ライフサイエンスコーパス: proenzyme

1 yme did not accelerate the processing of the proenzyme.

2 ive intramolecular activation pathway of the proenzyme.

3 h increased stability of the secreted 72-kDa proenzyme.

4 r protein, consistent with misfolding of the proenzyme.

5 gest an explanation for the stability of the proenzyme.

6 translated as part of an unusual polyprotein proenzyme.

7 0 and p18 as processed subunits of the CPP32 proenzyme.

8 though it reduced the positive charge of the proenzyme.

9 rms as well as a small fraction of insoluble proenzyme.

10 ch are dependent on the concentration of the proenzyme.

11 nal antiserum raised against the recombinant proenzyme.

12 domain promotes folding and secretion of the proenzyme.

13 an when it was added after activation of the proenzyme.

14 ays a critical role in the activation of the proenzyme.

15 al known virulence factors and secreted as a proenzyme.

16 istinguish the active two-chain uPA from its proenzyme.

17 on of sorting of newly synthesized lysosomal proenzymes.

18 res proteolytic processing of their inactive proenzymes.

19 proteinases (MMPs) are synthesized as latent proenzymes.

20 important for the maturation of several ADAM proenzymes.

21 of caspase-3 and poly(ADP-ribose) polymerase proenzymes.

22 rified MMP-2 and MMP-9 to show activation of proenzymes.

23 BMP-1 and mTld predominantly as unprocessed proenzymes.

24 Mch4 and Mch5, are derived from single chain proenzymes.

25 he autocatalytic activation of these mutated proenzymes.

26 d more active than procaspase-3, making this proenzyme a remarkably inactive zymogen.

27 e characteristic stimulation of the cationic proenzyme, acidic pH inhibited autoactivation of anionic

28 ly, we found that upon binding, the purified proenzyme acquired activity against both the fluorogenic

29 tivators to explore fundamental processes of proenzyme activation and their fate-determining roles in

30 ese studies demonstrate a novel approach for proenzyme activation through binding to fibrils, which m

31 strated that RHBDL2 activity is regulated by proenzyme activation, revealed a role for the conserved

32 these studies presage the discovery of other proenzyme activators to explore fundamental processes of

33 gest general strategies for the discovery of proenzyme activators.

34 ealed a high degree of similarity within the proenzyme active site, reflecting shared chemical constr

35 The molecular weight of the proenzyme, active enzyme, and enzyme fragments was deter

36 Cathepsin K is synthesized as an inactive proenzyme and activated under conditions of low pH.

37 a strong physical association between PkPSD proenzyme and anionic lipids.

38 ion of 17- and 12-kDa fragments of caspase-3 proenzyme and by cleavage of poly(ADP-ribose) polymerase

39 PgCHT1 in that the P. falciparum gene lacks proenzyme and chitin-binding domains.

40 oenzyme processed much faster than the human proenzyme and did not require putrescine for an optimal

41 as well as the ability to activate the MMP-2 proenzyme and directionally remodel a three-dimensional

42 Carboxypeptidase-U circulates as an inactive proenzyme and is activated by thrombin in a process that

43 Pro-lysyl oxidase is secreted as a 50-kDa proenzyme and is then cleaved to a 30-kDa mature enzyme

44 ichia coli leads to the formation of soluble proenzyme and mature enzyme forms as well as a small fra

45 s using antibodies capable of detecting both proenzyme and processed enzyme forms or the intact or cl

46 ctivity of caspase-12 is confined to its own proenzyme and that autocleavage within the caspase-1 com

47 , caspase-3 is found as a cytosolic inactive proenzyme and that caspase-3 activation is largely confi

48 Here, we show that RHBDL2 is produced as a proenzyme and that the processing of RHBDL2 is required

49 oblot analyses confirmed the presence of the proenzyme and the catalytically active form of MMP-9.

50 en the activation and the uptake rate of the proenzyme and the enzyme of MT1-MMP.

51 tion of the specific interaction between the proenzyme and the lipids can provide a novel mechanism t

52 8A mutant and have constructed models of the proenzyme and the oxyoxazolidine intermediate.

