188 results found
Purcell IF, Bing W, Marston SB, 1999, Functional analysis of human cardiac troponin by the in vitro motility assay: comparison of adult, foetal and failing hearts, CARDIOVASCULAR RESEARCH, Vol: 43, Pages: 884-891, ISSN: 0008-6363
Krymsky MA, Chibalina MV, Shirinsky VP, et al., 1999, Evidence against the regulation of caldesmon inhibitory activity by p42/p44(erk) mitogen-activated protein kinase in vitro and demonstration of another caldesmon kinase in intact gizaard smooth muscle, FEBS LETTERS, Vol: 452, Pages: 254-258, ISSN: 0014-5793
Burton DJ, Marston SB, 1999, Control of shortening speed in single guinea-pig taenia coli smooth muscle cells by Ca2+, phosphorylation and caldesmon, PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY, Vol: 437, Pages: 267-275, ISSN: 0031-6768
Marston S, Burton D, Copeland O, et al., 1998, Structural interactions between actin, tropomyosin, caldesmon and calcium binding protein and the regulation of smooth muscle thin filaments, ACTA PHYSIOLOGICA SCANDINAVICA, Vol: 164, Pages: 401-414, ISSN: 0001-6772
Bing W, Razzaq A, Sparrow J, et al., 1998, Tropomyosin and troponin regulation of wild type and E93K mutant actin filaments from Drosophila flight muscle - Charge reversal on actin changes actin-tropomyosin from on to off state, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 273, Pages: 15016-15021, ISSN: 0021-9258
El-Mezgueldi M, Copeland O, Fraser IDC, et al., 1998, Characterization of the functional properties of smooth muscle caldesmon domain 4a: evidence for an independent inhibitory actin-tropomyosin binding domain, BIOCHEMICAL JOURNAL, Vol: 332, Pages: 395-401, ISSN: 0264-6021
Huber PAJ, Gao Y, Fraser IDC, et al., 1998, Structure-activity studies of the regulatory interaction of the 10 kilodalton C-terminal fragment of Caldesmon with actin and the effect of mutation of Caldesmon residues 691-696, BIOCHEMISTRY, Vol: 37, Pages: 2314-2326, ISSN: 0006-2960
Huber PAJ, Levine BA, Copeland O, et al., 1998, Characterisation of the effects of mutation of the caldesmon sequence (691)glu-trp-leu-thr-lys-thr(696) to pro-gly-his-tyr-asn-asn on caldesmon-calmodulin interaction, FEBS LETTERS, Vol: 423, Pages: 93-97, ISSN: 0014-5793
Polyakov AA, Huber PAJ, Marston SB, et al., 1998, Interaction of isoforms of S100 protein with smooth muscle caldesmon, FEBS LETTERS, Vol: 422, Pages: 235-239, ISSN: 1873-3468
Vorotnikov AV, Marston SB, Huber PAJ, 1997, Location and functional characterization of myosin contact sites in smooth-muscle caldesmon, BIOCHEMICAL JOURNAL, Vol: 328, Pages: 211-218, ISSN: 0264-6021
Hodgkinson JL, ElMezgueldi M, Craig R, et al., 1997, 3-D image reconstruction of reconstituted smooth muscle thin filaments containing calponin: Visualization of interactions between F-actin and calponin, JOURNAL OF MOLECULAR BIOLOGY, Vol: 273, Pages: 150-159, ISSN: 0022-2836
Bing W, Fraser IDC, Marston SB, 1997, Troponin I and troponin T interact with troponin C to produce different Ca2+-dependent effects on actin-tropomyosin filament motility, BIOCHEMICAL JOURNAL, Vol: 327, Pages: 335-340, ISSN: 0264-6021
Bing W, Redwood CS, Purcell IF, et al., 1997, Effects of two hypertrophic cardiomyopathy mutations in alpha-tropomyosin, Asp175Asn and Glu180Gly, on Ca2+ regulation of thin filament motility, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, Vol: 236, Pages: 760-764, ISSN: 0006-291X
Hodgkinson JL, Marston SB, Craig R, et al., 1997, Three-dimensional image reconstruction of reconstituted smooth muscle thin filaments: Effects of caldesmon, BIOPHYSICAL JOURNAL, Vol: 72, Pages: 2398-2404, ISSN: 0006-3495
Medvedeva MV, Kolobova EA, Huber PAJ, et al., 1997, Mapping of contact sites in the caldesmon-calmodulin complex, BIOCHEMICAL JOURNAL, Vol: 324, Pages: 255-262, ISSN: 0264-6021
Fraser IDC, Copeland O, Wu B, et al., 1997, The inhibitory complex of smooth muscle caldesmon with actin and tropomyosin involves three interacting segments of the C-terminal domain 4, BIOCHEMISTRY, Vol: 36, Pages: 5483-5492, ISSN: 0006-2960
ElMezgueldi M, Marston SB, 1996, The effects of smooth muscle calponin on the strong and weak myosin binding sites of F-actin, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 271, Pages: 28161-28167, ISSN: 0021-9258
Hnath EJ, Wang CLA, Huber PAJ, et al., 1996, Affinity and structure of complexes of tropomyosin and caldesmon domains, BIOPHYSICAL JOURNAL, Vol: 71, Pages: 1920-1933, ISSN: 0006-3495
