Synthetic peptides of actin-tropomyosin binding region of troponin 1 and heat shock protein 20 modulate the relaxation process of skinned preparations of taenia caeci from guinea pig

Yasumasa Yoshino, Wataru Sakurai, Sachio Morimoto, Masaru Watanabe

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

To explore the possible role of the thin filament-linked regulation of cross-bridge cycling in living smooth muscle contraction, we studied the effects of Tnlp and HSP20p, a synthetic peptide originating from an actin tropomyosin binding region of rabbit cardiac troponin I (residues 136-147; GKFKRPTLRRVR), and that of human heat shock protein 20 (residues 110-121; GFVAREFHRRYR) on the relaxation of skinned (cell membrane ilized) preparations from guinea pig taenia caeci. An active stress of the skinned preparations, resulting from actin-myosin interaction, rapidly decayed following Ca2+ removal (relaxation). Tnlp accelerated the initial rapid phase and slowed the following slow phase of the relaxation. On the other hand, HSP20p only slowed the whole process of the relaxation. The relaxation time courses were well fitted in a double exponential manner, and the double exponential decay of the stress could be explained as a portion of fast-detaching cross bridges not to dissociate rapidly by Ca2+ removal, but to transfer to latch bridges dissociating very slowly. Our present results suggested that (i) Tnlp and HSP20p accelerated transferring from fast-detaching cross bridges to slow-detaching (latch) bridges, and (ii) Tnlp accelerated dissociation of the fast-detaching cross bridges and the latch bridges, while HSP20p slowed dissociation of the fast-detaching cross bridges. Since Tnlp and HSP20p are thought to bind to actin and tropomyosin, but not to myosin, we concluded that through thin-filament-dependent mechanisms these peptides regulated the formation and/or deformation of latch bridges in smooth muscle. The thin-filament-dependent regulation might physiologically control the stress maintenance and relaxation in smooth muscle cells.

Original languageEnglish
Pages (from-to)373-378
Number of pages6
JournalJapanese Journal of Physiology
Volume55
Issue number6
DOIs
Publication statusPublished - Dec 1 2005

Fingerprint

HSP20 Heat-Shock Proteins
Taenia
Tropomyosin
Troponin
Actins
Guinea Pigs
Myosins
Peptides
Smooth Muscle
Troponin I
Muscle Contraction
Smooth Muscle Myocytes
Maintenance
Cell Membrane
Rabbits

All Science Journal Classification (ASJC) codes

  • Physiology

Cite this

Synthetic peptides of actin-tropomyosin binding region of troponin 1 and heat shock protein 20 modulate the relaxation process of skinned preparations of taenia caeci from guinea pig. / Yoshino, Yasumasa; Sakurai, Wataru; Morimoto, Sachio; Watanabe, Masaru.

In: Japanese Journal of Physiology, Vol. 55, No. 6, 01.12.2005, p. 373-378.

Research output: Contribution to journalArticle

@article{616befa8310646759b6884b1a0c879a0,
title = "Synthetic peptides of actin-tropomyosin binding region of troponin 1 and heat shock protein 20 modulate the relaxation process of skinned preparations of taenia caeci from guinea pig",
abstract = "To explore the possible role of the thin filament-linked regulation of cross-bridge cycling in living smooth muscle contraction, we studied the effects of Tnlp and HSP20p, a synthetic peptide originating from an actin tropomyosin binding region of rabbit cardiac troponin I (residues 136-147; GKFKRPTLRRVR), and that of human heat shock protein 20 (residues 110-121; GFVAREFHRRYR) on the relaxation of skinned (cell membrane ilized) preparations from guinea pig taenia caeci. An active stress of the skinned preparations, resulting from actin-myosin interaction, rapidly decayed following Ca2+ removal (relaxation). Tnlp accelerated the initial rapid phase and slowed the following slow phase of the relaxation. On the other hand, HSP20p only slowed the whole process of the relaxation. The relaxation time courses were well fitted in a double exponential manner, and the double exponential decay of the stress could be explained as a portion of fast-detaching cross bridges not to dissociate rapidly by Ca2+ removal, but to transfer to latch bridges dissociating very slowly. Our present results suggested that (i) Tnlp and HSP20p accelerated transferring from fast-detaching cross bridges to slow-detaching (latch) bridges, and (ii) Tnlp accelerated dissociation of the fast-detaching cross bridges and the latch bridges, while HSP20p slowed dissociation of the fast-detaching cross bridges. Since Tnlp and HSP20p are thought to bind to actin and tropomyosin, but not to myosin, we concluded that through thin-filament-dependent mechanisms these peptides regulated the formation and/or deformation of latch bridges in smooth muscle. The thin-filament-dependent regulation might physiologically control the stress maintenance and relaxation in smooth muscle cells.",
author = "Yasumasa Yoshino and Wataru Sakurai and Sachio Morimoto and Masaru Watanabe",
year = "2005",
month = "12",
day = "1",
doi = "10.2170/jjphysiol.RP002605",
language = "English",
volume = "55",
pages = "373--378",
journal = "Journal of Physiological Sciences",
issn = "1880-6546",
publisher = "Springer Japan",
number = "6",