53 Pro-LOX is secreted as a 50 kDa proenzyme and then undergoes biosynthetic proteolytic pr

54 ss of apoptosis, are synthesized as inactive proenzymes and are activated in a proteolytic cascade af

55 cysteine protease family are synthesized as proenzymes and require proteolytic processing to produce

56 We investigated the activation of pancreatic proenzymes and signs of peripancreatic inflammation in p

57 irectly by processing other proteins such as proenzymes and/or other proteins that have an essential

58 n conformation directs proper folding of the proenzyme, and suggested that the cathepsin K active sit

59 at was immunoreactive with the RgpB-specific proenzyme antibodies.

60 lypeptide substrate, including other caspase proenzymes, apoptotic substrates, cytokine precursors, o

61 Thus, our study proposes a phototherapeutic-proenzyme approach toward complete-remission cancer ther

62 butanol on the processing of mutant AdoMetDC proenzymes are consistent with a model in which a single

63 e observed that in the absence of PrsA2, the proenzymes are secreted at physiological pH and do not m

64 ibed, all of which are initially produced as proenzymes, are activated by endoproteases, and remove e

65 tissue inhibitor of metalloproteinases-free proenzyme as a substrate for the activator, it is possib

66 s were dependent on the concentration of the proenzyme as well as active collagenase-3.

67 rocathepsin L also induced misfolding of the proenzyme, as indicated by addition of the second oligos

68 or changes of the secondary structure of the proenzyme, as revealed by CD spectroscopy.

69 sharp contrast to observations with the rat proenzyme, at pH 8.0, 37 degrees C, autoactivation kinet

70 Its proenzyme autoactivates under acidic conditions in vitro

71 mutant enzyme and demonstrated that the PSD proenzyme binds strongly to PS and PG but not to phospha

72 icamycin reduced the molecular mass of TPP I proenzyme by approximately 10 kDa, which indicates that

73 Activation of the proenzyme by either 4-aminophenylmercuric acetate or chy

74 (MMP-9, gelatinase B) was produced from the proenzyme by limited digestion with trypsin.

75 ecause EDTA prevents activation of exogenous proenzyme by membrane fractions.

76 units, which are derived from the pre-cursor proenzyme by processing at Asp-227, Asp-233, Asp-391, an

77 Interaction with the proenzyme C3bB was investigated by flowing factor B acro

78 expressed human granzyme A in bacteria as a proenzyme capable of in vitro activation by enterokinase

79 necessary for normal folding of the nascent proenzyme chain.

80 l serine protease inhibitor, PMSF, prevented proenzyme cleavage and permitted its purification free o

81 The mechanism of PSD proenzyme cleavage has long been unclear.

82 ol switch for the observed pH sensitivity of proenzyme cleavage in (trypanosomal) CathL-like protease

83 s using ionophore A23187 greatly accelerated proenzyme cleavage, suggesting that a serine protease pr

84 roximately 92-kD, Ca2+ - and Zn2+ -dependent proenzyme cleaved over time to smaller, active forms.

85 o steps: 1) zymogen autoactivation, when one proenzyme cleaves another proenzyme molecule of the same

86 essing ECs secreted greater amounts of MMP-1 proenzyme compared with control ECs, and readily convert

87 the protein is essential for maintaining the proenzyme conformation needed for autocatalytic processi

88 sembles activation sites in effector caspase proenzymes, consistent with a role for these enzymes as

89 of proteins resulting from the refolding of proenzyme constructs.

90 PB1 are secreted by the pancreas as inactive proenzymes containing a 94-96-amino acid-long propeptide

91 The truncated proenzyme could be processed by aminophenylmercuric acet

92 redetermined the structure of the wild-type, proenzyme CT from two crystal forms, both of which exhib

93 ext-generation sequencing-based approach for proenzyme design.

94 s in either the potato or the human AdoMetDC proenzyme did not prevent processing but caused a signif

95 o-MMP-9 forms a complex with alpha2(IV), the proenzyme does not bind to triple-helical collagen IV.

96 imary amino acid sequence include a putative proenzyme domain delineated by a consensus autocatalytic

97 f a highly conserved cysteine residue in the proenzyme domain, the so-called "cysteine switch," which

98 D binding site of the X-ray structure of the proenzyme DT-NAD complex.

99 ng INS cells, a substantial fraction of both proenzymes exhibit regulated exocytosis.

