ライフサイエンスコーパス: antitrypsin

1 ation by alpha1-proteinase inhibitor (alpha1-antitrypsin).

2 prions, vasopressin receptor 2, and alpha-1-antitrypsin.

3 the dislocation of misfolded luminal alpha-1 antitrypsin.

4 his could be inhibited by addition of alpha1-antitrypsin.

5 and proteasomal degradation of mutant alpha1-antitrypsin.

6 ns stable at approximately 3.5 A in alpha(1)-antitrypsin.

7 protein, null Hong Kong variant of alpha(1)-antitrypsin.

8 and in beta-strand 1C compared with alpha(1)-antitrypsin.

9 hile no such movement is evident in alpha(1)-antitrypsin.

10 the pathological polymers formed by alpha(1)-antitrypsin.

11 on when compared to the wild-type M alpha(1)-antitrypsin.

12 ir effects on the shutter region of alpha(1)-antitrypsin.

13 ined several degradation products of alpha-1 antitrypsin.

14 ema caused by mutations in the serpin alpha1-antitrypsin.

15 ited by alpha-ACT but not by related alpha-1-antitrypsin.

16 nificant amounts of human albumin and alpha1-antitrypsin.

17 HD severity markers, calprotectin and alpha1-antitrypsin.

18 of polarity, and reduced secretion of alpha1-antitrypsin.

19 sease associated with the Z allele of alpha1-antitrypsin.

20 , transferrin, alpha-fetoprotein, and alpha1-antitrypsin.

21 reduced level or loss of function of alpha1-antitrypsin.

22 key anti-elastase within the lung: alpha(1)-antitrypsin.

23 s fragmentation in cells expressing Z-alpha1-antitrypsin.

24 romising the inhibitory activity of Z alpha1-antitrypsin.

25 of anti-inflammatory signalling by M alpha1-antitrypsin.

26 n-dependent degradation of misfolded alpha-1 antitrypsin.

27 required for ubiquitination of mutant alpha1-antitrypsin, a luminal ERAD substrate.

28 Alpha-1-antitrypsin (a1AT) deficiency is caused by homozygosity

29 on transplantation, human albumin and alpha1-antitrypsin (A1AT) in mouse sera secreted by encapsulate

30 ssion of the human protease inhibitor alpha1-antitrypsin (A1AT) in Nicotiana benthamiana.

31 alpha-1 Antitrypsin (A1AT) is an abundant circulating serpin wit

32 f this correlation and the effect of alpha-1-antitrypsin (A1AT) on the expression of the iron hormone

33 alpha1-Antitrypsin (A1AT) purified from human plasma upregulate

34 This study shows that human alpha1-antitrypsin (A1AT) upregulates expression and release of

35 alpha1-Antitrypsin (A1AT) was identified as a plasma protease i

36 I), apolipoprotein C-III (ApoC-III), alpha-1-antitrypsin (A1AT), and alpha-2-HS-glycoprotein (A2HSG);

37 ove function with supplementation of alpha-1 antitrypsin (A1AT).

38 ined by proper circulating levels of alpha-1 antitrypsin (A1AT).

39 ers of the serine protease inhibitor alpha-1-antitrypsin (A1AT).

40 a point mutation (Glu342Lys) in the alpha(1)-antitrypsin (A1AT, also known as SERPINA1) gene that is

41 Human alpha-1-antitrypsin (A1PI) is a plasma protein with the function

42 The rationale of alpha1-antitrypsin (AAT) augmentation therapy to treat progress

43 Mutations in alpha1-antitrypsin (AAT) can cause the protein to polymerise an

44 Because alpha-1-antitrypsin (AAT) decreases HIV replication in PBMCs and

45 Alpha-1-antitrypsin (AAT) deficiency (AATD) is a genetic disease

46 alpha-1 Antitrypsin (AAT) deficiency (AATD) is characterized by

47 Alpha-1 antitrypsin (AAT) deficiency (AATD) is characterized by

48 Alpha-1 antitrypsin (AAT) deficiency is a common single-gene dis

49 alpha(1)-Antitrypsin (AAT) deficiency is an underrecognized genet

50 alpha1 -Antitrypsin (AAT) deficiency is one of the most common g

51 Alpha-1 antitrypsin (AAT) deficiency is well-suited as a target

52 In this study we used alpha-1 antitrypsin (AAT) deficiency with the piZZ mutant phenot

53 Using iPSC lines from patients with alpha-1 antitrypsin (AAT) deficiency, for which there is current

54 treatment for the monogenic disorder alpha-1-antitrypsin (AAT) deficiency.

55 e that results from mutations in the alpha-1 antitrypsin (AAT) gene.

