ライフサイエンスコーパス: caldesmon

1 h the actin-binding proteins tropomyosin and caldesmon.

2 with the myosin-binding domain of endogenous caldesmon.

3 muscle, active crossbridges are inhibited by caldesmon.

4 he bound S1 was resistant to displacement by caldesmon.

5 ause Ca2+/calmodulin blocks actin binding of caldesmon.

6 carotid smooth muscle tissue deficient in h-caldesmon.

7 ay be attached to the NH2-terminal region of caldesmon.

8 ost, but not all, of the S1 was displaced by caldesmon.

9 form of the cytoskeletal regulatory protein caldesmon.

10 activity; i.e., their effect is opposite to caldesmon.

11 ding between calponin and the COOH-domain of caldesmon.

12 RK MAP kinases leading to phosphorylation of caldesmon.

13 d to the strong binding site seen with whole caldesmon.

14 wed homology with the actin-binding protein, caldesmon.

15 ficantly less myosin, actin, calponin, and h-caldesmon.

16 ed inactivation of the actomyosin inhibitor, caldesmon.

17 lecular basis for the inhibitory function of caldesmon.

18 te of S1 binding to actin in the presence of caldesmon.

19 nhibition of actin-myosin ATPase activity by caldesmon.

20 motility that involves, downstream of cdc2, caldesmon.

21 he amino-terminal (myosin-binding) domain of caldesmon.

22 Grb2 and the cytoskeletal regulatory protein caldesmon.

23 n actin-caldesmon but to the displacement of caldesmon.

24 ve binding of S1 to actin in the presence of caldesmon.

25 blocking of myosin binding sites on actin by caldesmon.

26 wever, express the smooth muscle cell marker caldesmon.

27 lls against UVB radiation-induced changes in caldesmon 1 isoform, lamin A/C transcript variant 1, DEA

28 of 0.6 +/- 0.07 to 1.1 +/- 0.15 mol P1 (mol caldesmon)-1 after 2 min.

29 ic studies identified cytoskeletal proteins (caldesmon-1 and vimentin), endoplasmic reticulum protein

30 Unphosphorylated turkey gizzard caldesmon (3 microM) significantly reduced mean sliding

31 Immunoblotting with antisera to caldesmon, a cytoskeletal calmodulin-binding protein of

32 Caldesmon, a narrow, elongated actin-binding protein, is

33 eins as isoforms of the actomyosin regulator caldesmon, a protein known to influence contractility, s

34 results indicate that experiments involving caldesmon, actin, tropomyosin, and myosin are inherently

35 e the structural basis of the multiple-sited caldesmon-actin-tropomyosin interaction.

36 No evidence for a stable caldesmon-actin-tropomyosin-S1 complex was observed, alt

37 tides produced a significant decrease in the caldesmon/actin ratio, but no change was measured in the

38 ot readily explained by a mechanism in which caldesmon acts only by stabilizing an inactive state of

39 that a fragment of the actin-binding protein caldesmon added to polymerizing actin increases the Arp2

40 Caldesmon alone or TM alone has little or no effect on t

41 Whereas smooth muscle caldesmon alone or TM alone shows no effect, caldesmon t

42 eal that, in contrast to the distribution of caldesmon along actin stress fibers in normal fibroblast

43 , and the typical PILS components cortactin, caldesmon, alpha-actinin, N-WASP, Arp-3, and cdc42 coloc

44 Caldesmon also inhibits the binding of myosin to actin.

45 eptides derived from the C-terminus of human caldesmon (amino acids 663-793, domain 4) to determine t

46 tions between calponin, a basic protein, and caldesmon, an acidic protein, contribute to the stabiliz

47 of a 314 amino acid domain with homology to caldesmon, an actin-binding protein, suggesting an inter

48 and absence of tropomyosin with both intact caldesmon and a recombinant 35 kDa actin binding fragmen

49 transfer and disulfide cross-linking between caldesmon and actin.

50 der these conditions the affinities of whole caldesmon and CaD-4 were both in the micromolar range.

51 Overall, these findings suggest that caldesmon and calponin in the amygdala are closely assoc

52 uscle epitopes of alpha-smooth muscle actin, caldesmon and calponin, which localized adjacent and ext

53 indle-shaped cellular appearance, with low l-caldesmon and high calponin-1.

54 istic round shape of VSMCs expressing high l-caldesmon and low calponin-1 (dedifferentiation state) w

55 Two proteins (caldesmon and myeloid nuclear differentiation antigen) w

56 he multiple binding model for the binding of caldesmon and myosin heads to actin.

