Protease inhibitor homologues of dendrotoxin do not bind to dendrotoxin acceptors on synaptosomal membranes or facilitate neuromuscular transmission

D L Marshall, A L Harvey

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

The dendrotoxins are a homologous group of potassium channel-blocking polypeptides found in mamba snake venom. They are similar in sequence and structure to Kunitz-type serine protease inhibitors. Modified and native protease inhibitors were assayed for dendrotoxin-like activity using radioligand-binding and twitch tension-recording methods. Despite the large number and high concentration of compounds tested, no protease inhibitor displayed dendrotoxin-like activity. The results indicate that the protease-inhibiting and potassium channel-blocking activities of these two groups of polypeptides are not linked.
Original languageEnglish
Pages (from-to)707-714
Number of pages8
JournalBiological chemistry Hoppe-Seyler
Volume373
Issue number8
DOIs
Publication statusPublished - 1992

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Protease Inhibitors
Potassium Channels
Membranes
Elapidae
Peptides
Snake Venoms
Serine Proteinase Inhibitors
Peptide Hydrolases
dendrotoxin

Keywords

  • amino acid sequence
  • animals
  • chickens
  • elapid venoms
  • iodine radioisotopes
  • kinetics
  • membranes
  • molecular sequence data
  • muscle contraction
  • neuromuscular junction
  • potassium channels
  • protease inhibitors
  • radioligand assay
  • rats
  • cholinergic receptors
  • structure-activity relationship
  • synaptic transmission
  • synaptosomes

Cite this

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title = "Protease inhibitor homologues of dendrotoxin do not bind to dendrotoxin acceptors on synaptosomal membranes or facilitate neuromuscular transmission",
abstract = "The dendrotoxins are a homologous group of potassium channel-blocking polypeptides found in mamba snake venom. They are similar in sequence and structure to Kunitz-type serine protease inhibitors. Modified and native protease inhibitors were assayed for dendrotoxin-like activity using radioligand-binding and twitch tension-recording methods. Despite the large number and high concentration of compounds tested, no protease inhibitor displayed dendrotoxin-like activity. The results indicate that the protease-inhibiting and potassium channel-blocking activities of these two groups of polypeptides are not linked.",
keywords = "amino acid sequence, animals, chickens, elapid venoms, iodine radioisotopes, kinetics, membranes, molecular sequence data, muscle contraction, neuromuscular junction, potassium channels, protease inhibitors, radioligand assay, rats, cholinergic receptors, structure-activity relationship, synaptic transmission, synaptosomes",
author = "Marshall, {D L} and Harvey, {A L}",
year = "1992",
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language = "English",
volume = "373",
pages = "707--714",
journal = "Biological chemistry Hoppe-Seyler",
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publisher = "Walter de Gruyter GmbH",
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T1 - Protease inhibitor homologues of dendrotoxin do not bind to dendrotoxin acceptors on synaptosomal membranes or facilitate neuromuscular transmission

AU - Marshall, D L

AU - Harvey, A L

PY - 1992

Y1 - 1992

N2 - The dendrotoxins are a homologous group of potassium channel-blocking polypeptides found in mamba snake venom. They are similar in sequence and structure to Kunitz-type serine protease inhibitors. Modified and native protease inhibitors were assayed for dendrotoxin-like activity using radioligand-binding and twitch tension-recording methods. Despite the large number and high concentration of compounds tested, no protease inhibitor displayed dendrotoxin-like activity. The results indicate that the protease-inhibiting and potassium channel-blocking activities of these two groups of polypeptides are not linked.

AB - The dendrotoxins are a homologous group of potassium channel-blocking polypeptides found in mamba snake venom. They are similar in sequence and structure to Kunitz-type serine protease inhibitors. Modified and native protease inhibitors were assayed for dendrotoxin-like activity using radioligand-binding and twitch tension-recording methods. Despite the large number and high concentration of compounds tested, no protease inhibitor displayed dendrotoxin-like activity. The results indicate that the protease-inhibiting and potassium channel-blocking activities of these two groups of polypeptides are not linked.

KW - amino acid sequence

KW - animals

KW - chickens

KW - elapid venoms

KW - iodine radioisotopes

KW - kinetics

KW - membranes

KW - molecular sequence data

KW - muscle contraction

KW - neuromuscular junction

KW - potassium channels

KW - protease inhibitors

KW - radioligand assay

KW - rats

KW - cholinergic receptors

KW - structure-activity relationship

KW - synaptic transmission

KW - synaptosomes

U2 - 10.1515/bchm3.1992.373.2.707

DO - 10.1515/bchm3.1992.373.2.707

M3 - Article

VL - 373

SP - 707

EP - 714

JO - Biological chemistry Hoppe-Seyler

JF - Biological chemistry Hoppe-Seyler

SN - 0177-3593

IS - 8

ER -