56 alpha-1 antitrypsin (AAT) has been shown to reduce inflammatory

57 tudied the effects of treatment with alpha 1-antitrypsin (AAT) in a syngeneic nonautoimmune islet gra

58 alpha1-Antitrypsin (AAT) is a potent protease inhibitor, defici

59 Alpha-1-antitrypsin (AAT) is synthesized and secreted mainly by

60 n inverse correlation between plasma alpha-1-antitrypsin (AAT) levels in human donors and the develop

61 ect of the serine protease inhibitor alpha-1 antitrypsin (AAT) on IL-32 levels and showed suppression

62 The serum protease inhibitor alpha1-antitrypsin (AAT) possesses antiinflammatory properties

63 on of the serine proteinase inhibitor alpha1-antitrypsin (AAT) prevents type 1 diabetes development i

64 soluble distribution of two misfolded alpha1-antitrypsin (AAT) variants responsible for AAT deficienc

65 on of the disease relevant inhibitor alpha-1-antitrypsin (AAT) Z-variant with catalytically inactive

66 We demonstrate that treatment with alpha1-antitrypsin (AAT), an agent that dampens inflammation, d

67 selected from the proteomic analysis, alpha1-antitrypsin (AAT), hemopexin (HX), and gelsolin (GSN), a

68 for concentrations of the biomarkers alpha-1-antitrypsin (AAT), myeloperoxidase, and neopterin.

69 d human islets, we demonstrated that alpha-1 antitrypsin (AAT; Prolastin-C), a serine protease inhibi

70 amily A member 1 (SERPINA1) encoding alpha-1 antitrypsin [AAT; p.V213A; P = 5.99E-9, odds ratio (OR)

71 in and, thus, may prove useful for assessing antitrypsin activity in clinical specimens.

72 The new method yields serum antitrypsin activity levels that correlate well with imm

73 Polymers of Z alpha(1)-antitrypsin aggregate within the liver leading to juveni

74 Deficiency of alpha(1) -antitrypsin (alpha(1) AT) may be a determinant of suscep

75 Homozygous (PIZZ) alpha-1-antitrypsin (alpha(1)-AT) deficiency is associated with

76 Alpha-1 antitrypsin (alpha(1)-AT) is a member of the serpin clas

77 mechanism of peptide modulation of alpha(1)-antitrypsin (alpha(1)-AT) polymerization and depolymeriz

78 imed to evaluate fecal calprotectin, alpha-1-antitrypsin (alpha(1)-AT), and elastase at the time of f

79 lding of the canonical serpin human alpha(1)-antitrypsin (alpha(1)-AT).

80 nd emphysema caused by mutations in alpha(1)-antitrypsin (alpha(1)AT), and thrombosis caused by mutat

81 tional dynamics of the serpin human alpha(1)-antitrypsin (alpha(1)AT).

82 Alpha-1 antitrypsin (alpha1-AT) deficiency is the most common ge

83 n serine protease inhibitor (serpin) alpha-1 antitrypsin (alpha1-AT) protects tissues from proteases

84 of three HNF-4alpha sensitive genes, alpha1-antitrypsin (alpha1-AT), transthyretin (TTR), and apolip

85 ecific to liver proteins: albumin and alpha1-antitrypsin (alpha1-AT).

86 alpha1-Antitrypsin (alpha1AT) deficiency (alpha1ATD) is a conse

87 Liver disease in alpha-1-antitrypsin (alpha1AT) deficiency is caused by a gain-of

88 In alpha(1)-antitrypsin (alpha1AT) deficiency, a polymerogenic mutan

89 Point mutants of alpha1 -antitrypsin (alpha1AT) form ordered polymers that are re

90 ol region (LCR) upstream of the human alpha1-antitrypsin (alpha1AT) gene that is required for gene ac

91 Inhibitory activity of alpha1-antitrypsin (alpha1AT) toward elastase showed negative c

92 Lys) in the serine protease inhibitor alpha1-antitrypsin (alpha1AT), which is found in more than 4% o

93 family: protein C inhibitor (PCI) and alpha1-antitrypsin (alpha1AT); however, both exhibit poor react

94 ion could be recovered by addition of alpha1-antitrypsin, an endogenous inhibitor of serine proteases

95 ere that monomers of plasma serpins alpha(1)-antitrypsin and antithrombin are stable on incubation wi

96 adation of two other ERAD substrates, alpha1-antitrypsin and deltaCD3.

97 ded, with significant accumulation of alpha1-antitrypsin and GRP78.

98 ations stabilise the native fold of alpha(1)-antitrypsin and increase secretion of monomeric protein

99 cretion and secretion of endogenous alpha(1)-antitrypsin and serum albumin from HepG2 cells.

