF THIS BRANCH OF THE LIGAND-GATED ION CHANNEL GENE SUPERFAMILY
复制标题
DOI:
10.1016/0896-6273(90)90031-a
复制
发表时间:
1990-07-01
期刊:
影响因子:
16.2
通讯作者:
LINDSTROM, J
中科院分区:
文献类型:
--
作者:
SCHOEPFER, R;CONROY, WG;LINDSTROM, J
Summary a-Bungarotoxin (aBgt) is a potent, high-affinity antagonist for nicotinic acetylcholine receptors (AChRs) from muscle, but not for AChRs from neurons. Both muscle and neuronal AChRs are thought to be formed from multiple homologous subunits aligned around a central cation channel whose opening is regulated by ACh binding. In contrast, the exact structure and function of highaffinity aBgt binding proteins (aBgtBPs) found in avian and mammalian neurons remain unknown. Here we show that cDNA clones encoding aBgtBP al and a2 subunits define aBgtBPs as members of a gene family within the ligand-gated ion channel 8ene superfamily, but distinct from the gene families of AChRs from muscles and nerves. Subunit-specific monoclonal antibodies raised against bacterially expressed aBgtBP al and a2 subunit fragments reveal the existence of at least two different aBgtBP subtypes in embryonic day 18 chicken brains. More than 75% of all aBgtBPs have the al subunit, but no a2 subunit, and a minor aBgtBP subtype (~, 15%) has both the al and a2 subunits.