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One scorpion, two venoms: Prevenom of Parabuthus transvaalicus acts an alternative type of venom with distinct mechanism of action.

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Title: One scorpion, two venoms: Prevenom of Parabuthus transvaalicus acts an alternative type of venom with distinct mechanism of action.
Authors: Inceoglu, Bora, Lango, Jozsef, Jie Ling, Lili Chen, Doymaz, Fuat, Pessah, Isaac N., Hammock, Bruce D.
Source: Proceedings of the National Academy of Sciences of the United States of America. 2/4/2003, Vol. 100 Issue 3, p922. 6p. 2 Black and White Photographs, 1 Chart, 5 Graphs.
Subjects: Scorpion venom, Salts, Peptides, Proteins
Abstract: Scorpion venom is a complex mixture of salts, small molecules, peptides, and proteins. Scorpions employ this valuable tool in several sophisticated ways for subduing prey, deterring predators, and possibly during mating. Here, a subtle but clever strategy of venom utilization by scorpions is reported. Scorpions secrete a small quantity of transparent venom when initially stimulated that we propose to name prevenom. If secretion continues, a cloudy and dense venom that is white in color is subsequently released. The prevenom contains a combination of high K[sup +] salt and several peptides including some that block rectifying K[sup +] channels and elicit significant pain and toxicity because of a massive local depolarization. The presence of high extracellular K[sup +] in the prevenom can depolarize cells and also decrease the local electrochemical gradient making it more difficult to reestablish the resting potential. When this positive change to the K[sup +] equilibrium potential is combined with the blockage of rectifying K[sup +] channels, this further delays the recovery of the resting potential, causing a prolonged effect. We propose that the prevenom of scorpions is used as a highly efficacious predator deterrent and for immobilizing small prey while conserving metabolically expensive venom until a certain level of stimuli is reached, after which the venom is secreted. [ABSTRACT FROM AUTHOR]
Copyright of Proceedings of the National Academy of Sciences of the United States of America is the property of National Academy of Sciences and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
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DbLabel: Engineering Source
An: 9146895
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PubType: Academic Journal
PubTypeId: academicJournal
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  Data: One scorpion, two venoms: Prevenom of Parabuthus transvaalicus acts an alternative type of venom with distinct mechanism of action.
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  Data: <searchLink fieldCode="AR" term="%22Inceoglu%2C+Bora%22">Inceoglu, Bora</searchLink><br /><searchLink fieldCode="AR" term="%22Lango%2C+Jozsef%22">Lango, Jozsef</searchLink><br /><searchLink fieldCode="AR" term="%22Jie+Ling%22">Jie Ling</searchLink><br /><searchLink fieldCode="AR" term="%22Lili+Chen%22">Lili Chen</searchLink><br /><searchLink fieldCode="AR" term="%22Doymaz%2C+Fuat%22">Doymaz, Fuat</searchLink><br /><searchLink fieldCode="AR" term="%22Pessah%2C+Isaac+N%2E%22">Pessah, Isaac N.</searchLink><br /><searchLink fieldCode="AR" term="%22Hammock%2C+Bruce+D%2E%22">Hammock, Bruce D.</searchLink>
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  Data: <searchLink fieldCode="DE" term="%22Scorpion+venom%22">Scorpion venom</searchLink><br /><searchLink fieldCode="DE" term="%22Salts%22">Salts</searchLink><br /><searchLink fieldCode="DE" term="%22Peptides%22">Peptides</searchLink><br /><searchLink fieldCode="DE" term="%22Proteins%22">Proteins</searchLink>
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  Label: Abstract
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  Data: Scorpion venom is a complex mixture of salts, small molecules, peptides, and proteins. Scorpions employ this valuable tool in several sophisticated ways for subduing prey, deterring predators, and possibly during mating. Here, a subtle but clever strategy of venom utilization by scorpions is reported. Scorpions secrete a small quantity of transparent venom when initially stimulated that we propose to name prevenom. If secretion continues, a cloudy and dense venom that is white in color is subsequently released. The prevenom contains a combination of high K[sup +] salt and several peptides including some that block rectifying K[sup +] channels and elicit significant pain and toxicity because of a massive local depolarization. The presence of high extracellular K[sup +] in the prevenom can depolarize cells and also decrease the local electrochemical gradient making it more difficult to reestablish the resting potential. When this positive change to the K[sup +] equilibrium potential is combined with the blockage of rectifying K[sup +] channels, this further delays the recovery of the resting potential, causing a prolonged effect. We propose that the prevenom of scorpions is used as a highly efficacious predator deterrent and for immobilizing small prey while conserving metabolically expensive venom until a certain level of stimuli is reached, after which the venom is secreted. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
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  Data: <i>Copyright of Proceedings of the National Academy of Sciences of the United States of America is the property of National Academy of Sciences and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1073/pnas.242735499
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        Text: English
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        PageCount: 6
        StartPage: 922
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      – SubjectFull: Scorpion venom
        Type: general
      – SubjectFull: Salts
        Type: general
      – SubjectFull: Peptides
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      – SubjectFull: Proteins
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            NameFull: Lango, Jozsef
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            NameFull: Jie Ling
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              Text: 2/4/2003
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              Y: 2003
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