57 brium measurements of the rate of binding of caldesmon and myosin S1 to actin-tropomyosin from differ

58 CPASMCs and intact CPAs expressed h-caldesmon and non-muscle myosin heavy chain-2; phenotypi

59 , suggesting that the effect was specific to caldesmon and not other thin-filament-associated protein

60 is to study the kinetics of binding of both caldesmon and S1 to actin.

61 This colocalization of caldesmon and Shc correlates with actin stress fiber dis

62 Only whole caldesmon and the carboxyl-terminal domain of caldesmon

63 mains of two known F-actin binding proteins: caldesmon and the villin headpieces (CI, CII, VI, VII).

64 -cyclin expression modulates the activity of caldesmon and through this the microfilament functions i

65 he inhibition of fascin-actin interaction by caldesmon and TM becomes Ca2+ dependent because Ca2+/cal

66 These results suggest important roles for caldesmon and TM in the regulation of the function of hu

67 we have examined the effects of culture cell caldesmon and tropomyosin (TM) on actin binding activity

68 actin monomers that are fully saturated with caldesmon and tropomyosin.

69 basic C-terminal half and correspond to the caldesmon and villin headpiece homologous regions.

70 and CD140b), and smooth muscle (alpha-actin, caldesmon, and calponin) markers.

71 ing proteins, including myosin, tropomyosin, caldesmon, and calponin.

72 and suppressed the phosphorylation of MAPKs, caldesmon, and heat shock protein 27 in the spastic cere

73 The tyrosine phosphorylation of caldesmon, and its association with the Shc-Grb2-Sos sig

74 sion of smooth muscle-alpha actin, calponin, caldesmon, and myosin heavy chain.

75 rylated forms of p21-activated kinase (Pak), caldesmon, and myosin light chain kinase.

76 esents a novel regulatory mechanism by which caldesmon, and potentially other actin-binding proteins,

77 iation markers (alpha-smooth muscle actin, h-caldesmon, and smooth muscle myosin heavy chain), wherea

78 nge of caldesmon concentrations, the type of caldesmon, and the method of data analysis used.

79 were fitted to the atomic model of F-actin, caldesmon appeared to cover potentially weak sites of my

80 The effects of caldesmon are blocked by the ionophore A23187, thapsigar

81 petitive binding model, in which both S1 and caldesmon are competing for the same binding sites on ac

82 cdc2 and caldesmon are shown here to localize in membrane ruffles

83 correlated with an increase in the extent of caldesmon attachment as S1-ATP dissociated.

84 on the actin- and myosin-binding regions of caldesmon, because a truncated variant lacking both of t

85 Additional parts of caldesmon bind less tightly to actin, causing caldesmon

86 us knowledge that COOH-terminal fragments of caldesmon bind to actin whereas NH2-terminal fragments d

87 In all cases caldesmon binding could be simulated with a model having

88 in with S1 reduced the amplitude (extent) of caldesmon binding in proportion to the fraction of actin

89 e number of actin monomers that constitute a caldesmon binding site.

90 ear if the fluorescence change resulted from caldesmon binding, the movement of tropomyosin over acti

91 Smooth muscle caldesmon binds actin and inhibits actomyosin ATPase act

92 A simple interpretation of the data is that caldesmon binds tightly to 2-3 actin monomers.

93 esults suggest that the carboxyl-terminus of caldesmon binds tightly to tropomyosin and that other re

94 Since the NH2 domain of caldesmon binds to the neck region of myosin, a dissocia

95 When caldesmon bound to actin during the polymerization of G-

96 ata from the x-ray studies showed that whole caldesmon bound to tropomyosin in several places, with t

97 not due to a conformational change in actin-caldesmon but to the displacement of caldesmon.

98 anization involves an enhanced expression of caldesmon, but not vinculin, alpha-actinin, or gelsolin.

99 Furthermore, as phosphorylation of caldesmon by cdc2 kinase inhibits actin binding of calde

100 Phosphorylation of caldesmon by extracellular signal-regulated kinase (ERK)

101 nd its properties resemble actin-tropomyosin-caldesmon-Ca2+ x calmodulin.

102 9 and W692) in chicken gizzard smooth muscle caldesmon (CaD) are located within the calmodulin (CaM)

103 Smooth muscle caldesmon (CaD) binds F-actin and inhibits actomyosin AT

104 from the smooth muscle thin filament protein caldesmon (CaD) by using small-angle X-ray and neutron s

105 Smooth muscle caldesmon (CaD) exhibits apparent heat stability.

106 It is well-known that caldesmon (CaD) is a substrate for casein kinase II (CKI

107 Caldesmon (CaD) is an important actin modulator that ass

108 598-756 of the chicken gizzard smooth muscle caldesmon (CaD) molecule.

