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Effects of the Scorpion Toxin (BmP09) on Muscle Cells in the Tobacco Hawkmoth
Author(s) -
Gerner Emily,
Gerner Zach,
Kim Que,
Speagle Josh,
Vangala Sai,
Shankar Darshan,
Thompson Louise,
Witten Jane
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.lb318
Subject(s) - repolarization , myocyte , scorpion toxin , bk channel , toxin , potassium channel , chemistry , medicine , cardiology , anatomy , pharmacology , venom , electrophysiology , biochemistry , scorpion
A partnership between the Brookfield Central High School students participating in the MSOE SMART Team (Students Modeling a Research Topic) program and a researcher enabled the team to explore the structure and function of a potassium channel bound to a toxin and to build a 3D physical model of the protein. In the larvae of the Tobacco Hawkmoth, the Tobacco Hornworm, the muscle under study is a posture muscle that has a slow recovery (repolarization) rate, and is classified as "slow‐twitch". Metamorphosis transforms this muscle into a flight muscle requiring a fast repolarization rate, becoming a "fast‐twitch" muscle. The repolarization rate of these muscle cells is directly linked to the muscle's rate of contraction. An explosive increase in the number of the Ca 2+ ‐gated K + channels (BK) in these muscles corresponds to these metamorphic changes. The Chinese scorpion toxin BmP09, from Buthus martensi Karsch, will be used to identify the BK channel as responsible for the change from posture to flight muscle. This toxin binds specifically to the BK channel, preventing the channel from removing K + from the cell, slowing repolarization. Binding the toxin to flight muscle, repolarization rates can be studied to determine if the BK channel is involved in the transformation from posture to flight muscle. Supported by a grant from NIH‐NCRR‐SEPA.