}

TY - JOUR

T1 - Synthetic peptides of actin-tropomyosin binding region of troponin 1 and heat shock protein 20 modulate the relaxation process of skinned preparations of taenia caeci from guinea pig

AU - Yoshino, Yasumasa

AU - Sakurai, Wataru

AU - Morimoto, Sachio

AU - Watanabe, Masaru

PY - 2005/12/1

Y1 - 2005/12/1

N2 - To explore the possible role of the thin filament-linked regulation of cross-bridge cycling in living smooth muscle contraction, we studied the effects of Tnlp and HSP20p, a synthetic peptide originating from an actin tropomyosin binding region of rabbit cardiac troponin I (residues 136-147; GKFKRPTLRRVR), and that of human heat shock protein 20 (residues 110-121; GFVAREFHRRYR) on the relaxation of skinned (cell membrane ilized) preparations from guinea pig taenia caeci. An active stress of the skinned preparations, resulting from actin-myosin interaction, rapidly decayed following Ca2+ removal (relaxation). Tnlp accelerated the initial rapid phase and slowed the following slow phase of the relaxation. On the other hand, HSP20p only slowed the whole process of the relaxation. The relaxation time courses were well fitted in a double exponential manner, and the double exponential decay of the stress could be explained as a portion of fast-detaching cross bridges not to dissociate rapidly by Ca2+ removal, but to transfer to latch bridges dissociating very slowly. Our present results suggested that (i) Tnlp and HSP20p accelerated transferring from fast-detaching cross bridges to slow-detaching (latch) bridges, and (ii) Tnlp accelerated dissociation of the fast-detaching cross bridges and the latch bridges, while HSP20p slowed dissociation of the fast-detaching cross bridges. Since Tnlp and HSP20p are thought to bind to actin and tropomyosin, but not to myosin, we concluded that through thin-filament-dependent mechanisms these peptides regulated the formation and/or deformation of latch bridges in smooth muscle. The thin-filament-dependent regulation might physiologically control the stress maintenance and relaxation in smooth muscle cells.

AB - To explore the possible role of the thin filament-linked regulation of cross-bridge cycling in living smooth muscle contraction, we studied the effects of Tnlp and HSP20p, a synthetic peptide originating from an actin tropomyosin binding region of rabbit cardiac troponin I (residues 136-147; GKFKRPTLRRVR), and that of human heat shock protein 20 (residues 110-121; GFVAREFHRRYR) on the relaxation of skinned (cell membrane ilized) preparations from guinea pig taenia caeci. An active stress of the skinned preparations, resulting from actin-myosin interaction, rapidly decayed following Ca2+ removal (relaxation). Tnlp accelerated the initial rapid phase and slowed the following slow phase of the relaxation. On the other hand, HSP20p only slowed the whole process of the relaxation. The relaxation time courses were well fitted in a double exponential manner, and the double exponential decay of the stress could be explained as a portion of fast-detaching cross bridges not to dissociate rapidly by Ca2+ removal, but to transfer to latch bridges dissociating very slowly. Our present results suggested that (i) Tnlp and HSP20p accelerated transferring from fast-detaching cross bridges to slow-detaching (latch) bridges, and (ii) Tnlp accelerated dissociation of the fast-detaching cross bridges and the latch bridges, while HSP20p slowed dissociation of the fast-detaching cross bridges. Since Tnlp and HSP20p are thought to bind to actin and tropomyosin, but not to myosin, we concluded that through thin-filament-dependent mechanisms these peptides regulated the formation and/or deformation of latch bridges in smooth muscle. The thin-filament-dependent regulation might physiologically control the stress maintenance and relaxation in smooth muscle cells.

UR - http://www.scopus.com/inward/record.url?scp=33646232946&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33646232946&partnerID=8YFLogxK

U2 - 10.2170/jjphysiol.RP002605

DO - 10.2170/jjphysiol.RP002605

M3 - Article

C2 - 16417677

AN - SCOPUS:33646232946

VL - 55

SP - 373

EP - 378

JO - Journal of Physiological Sciences

JF - Journal of Physiological Sciences

SN - 1880-6546

IS - 6

ER -