109 The actin-binding protein caldesmon (CaD) reversibly inhibits smooth muscle contra

110 The ability of chicken gizzard smooth muscle caldesmon (CaD) to inhibit actomyosin ATPase activity is

111 ng of the N-terminal region of smooth muscle caldesmon (CaD) to myosin and its C-terminal region to a

112 ion mutants of chicken gizzard smooth muscle caldesmon (CaD) were made using a polymerase chain react

113 cles, but no change in the protein levels of caldesmon (CaD), actin, desmin or extracellular regulate

114 s results in the tyrosine phosphorylation of caldesmon (CaD), an actin- and calmodulin-binding protei

115 ough significant reduction in the content of caldesmon (CaD), calponin (CaP), and the 20-kDa regulato

116 aldesmon and the carboxyl-terminal domain of caldesmon (CaD-4, chicken gizzard residues 597-756) boun

117 modulin on the 22 kDa C-terminal fragment of caldesmon (CaD22).

118 of the actin- and calmodulin-binding protein caldesmon (CALD1) as a novel K-cyclin.CDK substrate, whi

119 e cell (SMC) markers, such as myosin, actin, caldesmon, calponin, and LPP, were down-regulated in emb

120 Caldesmon (Cd) and calponin (Cp) are two actin/calmoduli

121 e levels of phosphorylated LC(20), calponin, caldesmon, cofilin, and HSP27, as well as G-actin conten

122 g actin stress fibers in normal fibroblasts, caldesmon colocalizes with Shc in plasma membrane blebs

123 due to variations in the assay, the range of caldesmon concentrations, the type of caldesmon, and the

124 with a C-terminal fragment, hH32K, of human caldesmon containing the principal actin-binding domains

125 ssbridge cycling; strips containing normal h-caldesmon content did not redevelop force on release.

126 Caldesmon content was decreased by 78% after 7 days in c

127 e conclude that three regions in domain 4 of caldesmon contribute to tropomyosin-dependent inhibition

128 nphosphorylated, but not ERK-phosphorylated, caldesmon could stabilize actin filaments and resist F-a

129 d by the inhibition of fascin-actin binding, caldesmon coupled with TM also inhibits actin bundling a

130 tly decreased the accessibility of probes at caldesmon Cys-580 to the quencher, whereas for probes at

131 energy transfer from donor labels on either caldesmon cysteine to acceptor labels on Cys-374 of acti

132 We observed that caldesmon decreased the rate of binding of S1 to actin i

133 Unstimulated h-caldesmon-deficient smooth muscle tissues stretched and

134 In contrast, h-caldesmon-deficient tissues produced 62% less KCl-induce

135 Caldesmon density was clearly delineated in reconstructi

136 Because mutant caldesmon did not inhibit cyclin B/cdc2 kinase activity,

137 On the other hand, caldesmon does not appear to interact with the Cys-36 re

138 The interaction of caldesmon domains with tropomyosin has been studied usin

139 Because this caldesmon effect is shown to be independent of nucleotid

140 We found that microinjection of mutant caldesmon effectively blocked early cell division of Xen

141 inhibition of the binding between actin and caldesmon either by Ca(2+)/calmodulin or by phosphorylat

142 The 32-nucleotide caldesmon enhancer caused effective usage of the exon-in

143 In this study, we have compared the caldesmon enhancer with another purine-rich enhancer fro

144 FPA cells and surrounding fibroblasts modify caldesmon expression and polymerization in fibroblasts,

145 246-295, containing sequences homologous to caldesmon F-actin binding site I and II, respectively (C

146 Substituting smooth muscle caldesmon for skeletal muscle troponin produced a simila

147 A caldesmon fragment that encompasses residues 1-240 (N240

148 S1 binding resulted in rapid dissociation of caldesmon from actin or actin-tropomyosin.

149 ng mitosis, resulting in the dissociation of caldesmon from microfilaments.

150 more strongly and was capable of displacing caldesmon from myosin.

151 results and have led to different models of caldesmon function.

152 ntly described purine-rich enhancer from the caldesmon gene has an additional activity by which it di

153 enching studies showed that actin binding to caldesmon greatly decreased the accessibility of probes

154 We have found that caldesmon greatly retards Arp2/3-induced actin polymeriz

155 zed the expression of smooth muscle-specific caldesmon (h-CaD) and non-muscle (l-CaD) by Western blot

156 ar mass isoform of the actin-binding protein caldesmon (h-CaD) at two sites (Ser(759) and Ser(789)) d

157 amino acids to reach the C-terminus of human caldesmon (H2+26), inhibition is more potent.