100 A selected disulfide-containing proenzyme exhibits significantly lower activity relative

101 g experiments that demonstrated that the new proenzyme failed to process to the expected point, the n

102 60 may be isolated as a cross-link-deficient proenzyme following anaerobic overexpression in E. coli.

103 ent media of recombinant cells as the stable proenzyme form ([Val217]phK2).

104 eas the peripheral cornea contained both the proenzyme form and the active form of gelatinase A.

105 a region within the primary sequence of the proenzyme form of cathepsin L which affects its subcellu

106 The proenzyme form of DPAP1 was found to accumulate in the p

107 icated that the central cornea contained the proenzyme form of gelatinase A, whereas the peripheral c

108 ved from dog mastocytomas secrete the 92-kDa proenzyme form of gelatinase B.

109 We expressed the proenzyme form of GzmB as well and determined that pro-G

110 ealed that levels of the full-length, 85 kDa proenzyme form of MMP-8 increased significantly within 8

111 active form of MMP-9 (actMMP-9), but not the proenzyme form of MMP-9 (proMMP-9), developed BP.

112 ve solved the X-ray crystal structure of the proenzyme form of the catalytic domain of plasminogen, w

113 hat plays a requisite role in processing the proenzyme form of the CTL granule serine proteases (gran

114 Activation of the proenzyme form of the malarial protease PfSUB-1 involves

115 d in cultured neurons and brain lysates in a proenzyme form that is activated by furin and degraded b

116 The cell expresses MMP2 in its proenzyme form, pro-MMP2, as well as MT1-MMP and TIMP2.

117 ind to the CaM column and was present in the proenzyme form.

118 Secreted proenzyme formed non-native, interchain disulfide bridge

119 ysis revealed constitutive expression of the proenzyme forms of caspase-1, -3, and -9 in the human pr

120 cognise the MMP-9 proenzyme or the active or proenzyme forms of matrix metalloproteinase-2 (MMP-2, ge

121 ) mutants have been identified which secrete proenzyme forms of soluble vacuolar hydrolases to the ce

122 In addition, mature and proenzyme forms of the proteases cathepsin B and catheps

123 thods are included for the activation of the proenzyme forms of these MMPs and the assay can also be

124 se conversion of caspases from their dormant proenzyme forms to active enzymes has a critical role in

125 stromelysin, which remained predominantly in proenzyme forms, as determined by Western analysis of cu

126 ovary, eggs, and embryos were present as the proenzyme forms, suggesting that the functions of these

127 I) exists in circulation as heterotetrameric proenzyme FXIII-A2B2 Effectively all FXIII-A2B2 circulat

128 talytic self-processing of the AdoMetDC/SpeD proenzyme generates a pyruvoyl cofactor from an internal

129 an increase in the proportion of the anionic proenzyme had no significant effect on the levels of try

130 caspase-3, we demonstrate that the caspase-3 proenzyme has a mitochondrial and cytosolic distribution

131 have found that TGF-beta1 induces the MMP-9 proenzyme; however, this induction does not result from

132 lls as well as maturation of the endocytosed proenzyme in CLN2 lymphoblasts, fibroblasts, and N2a cel

133 We report the expression of the prostasin proenzyme in Escherichia coli as insoluble inclusion bod

134 -3 dramatically stimulates maturation of the proenzyme in vitro.

135 to an active form or remains as unprocessed proenzyme, in a cell type-dependent manner.

136 ediate autoproteolytic maturation of its own proenzyme, in both cis and trans, it was not able to cle

137 anchored metalloproteases are synthesized as proenzymes, in which the latency is maintained by their

138 not contribute to the activation rate of the proenzyme initiated by collagenase-3 and our results ind

139 (PvlArgDC) formed by the self-cleavage of a proenzyme into a 5-kDa subunit and a 12-kDa subunit that

140 A proteolytic processing then transforms the proenzyme into a catalytically active form.

141 Processing of a malarial PSD proenzyme into its active alpha and beta subunits is by

142 apopain, as was indicated by cleavage of the proenzyme into its proteolytically active fragments.

