Myofibrillar regulation of contraction as revealed with phallotoxins

A. E. Bukatina, Gary C Sieck

Research output: Contribution to journalArticle

Abstract

The thin filament regulation of striated muscle contraction involves activation of the thin filament by both Ca2+ and strongly bound myosin cross-bridges (XBs). Phallotoxins cause a variety of specific changes in myofibrillar functioning, being a potentially valuable tool for muscle research. There are two very distinct classes of agents among phallotoxins. One is the more recently discovered secophalloidin group. The unique property of secophalloidin is muscle activation without Ca2+, possibly by direct influence on actomyosin interaction. These drugs appear to be especially useful for studying the role of XBs in muscle regulation. The other is the phalloidin group, which includes the majority of phallotoxins. Binding to the phalloidin site on F-actin, they cause muscle-specific changes. In cardiac muscle they work as Ca2+ sensitizers, increasing both the maximal force and the Ca2+ sensitivity. A particular advantage of these drugs is that the target site is known, which gives an opportunity to unravel the sequence of molecular events leading to increased contractile function. The complex effect of phalloidin in skeletal muscle most probably involves disturbance of the actin-nebulin interaction, and this may help clarify the role of nebulin in regulating contraction.

Original languageEnglish (US)
Pages (from-to)1003-1010
Number of pages8
JournalBiophysics
Volume48
Issue number6
StatePublished - 2003

Fingerprint

Phalloidine
Muscles
Actins
Actomyosin
Striated Muscle
Myosins
Muscle Contraction
Pharmaceutical Preparations
Myocardium
Skeletal Muscle
phallotoxin
Research
nebulin

Keywords

  • Calcium sensitizers
  • Cross-bridges
  • F-actin stabilization
  • Phalloidin
  • Secophalloidin
  • Thin filament

ASJC Scopus subject areas

  • Biophysics

Cite this

Bukatina, A. E., & Sieck, G. C. (2003). Myofibrillar regulation of contraction as revealed with phallotoxins. Biophysics, 48(6), 1003-1010.

Myofibrillar regulation of contraction as revealed with phallotoxins. / Bukatina, A. E.; Sieck, Gary C.

In: Biophysics, Vol. 48, No. 6, 2003, p. 1003-1010.

Research output: Contribution to journalArticle

Bukatina, AE & Sieck, GC 2003, 'Myofibrillar regulation of contraction as revealed with phallotoxins', Biophysics, vol. 48, no. 6, pp. 1003-1010.
Bukatina, A. E. ; Sieck, Gary C. / Myofibrillar regulation of contraction as revealed with phallotoxins. In: Biophysics. 2003 ; Vol. 48, No. 6. pp. 1003-1010.
@article{6c1bf32b9ee64e6a86306456ff899057,
title = "Myofibrillar regulation of contraction as revealed with phallotoxins",
abstract = "The thin filament regulation of striated muscle contraction involves activation of the thin filament by both Ca2+ and strongly bound myosin cross-bridges (XBs). Phallotoxins cause a variety of specific changes in myofibrillar functioning, being a potentially valuable tool for muscle research. There are two very distinct classes of agents among phallotoxins. One is the more recently discovered secophalloidin group. The unique property of secophalloidin is muscle activation without Ca2+, possibly by direct influence on actomyosin interaction. These drugs appear to be especially useful for studying the role of XBs in muscle regulation. The other is the phalloidin group, which includes the majority of phallotoxins. Binding to the phalloidin site on F-actin, they cause muscle-specific changes. In cardiac muscle they work as Ca2+ sensitizers, increasing both the maximal force and the Ca2+ sensitivity. A particular advantage of these drugs is that the target site is known, which gives an opportunity to unravel the sequence of molecular events leading to increased contractile function. The complex effect of phalloidin in skeletal muscle most probably involves disturbance of the actin-nebulin interaction, and this may help clarify the role of nebulin in regulating contraction.",
keywords = "Calcium sensitizers, Cross-bridges, F-actin stabilization, Phalloidin, Secophalloidin, Thin filament",
author = "Bukatina, {A. E.} and Sieck, {Gary C}",
year = "2003",
language = "English (US)",
volume = "48",
pages = "1003--1010",
journal = "Biophysics (Russian Federation)",
issn = "0006-3509",
publisher = "Maik Nauka-Interperiodica Publishing",
number = "6",

}

TY - JOUR

T1 - Myofibrillar regulation of contraction as revealed with phallotoxins

AU - Bukatina, A. E.

AU - Sieck, Gary C

PY - 2003

Y1 - 2003

N2 - The thin filament regulation of striated muscle contraction involves activation of the thin filament by both Ca2+ and strongly bound myosin cross-bridges (XBs). Phallotoxins cause a variety of specific changes in myofibrillar functioning, being a potentially valuable tool for muscle research. There are two very distinct classes of agents among phallotoxins. One is the more recently discovered secophalloidin group. The unique property of secophalloidin is muscle activation without Ca2+, possibly by direct influence on actomyosin interaction. These drugs appear to be especially useful for studying the role of XBs in muscle regulation. The other is the phalloidin group, which includes the majority of phallotoxins. Binding to the phalloidin site on F-actin, they cause muscle-specific changes. In cardiac muscle they work as Ca2+ sensitizers, increasing both the maximal force and the Ca2+ sensitivity. A particular advantage of these drugs is that the target site is known, which gives an opportunity to unravel the sequence of molecular events leading to increased contractile function. The complex effect of phalloidin in skeletal muscle most probably involves disturbance of the actin-nebulin interaction, and this may help clarify the role of nebulin in regulating contraction.

AB - The thin filament regulation of striated muscle contraction involves activation of the thin filament by both Ca2+ and strongly bound myosin cross-bridges (XBs). Phallotoxins cause a variety of specific changes in myofibrillar functioning, being a potentially valuable tool for muscle research. There are two very distinct classes of agents among phallotoxins. One is the more recently discovered secophalloidin group. The unique property of secophalloidin is muscle activation without Ca2+, possibly by direct influence on actomyosin interaction. These drugs appear to be especially useful for studying the role of XBs in muscle regulation. The other is the phalloidin group, which includes the majority of phallotoxins. Binding to the phalloidin site on F-actin, they cause muscle-specific changes. In cardiac muscle they work as Ca2+ sensitizers, increasing both the maximal force and the Ca2+ sensitivity. A particular advantage of these drugs is that the target site is known, which gives an opportunity to unravel the sequence of molecular events leading to increased contractile function. The complex effect of phalloidin in skeletal muscle most probably involves disturbance of the actin-nebulin interaction, and this may help clarify the role of nebulin in regulating contraction.

KW - Calcium sensitizers

KW - Cross-bridges

KW - F-actin stabilization

KW - Phalloidin

KW - Secophalloidin

KW - Thin filament

UR - http://www.scopus.com/inward/record.url?scp=33750515251&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33750515251&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:33750515251

VL - 48

SP - 1003

EP - 1010

JO - Biophysics (Russian Federation)

JF - Biophysics (Russian Federation)

SN - 0006-3509

IS - 6

ER -