158 the sequence near the N-terminal extreme of caldesmon harbors a major myosin-binding site of caldesm

159 H-caldesmon-immunopositive VSMCs were observed surrounding

160 inical samples showed that the expression of caldesmon in stromal cells and the expression of osteopo

161 These results indicate a role for nonmuscle caldesmon in the physiological regulation of actomyosin

162 significance of tethering actin to myosin by caldesmon in the regulation of smooth muscle contraction

163 Phosphorylation of caldesmon in vivo may reverse inhibitory influences of c

164 esmon harbors a major myosin-binding site of caldesmon, in which both the nonpolar residues and clust

165 It is known that the actin-binding protein caldesmon inhibits actomyosin ATPase activity and might

166 Caldesmon inhibits the activation of myosin ATPase activ

167 Kinetic analyses have revealed that caldesmon inhibits the nucleation process, whereas it do

168 scence studies provide evidence to show that caldesmon interacts with and alters the position of trop

169 Caldesmon interacts with the Cys-190 region in the COOH-

170 Expression of caldesmon interferes with Rho A-V14-mediated formation o

171 Smooth muscle caldesmon is a single polypeptide chain with its NH2- an

172 Caldesmon is a thin-filament-associated protein believed

173 Caldesmon is an actin- and myosin-binding protein found

174 Caldesmon is an actin-binding protein that regulates act

175 not, indicate that, while the COOH domain of caldesmon is bound to actin, the NH2 domain is largely d

176 The activity of caldesmon is controlled by phosphorylation and by bindin

177 Caldesmon is found to inhibit binding of Arp2/3 to F-act

178 Caldesmon is known to inhibit the ATPase activity of act

179 at the cooperativity observed in the case of caldesmon is not due to a conformational change in actin

180 Caldesmon is phosphorylated by cdc2 kinase during mitosi

181 Because caldesmon is present in membrane ruffles, as well as in

182 The binding between acidic calponin and caldesmon is strengthened to 1.8 x 10(7) M-1 in the pres

183 When the concentration of either S1 or caldesmon is varied, the amount of the other component b

184 Although a nonmuscle isoform of caldesmon is widely expressed, its functional role has n

185 Endogenous caldesmon kinase activities were also identified by the

186 tion of the actin binding proteins Hsp27 and caldesmon, known substrates for the Ser/Thr kinase MAPKA

187 smooth muscle alpha-actin levels, whereas h-caldesmon levels are increased in the double knockout bl

188 in, our results suggest a mechanism by which caldesmon maintains newly polymerized actin in a distinc

189 Our results suggest that caldesmon may be a key protein that modulates membrane r

190 tly to tropomyosin and that other regions of caldesmon may interact with tropomyosin tightly only whe

191 odel whereby tethering of actin to myosin by caldesmon may play a role in regulating vascular tone by

192 better substrate for PKCalpha than calponin, caldesmon, MLC and myosin.

193 hough S1 did apparently bind to gaps between caldesmon molecules.

194 a, and examined effects of expression of the caldesmon mutant on M-phase progression.

195 nificance of phosphorylation, we generated a caldesmon mutant replacing all seven cdc2 phosphorylatio

196 A, clathrin, alpha-actinin, vimentin, actin, caldesmon, myosin IC, and annexin A2 as major proteins a

197 of the molecule, but the exact nature of the caldesmon-myosin interaction has not been well character

198 s confer the specificity and affinity of the caldesmon-myosin interaction.

199 nge that moves the C-terminal end segment of caldesmon near the phosphorylation site but not the upst

200 e phosphorylation-dependent contact sites of caldesmon on actin by low dose electron microscopy and t

201 ins to antagonize the inhibitory function of caldesmon on actomyosin contraction.

202 dc2 kinase reverses the inhibitory effect of caldesmon on Arp2/3-induced actin polymerization.

203 n, can simulate quantitatively the effect of caldesmon on both the equilibrium and the kinetics of S1

204 We studied the effects of nonmuscle caldesmon on cellular contractility, actin cytoskeletal

205 in vivo may reverse inhibitory influences of caldesmon on cross-bridge cycling.

206 age reconstruction to reveal the location of caldesmon on isolated smooth muscle thin filaments.