Marston SB, Fraser IDC, Bing W, et al., 1996, A simple method for automatic tracking of actin filaments in the motility assay, JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY, Vol: 17, Pages: 497-506, ISSN: 0142-4319
Huber PAJ, ElMezgueldi M, Grabarek Z, et al., 1996, Multiple-sited interaction of caldesmon with Ca2(+)-calmodulin, BIOCHEMICAL JOURNAL, Vol: 316, Pages: 413-420, ISSN: 0264-6021
Huber PA, Fraser ID, Marston SB, 1995, Location of smooth-muscle myosin and tropomyosin binding sites in the C-terminal 288 residues of human caldesmon., Biochem J, Vol: 312 ( Pt 2), Pages: 617-625, ISSN: 0264-6021
We have produced nine recombinant fragments, H1 to H9, from a human cDNA that codes for the C-terminal 288 residues of caldesmon. The fragment H1, encompassing the 288 residues, is equivalent to domains 3 and 4 of caldesmon (amino acids 506-793 in human, 476-737 in the chicken gizzard sequence). It has been shown [Huber, Redwood, Avent, Tanner and Marston (1993) J. Muscle Res. Cell Motil. 14, 385-391] to bind to actin, Ca(2+)-calmodulin, tropomyosin and myosin. The fragments, H2 to H9, differ in length between 60 and 176 residues and cover the whole of domains 3 and 4 with many of the fragments overlapping. We have characterized the myosin and tropomyosin binding of these fragments. The binding of both tropomyosin and myosin is highly dependent on salt concentration, indicating the ionic nature of these interactions. The location of the myosin binding is an extended region encompassing the junction of domains 3/4 and domain 4a (residues 622-714, human; 566-657, chicken gizzard). Tropomyosin binds in a smaller region within domain 4a of caldesmon (residues 663-714, human; 606-657 chicken gizzard). We confirmed predictions based on sequence similarities of a tropomyosin binding site in domain 3 of caldesmon; however, this site bound to skeletal-muscle tropomyosin and had little affinity for the smooth-muscle tropomyosin isoform. None of the protein fragments H2-H9 retained the affinity of the parent fragment H1 for either myosin or tropomyosin. This indicates the need for several interaction sites scattered over an extended region to attain higher affinity. The regions interacting with caldesmon in both tropomyosin and myosin are coiled-coil structures. This is probably the reason for their shared interaction sites on caldesmon and their similar natures of binding.
Tini M, Fraser RA, Giguère V, 1995, Functional Interactions between Retinoic Acid Receptor-related Orphan Nuclear Receptor (RORα) and the Retinoic Acid Receptors in the Regulation of the γF-Crystallin Promoter, Journal of Biological Chemistry, Vol: 270, Pages: 20156-20161, ISSN: 0021-9258
FRASER IDC, MARSTON SB, 1995, IN-VITRO MOTILITY ANALYSIS OF SMOOTH-MUSCLE CALDESMON CONTROL OF ACTIN-TROPOMYOSIN FILAMENT MOVEMENT, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 270, Pages: 19688-19693, ISSN: 0021-9258
Fraser ID, Marston SB, 1995, In vitro motility analysis of actin-tropomyosin regulation by troponin and calcium. The thin filament is switched as a single cooperative unit., J Biol Chem, Vol: 270, Pages: 7836-7841, ISSN: 0021-9258
In striated muscles, contractility is controlled by Ca2+ binding to the regulatory protein complex troponin, which is a component of the thin filaments. Troponin is an allosteric inhibitor acting on tropomyosin to switch the thin filament between "on" and "off" states. We have used an in vitro motility assay to examine troponin regulation of individual actin-tropomyosin filaments moving over immobilized skeletal muscle heavy meromyosin. The most striking observation is that the actintropomyosin filament appears to be regulated as a single unit. At pCa 9.0, addition of up to 4 nM troponin causes the proportion of filaments motile to decrease from > 85% to 20% with no dissociation of the filaments from the heavy meromyosin surface or change in velocity. Increasing Ca2+ concentration causes the filaments to be switched back on with half-maximal increase in the proportion of filaments motile at pCa 5.8-6.0 and a modest increase in filament velocity. This is an "all or none" process in which an entire filament, up to 15 microns long, switches rapidly as a single cooperative unit. Thus, the effect of Ca2+ upon the thin filament is to recruit motile filaments.