143 e by activation and conversion of the latent proenzyme into the active enzyme, and also via inhibitio

144 hyladenine, hampered the conversion of TPP I proenzyme into the mature form, suggesting that this pro

145 ecretion of high levels of the precursor GAA proenzyme into the plasma of treated animals.

146 tly, systemic distribution and uptake of the proenzyme into the skeletal and cardiac muscles of the G

147 TPP I proenzyme is converted in lysosomes into a mature enzyme

148 Taspase1 proenzyme is intramolecularly proteolyzed generating an

149 The secreted lysyl oxidase proenzyme is processed to a propeptide (LOX-PP) and a fu

150 n this report, we demonstrate that the CPP32 proenzyme is proteolytically processed and activated in

151 In vitro, the chMMP-13 proenzyme is rapidly and efficiently activated through t

152 to normal levels, demonstrating that the UCE proenzyme is stable in this cell type.

153 MT1-MMP exists in various forms: a 63-kDa proenzyme is synthesized as primary translation product,

154 mes to be efficient activators, whereas MASP proenzymes lacked such activity.

155 The propeptide region of the lysyl oxidase proenzyme (LOX-PP) has been shown to inhibit Ras signali

156 mbers of MMP family, MMP-12 is produced as a proenzyme, mainly by macrophages, and undergoes proteoly

157 Moreover, both activated and proenzyme MASP-1 can effectively cleave proenzyme MASP-2

158 Proenzyme MASP-1 R448Q readily cleaves synthetic substra

159 The structure of the catalytic region of proenzyme MASP-1 R448Q was solved at 2.5 A.

160 tic fragments, we demonstrated that a stable proenzyme MASP-1 variant (R448Q) cleaved the inactive, c

161 and proenzyme MASP-1 can effectively cleave proenzyme MASP-2.

162 ine proteinases plasmin and thrombin convert proenzyme matrix metalloproteinases (MMPs) into catalyti

163 These results suggest a picture for proenzyme maturation in the vacuole and will inform the

164 Proenzyme maturation is a general mechanism to control t

165 te is part of a general mechanism underlying proenzyme maturation of ADAMs that is independent of pro

166 suggesting that an oncogenic switch for this proenzyme may offer a therapeutic target not only in adv

167 tivation, when one proenzyme cleaves another proenzyme molecule of the same protease, and 2) autocata

168 Thus, the uptake rate of the latent MT1-MMP proenzyme noticeably exceeded that of the active enzyme.

169 t systems, MPR-mediated sorting of lysosomal proenzymes occurs to a variable extent within the trans-

170 The proenzyme of calpain 2 (m-calpain) is a heterodimeric ca

171 says demonstrated that Atox1, ATP7A, and the proenzyme of lysyl oxidase (LOX; copper-loaded via ATP7A

172 HK in the absence of prekallikrein (PK), the proenzyme of plasma kallikrein, on vascular endothelial

173 The proenzyme of Sf caspase-1 is 299 amino acids in length a

174 th muscle cells and prothrombin, the pivotal proenzyme of the blood coagulation system, is demonstrat

175 senic trioxide induced the expression of the proenzymes of caspase 2 and caspase 3 and activation of

176 enzymes, stromelysin-1 can also activate the proenzymes of other MMPs, making it an attractive target

177 a posttranslational modification of several proenzymes of the blood coagulation cascade, using eithe

178 cathepsin B was not related to secretion of proenzyme or secretion from mature lysosomes.

179 The antibodies do not recognise the MMP-9 proenzyme or the active or proenzyme forms of matrix met

180 lack of detectable processing of casp-9-CTD proenzyme or the induction of cell death following trans

181 ansiting and functionally mitogenic secreted proenzyme (pCatD) form of cathepsin D (mature CatD), a p

182 racellular serine protease that converts the proenzyme plasminogen into the active protease plasmin,

183 in an intramolecular reaction that cleaves a proenzyme precursor and converts a serine residue into p

184 s the LOX gene, which codes for the inactive proenzyme (Pro-Lox) from which, after extracellular secr

185 ynthesized and secreted as a 50-kDa inactive proenzyme (Pro-LOX), which is processed by proteolytic c

186 ng quantitatively the activation of the MMP2 proenzyme (pro-MMP2), the ectodomain shedding of MT1-MMP

187 TPP1 is synthesized as an inactive proenzyme (pro-TPP1) that is proteolytically processed i

188 Notably, we show that the proenzymes procaspase-3 and -9 are basally persulfidated

189 screen (HTS) that stimulates activation of a proenzyme, procaspase-3, to generate mature caspase-3.