207 MAP kinase reversed the inhibitory effect of caldesmon on sliding velocity.

208 This suggests that the inhibitory action of caldesmon on the actin-activated ATPase activity of myos

209 The effect of caldesmon on the binding and ATPase activity of S1 was m

210 inding sequences in the N-terminal region of caldesmon, on force directly recorded from single permea

211 Wild-type caldesmon, on the other hand, was much less potent in pr

212 s present (H2, H2+12), the actin-tropomyosin-caldesmon peptide complex is not inhibitory, and its pro

213 uffling and that this may involve changes in caldesmon phosphorylation and/or intracellular calcium c

214 Both ERK1/2 activity and nonmuscle l-caldesmon phosphorylation are blocked by h3/acidic calpo

215 erations in microfilament assembly caused by caldesmon phosphorylation are important for M-phase prog

216 To determine the effects of caldesmon phosphorylation by MAP kinase on the cross-bri

217 Stimulation with acetylcholine increased caldesmon phosphorylation significantly from a basal lev

218 migration by regulation of ERK1/2-mediated l-caldesmon phosphorylation.

219 d activation of FAK/Src and ERK pathways and caldesmon phosphorylation.

220 mon by cdc2 kinase inhibits actin binding of caldesmon, phosphorylation can also control actin bindin

221 These findings were the same for caldesmon prepared with or without heat treatment and wi

222 Transient transfection of nonmuscle caldesmon prevents myosin II-dependent cell contractilit

223 and constitutively phosphorylated states of caldesmon, respectively.

224 of smooth muscle calponin to Cys-580-labeled caldesmon resulted in an 18% drop in fluorescence intens

225 in, a dissociated NH2 domain may account for caldesmon's ability to link myosin and actin filaments.

226 may contribute to the overall regulation of caldesmon's activity.

227 m Met(1) to Tyr(27) of the human and chicken caldesmon sequence, respectively, plus an added cysteine

228 l synthetic peptides based on the N-terminal caldesmon sequence.

229 a-SM actin, SM myosin heavy chain, calponin, caldesmon, SM alpha-22), and the ability to contract and

230 cell-specific alpha actin (ASMA), calponin, caldesmon, SM22, myosin heavy chain (MHC), and smootheli

231 tone by positioning the C-terminal domain of caldesmon so that it is capable of blocking the actomyos

232 es, increasing alpha-smooth muscle actin and caldesmon staining and the expression of myocardin.

233 on without the need to assume multiple actin-caldesmon structures and produces a decreased rate of S1

234 trong, specific binding between calponin and caldesmon suggests that this interaction occurs within s

235 For Cys-153-labeled caldesmon, there was no change in fluorescence upon addi

236 aldesmon bind less tightly to actin, causing caldesmon to cover approximately 7 actin monomers.

237 ntained bound S1, but the rate of binding of caldesmon to free sites was not greatly altered.

238 zyxin cooperates with Ena/VASP proteins and caldesmon to influence integrin-dependent cell motility

239 The ability of caldesmon to limit the myosin-induced movement of tropom

240 Weaker association of other regions of caldesmon to tropomyosin residues 180-210 and 5-50 was a

241 However, caldesmon together with TM completely inhibits actin bin

242 caldesmon alone or TM alone shows no effect, caldesmon together with TM completely inhibits actin bun

243 therefore inhibition of actomyosin ATPase by caldesmon-tropomyosin and by troponin-tropomyosin cannot

244 Although caldesmon was a major wound-associated protein in calpai

245 Phosphorylation of caldesmon was assayed in canine colonic circular smooth

246 At higher head concentration caldesmon was dissociated from actin, consistent with th

247 When mutant caldesmon was introduced into CHO cells either by protei

248 Caldesmon was isolated by two-dimensional non-equilibriu

249 Caldesmon was labeled at either Cys-153 in the NH2 domai

250 Caldesmon was labeled at either Cys-153 in the NH2-termi

251 In contrast, actin-bound caldesmon was not moved by myosin heads at low head/acti

252 The primary myosin-binding site of caldesmon was thought to be in the N-terminal region of

253 Two new genes, EB-1 and EB-2, as well as Caldesmon were transcriptionally activated in each of se

254 ed with cytoskeleton organization, including caldesmon, were differentially expressed between fibrobl

255 ity for Ca2+ is increased in the presence of caldesmon, which could be a potential target molecule.

256 Interestingly, caldesmon, which inhibits tropomyosin's potentiation of

257 at non-muscle acidic calponin interacts with caldesmon with a much reduced association constant of 3.

258 Phosphorylation of caldesmon with sea star ERK1 MAP kinase reversed the inh

259 esented to show the possible interactions of caldesmon with tropomyosin.

260 olecules of S1 may bind to actin-tropomyosin-caldesmon without having the normal actin activation of

261 cooperativity for the binding of S1 to actin-caldesmon without the need to assume multiple actin-cald

262 The location of caldesmon would allow it to compete with a number of cel