HODGKINSON JL, NEWMAN TM, MARSTON SB, et al., 1995, THE STRUCTURE OF THE CONTRACTILE APPARATUS IN ULTRARAPIDLY FROZEN SMOOTH-MUSCLE - FREEZE-FRACTURE, DEEP-ETCH, AND FREEZE-SUBSTITUTION STUDIES, JOURNAL OF STRUCTURAL BIOLOGY, Vol: 114, Pages: 93-104, ISSN: 1047-8477
Marston S, 1995, Ca(2+)-dependent protein switches in actomyosin based contractile systems., Int J Biochem Cell Biol, Vol: 27, Pages: 97-108, ISSN: 1357-2725
Myosin is an ATPase enzyme with the unique property that the hydrolysis and release of Pi and ADP is coupled to movement via a cyclic interaction between myosin and actin filaments. Recent evidence indicates that for all myosin and myosin-like molecules, from slime mould and spinach vacuole to man, the mechanism of the molecular motor is essentially the same. It is now appropriate to ask general questions about how these motors are regulated by Ca2+. Is regulation the same throughout nature or are there different proteins in different phyla independently evolved? It is possible to define two basic mechanisms. Myosin may be regulated by EF hand Ca2+ binding proteins interacting with the regulatory domain or the thin filament activity may be regulated by accessory proteins. In this review I have analysed examples of myosin and actin-linked regulatory systems in order to determine the basic principles of the mechanism of these protein switches. I propose three principles common to all myosin-linked regulatory systems: (1) the regulatory proteins inhibit the cycling of a constitutively active myosin motor domain; (2) a regulatory domain in the myosin molecule has several special motifs ("IQ motif") which form binding sites for regulatory proteins; and (3) the regulatory proteins bound to the heavy chain are "EF hand" proteins related to calmodulin. I also propose a common set of principles for actin-linked regulatory systems: (1) the actin filament is normally capable of interacting with myosin to produce movement and the regulatory proteins inhibit the interaction; (2) inhibitory proteins are controlled by interaction with Ca(2+)-binding "EF hand" proteins; and (3) regulation is cooperative; the inhibitory proteins act as allosteric effectors of actin-tropomyosin state. The elongated tropomyosin propagates signals over many actins. It seems likely that myosin-linked regulation is of ancient origin. The origin of thin filament regulation is
Payne AM, Yue P, Pritchard K, et al., 1995, Caldesmon mRNA splicing and isoform expression in mammalian smooth-muscle and non-muscle tissues., Biochem J, Vol: 305 ( Pt 2), Pages: 445-450, ISSN: 0264-6021
The recent determination of the genomic sequence of human caldesmon indicates that eight caldesmon mRNA species could be generated by selection of exon 1 or 1', exon 3a or 3ab and/or exon 4. We used reverse transcriptase PCR to determine which transcripts were produced in human, rabbit and sheep artery, vein, lung, intestine, kidney and liver. In all tissues the same three transcripts were present: exons 1'-2-3a-5-6...13, exons 1'-2-3a3b-5-6-...13 and exons 1'-2-3a3b-4-5-6...13. Exon 1 was not present and exon 4 was only present when exon 3b was also present. Three protein isoforms of caldesmon can be distinguished by electrophoresis on high-porosity 6% polyacrylamide gel: 130 kDa, 120 kDa and 70 kDa. The 70 kDa isoform lacks the sequence encoded by exon 3b. We investigated whether the two high-molecular-mass isoforms correspond to the presence and absence of exon 4 using an antiserum specific to the sequence encoded by exon 4. Western-blotting and immunoprecipitation experiments showed that both the 130 kDa and the 120 kDa isoforms were expressed with and without the exon 4 sequence. We therefore propose that the molecular-mass heterogeneity arises from additional first exons, possibly with separate promoter regions, which have not yet been characterized in the genomic sequence.