190 The wild type potato AdoMetDC proenzyme processed much faster than the human proenzyme

191 ine space of unactivated eggs, apparently as proenzymes processed away from the original polyprotein.

192 d 70 of the parasite enzyme are critical for proenzyme processing and decarboxylase activity.

193 al mechanisms and/or after secretion through proenzyme processing and interactions with metalloprotei

194 rg at position 13 is a major determinant for proenzyme processing in the parasite enzyme.

195 In the human enzyme, both the proenzyme processing reaction and enzyme activity are st

196 involved in substrate binding, catalysis or proenzyme processing that were identified in the human a

197 The site of potato AdoMetDC proenzyme processing was found to be Ser73 in the conser

198 the putrescine stimulation of human AdoMetDC proenzyme processing was identified in the present studi

199 the putrescine activation of human AdoMetDC proenzyme processing.

200 rough ionic interactions is required for the proenzyme processing.

201 old increase in lysyl oxidase expression and proenzyme production.

202 catalytic requirements for neutrophil MMP-9 proenzyme (proMMP-9) to induce angiogenesis were investi

203 e, whereas PC-PLC is secreted as an inactive proenzyme (proPC-PLC) whose activation is mediated in vi

204 rostatic ducts as an inactive 244-amino acid proenzyme (proPSA) that is activated by cleavage of seve

205 ant H243A S-adenosylmethionine decarboxylase proenzyme provides a useful model system to examine the

206 es, including self-cleaved forms, during the proenzyme purification process.

207 A single point mutation in the lysosomal proenzyme receptor-inhibiting sequence near the N termin

208 e to suppress k(cat)/K(M) by 250-fold in the proenzyme relative to wild-type barnase.

209 dentified polybasic amino acid motifs in the proenzyme responsible for binding to PS.

210 elevation activates intracellular digestive proenzymes resulting in necrosis and inflammation.

211 en the large and small subunits of the CPP32 proenzyme, resulting in removal of the prodomain via an

212 In addition, cleavage of the proenzyme results in the formation of a threonine-threon

213 tructure of the Thermatoga maritima AdoMetDC proenzyme reveals a dimeric protein fold that is remarka

214 Analysis of the latent proenzyme's interface between the shielding C-terminal d

215 stive enzymes in vertebrates, are pancreatic proenzymes secreted into the intestines.

216 The resultant N terminus of the cleaved proenzyme serves as a nucleophile in amide bond hydrolys

217 normal male Sprague-Dawley rats, much of the proenzyme sorting appears to occur earlier, significantl

218 the C-terminal prosequence suggests that the proenzyme state is dependent on the presence of a basic

219 The proenzyme structure reveals suboptimal catalytic triad g

220 A purified proenzyme that accumulated in the His-72 mutant was show

221 t RIP2 protein is synthesized as an inactive proenzyme that can be processed in the caterpillar gut.

222 mical assays revealed that the nuclease is a proenzyme that cleaves DNA only after activation by its

223 decarboxylase (AdoMetDC) is synthesized as a proenzyme that cleaves itself in a putrescine-stimulated

224 show that UCE is synthesized as an inactive proenzyme that is activated by the endoprotease furin, w

225 monstrated that EmpA is secreted as a 46-kDa proenzyme that is activated extracellularly by the remov

226 2 gene product is synthesized as an inactive proenzyme that is autocatalytically converted to an acti

227 ombin-activatable fibrinolysis inhibitor), a proenzyme that is proteolytically activated by thrombin

228 s secreted from fibrogenic cells as a 50-kDa proenzyme that is proteolytically processed to the matur

229 of the CED-3/ICE family, is synthesized as a proenzyme that is subsequently processed into an active

230 methionine decarboxylase is synthesized as a proenzyme that undergoes an autocatalytic cleavage react