Marston SB, Fraser ID, Huber PA, 1994, Smooth muscle caldesmon controls the strong binding interaction between actin-tropomyosin and myosin., J Biol Chem, Vol: 269, Pages: 32104-32109, ISSN: 0021-9258
We have demonstrated that caldesmon does not alter the affinity of weak binding actomyosin complexes when it inhibits actin-tropomyosin activation at physiological ratios (1 per 14 actins), and we proposed that it acts upon the strong binding complexes in the same way that troponin-tropomyosin does. We therefore compared the effect of caldesmon, caldesmon fragments, and troponin upon the interaction of the strongly bound complexes S-1.ADP, S-1.adenylyl imidodiphosphate (AMP.PNP), and N-ethylmaleimide-treated myosin subfragment-1 (NEM-S-1) with actin-tropomyosin. In 0.17 M ionic strength buffer [14C]iodoacetamide-labeled S1.ADP bound to actin-smooth muscle tropomyosin with no evidence of cooperativity; Kd = 0.8 +/- 0.3 microM (n = 5). Inhibitory concentrations of sheep aorta caldesmon or rabbit skeletal muscle troponin made the binding highly cooperative. At low levels of saturation the apparent Kd was 10-40 microM with 10 microM caldesmon and 8-20 microM with 6 microM troponin; at > 50% saturation the binding was indistinguishable from actin-tropomyosin alone. A similar result was obtained for the binding of [14C]iodoacetamide-labeled S-1.AMP.PNP to actin-smooth muscle tropomyosin at 0.03 M ionic strength (Kd = 0.47 +/- 0.05 microM). Binding was slightly cooperative and became highly cooperative in the presence of inhibitory concentrations of troponin, caldesmon, and the human caldesmon fragments H7 (amino acids 622-767) and H9 (amino acids 726-793). We conclude that caldesmon and troponin both act as allosteric effectors of the "on"/"off" equilibrium of actin-tropomyosin. 0.1 NEM-S-1/actin potentiated actin-smooth muscle tropomyosin activation of myosin MgATPase 7-fold at 0.03 M ionic strength. Caldesmon inhibited the ATPase in the presence and absence of 0.5 microM NEM-S-1. NEM-S-1 reactivated actin-tropomyosin, which had been inhibited by troponin, caldesmon, H7, or H9. This is compatible with opposing effects of NEM-S-1 and caldesmon or tr
Reckless J, Fleetwood G, Tilling L, et al., 1994, Changes in the caldesmon isoform content and intimal thickening in the rabbit carotid artery induced by a silicone elastomer collar., Arterioscler Thromb, Vol: 14, Pages: 1837-1845, ISSN: 1049-8834
The presence of a silicone elastomer collar around one carotid artery of a rabbit induces thickening of the tunica intima. We used immunoblotting to study quantitatively changes in the isoforms of caldesmon, a protein implicated in the regulation of contractility in smooth muscle, while also monitoring the histological changes during 28 days after collaring. Control rabbit carotid arteries (n = 28) contained 245 +/- 6.4 nmol/g protein of the larger isoform of caldesmon (CDh) and 68.3 +/- 3.6 nmol/g protein of the smaller isoform (CD1). Four days after collaring, intimal thickening was slight, but 44% of arterial CDh had been lost; this loss of CDh was therefore from the tunica media. At 10 days, CDh fell to 37% of the control level. Immunofluorescence using CDh-specific antibodies showed that the CDh level was diminished but remained uniform across the wall of collared arteries. At 14 days, when intimal thickening was maximal, there was 30% more CD1 than in controls. At 28 days, the neointima had thinned, and CD1 had fallen to below control levels. Thus, CD1 levels reflected the development and regression of neointima. Changes in caldesmon isoforms showed that smooth muscle cell phenotypic changes occurred throughout the arterial wall.
HODGKINSON JL, SEVERS NJ, NEWMAN TM, et al., 1994, ULTRASTRUCTURE OF THE CONTRACTILE APPARATUS IN TRITON-EXTRACTED SMOOTH-MUSCLE AND INTACT ULTRARAPIDLY FROZEN SMOOTH-MUSCLE, JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY, Vol: 15, Pages: 218-219, ISSN: 0142-4319
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