231 This protein is translated as an inactive proenzyme that undergoes autoprocessing to become an act

232 mepsins are synthesized as integral membrane proenzymes that are activated by cleavage from the membr

233 yme (ICE), family members are synthesized as proenzymes that are proteolytically processed to form ac

234 Lysosomal proenzymes that fail to be sorted at both sites remain a

235 Caspases are normally present in the cell as proenzymes that require limited proteolysis for activati

236 In the structure of the MT1-MMP proenzyme, the R(89)-R-P-R-C(93) site, however, is inacc

237 first small molecules that directly activate proenzymes, the apoptotic procaspases-3 and -6.

238 d 63 residues that are derived from a common proenzyme; these proteins associate in an (alphabeta)(2)

239 ile (T282C) allowed determination of a 1.6-A proenzyme ThnT crystal structure, which revealed a level

240 smid increased the maturation of the soluble proenzyme three- to fourfold without influencing the con

241 is processed from a 75-kDa, Zn(2+)-activated proenzyme to a mature 65 kDa, Zn(2+)-independent L-SMase

242 sion (first detected after 6 h) of the CPP32 proenzyme to active caspase-3, a cysteine protease that

243 oportion of factor VII is converted from its proenzyme to active serine protease for several hours po

244 wth cones, and proteolytic conversion of the proenzyme to mature enzyme mainly occurred after the sec

245 sed proteolytic processing of the 45-kDa LOX proenzyme to the 30-kDa active form, with a correspondin

246 e to AEBSF participates in processing of the proenzyme to the mature, active form in vivo.

247 and switch effective autoactivation of TPP I proenzyme toward less acidic pH values (up to pH 6.0).

248 The pancreas secretes digestive proenzymes typically in their monomeric form.

249 formed in a concerted reaction when the PSD proenzyme undergoes an endoproteolytic cleavage into a l

250 When treated with peroxide, this proenzyme undergoes maturation to active enzyme with spe

251 Cathepsin K was expressed as a secreted proenzyme using baculovirus-infected Sf21 insect cells.

252 When (202)KR were mutated to AA, the proenzyme was also activated, suggesting that (197)RPRR

253 In vitro processing of WT PkPSD proenzyme was also inhibited by calcium, consistent with

254 Autoprocessing of TPP I proenzyme was carried out at a wide pH range, from appro

255 Western blotting demonstrated that the CPP32 proenzyme was expressed in granule neurons before induct

256 Also, the RgpB proenzyme was identified in this fraction by mass spectr

257 The 60-kDa proenzyme was kinetically competent to form the mature 4

258 Autolytic cleavage within the caspase-12 proenzyme was mapped to a single site at the large-small

259 In addition, the maturation of the proenzyme was not affected by the presence of glycerol.

260 uman protein and 25 residues from the potato proenzyme were compatible with processing.

261 tutive synthesis and activation of the MMP-2 proenzyme were modulated by stable transfections of tumo

262 Both Cwp84 and Cwp13 are produced as proenzymes which are processed by cleavage to produce ma

263 dine and spermine, is first synthesized as a proenzyme, which is cleaved posttranslationally to form

264 and differentiation and is synthesized as a proenzyme, which undergoes autocatalytic cleavage to gen

265 usceptible to rapid decay by DAF, unlike the proenzyme, which was unaffected.

266 caspases are initially expressed as inactive proenzymes, which undergo proteolytic cleavage to become

267 PC-PLC is made as an inactive proenzyme whose activation requires cleavage of an N-ter

268 PC-PLC is made as a proenzyme whose maturation is mediated by a metalloprote

269 Digestion of immunoprecipitated TPP I proenzyme with both N-glycosidase F and endoglycosidase

270 metalloproteinase present mostly as a 66-kD proenzyme with lower levels of a 62-kD active form.

271 Finally, the proenzyme with the active site mutated (S475L) was not p

272 cess that involves a trimer formation of the proenzyme with TIMP2 and MT1-MMP, is suppressed at high

273 ly not due to altered protein folding as the proenzyme within A23187-treated cells remained capable o

274 ost of CrMCA-II in the cell was present as a proenzyme (zymogen) attached to the plasma membrane (PM)