100 ate well with immunological levels of alpha1-antitrypsin and, thus, may prove useful for assessing an

101 erine protease inhibitors [Serpina1a (alpha1-antitrypsin) and Elafin] was dysregulated in Fbln5(-/-)

102 pathy (calprotectin, myeloperoxidase, alpha1-antitrypsin) and the prevalence of bacterial but not vir

103 obin increased, whereas transferrin, alpha-1-antitrypsin, and apolipoprotein A-1 decreased.

104 f metalloproteinase 2, -3, and -4 and alpha1-antitrypsin, and fibrosis was associated with increased

105 genes such as SERPINA1, which encodes alpha1 antitrypsin, and FOXP4, an inhibitor of mucus production

106 R2, Bid), optimal IL-13 inhibition of alpha1-antitrypsin, and IL-13-induction of and activation of ca

107 es, the solubility of mutant forms of alpha1-antitrypsin, and interactions with newly synthesized gly

108 flammation (high C-reactive protein, alpha-1-antitrypsin, and serum amyloid A), immune response (high

109 nic antigen, retinol binding protein, alpha1-antitrypsin, and squamous cell carcinoma antigen-were co

110 d levels of carcinoembryonic antigen, alpha1-antitrypsin, and squamous cell carcinoma antigen.

111 of surfactant proteins A, B, and C, alpha-1-antitrypsin, and the cystic fibrosis transmembrane condu

112 odepleted of albumin, IgG, IgA, haploglobin, antitrypsin, and transferrin.

113 Serum levels of nine biomarkers (alpha1 antitrypsin, apolipoprotein CIII, brain-derived neurotro

114 The S- and Z-deficiency alleles of alpha1-antitrypsin are found in more than 20% of some white pop

115 ular serpins such as antithrombin and alpha1-antitrypsin are the quintessential regulators of proteol

116 tifying cathepsin C, cathepsin Z, and alpha1-antitrypsin as additional potential cargoes for LMAN1, n

117 e found, using alpha-1-acid glycoprotein and antitrypsin as model systems for surface glycans, that t

118 levels of inflammatory biomarkers and alpha1-antitrypsin at baseline.

119 Alpha-1-antitrypsin (AT) deficiency is the most common genetic c

120 In the classical form of alpha1-antitrypsin (AT) deficiency, a point mutation in AT alte

121 molecular basis of liver disease in alpha-1-antitrypsin (AT) deficiency.

122 Alpha(1)-antitrypsin (AT) is the most abundantly circulating huma

123 ithelial cells with purified plasma M alpha1-antitrypsin attenuates this inflammatory response, openi

124 m due to accumulation of the mutant Z alpha1-antitrypsin (ATZ) and is a key example of an disease mec

125 unoglobulin G, transferrin, fibrinogen and a-antitrypsin), both in buffer and when spiked into human

126 the intracellular polymerization of Z alpha1-antitrypsin by 60%.

127 d the intracellular accumulation of Z alpha1-antitrypsin by 70% in a cell model of disease.

128 on reduces concentrations in serum of alpha1 antitrypsin by retaining polymerised molecules within he

129 ers, followed by IL-2 receptor alpha, alpha1-antitrypsin, C-reactive protein, YKL-40, cellular fibron

130 d by alpha(1)-proteinase inhibitor (alpha(1)-antitrypsin), C1 inhibitor, and most efficiently by anti

131 Polymers of mutant alpha1-antitrypsin can also form within the alveoli and small a

132 globulin, zinc alpha-2 glycoprotein, alpha-1 antitrypsin, complement factor B, haptoglobin, transthyr

133 leukin-6, interleukin-8, and elastase-alpha1-antitrypsin complexes compared with presurgery levels (p

134 leukin-8, interleukin-6, and elastase-alpha1-antitrypsin complexes were elevated compared with contro

135 nterleukin-6, interleukin-8, elastase-alpha1-antitrypsin complexes, thrombin-antithrombin complexes,

136 Alpha-1-antitrypsin concentrations partially mediate the seasona

137 nt with the serine protease inhibitor alpha1-antitrypsin decreased serum levels of HS, leading to a r

138 Alpha1-antitrypsin defciency-related liver disease is therefore

139 Liver disease due to alpha-1-antitrypsin deficiency (A1ATD) is associated with hepati

140 Alpha-1 antitrypsin deficiency (AATD) is a rare genetic disease

141 of the local folding environment in alpha-1-antitrypsin deficiency (AATD), Niemann-Pick type C1 dise

142 believed to cause lung destruction in alpha1-antitrypsin deficiency (AATD).

143 monary disease (COPD) associated with alpha1-antitrypsin deficiency (AATD).

144 alpha1-Antitrypsin deficiency (ATD) is a common genetic disorde

145 In the classical form of alpha1-antitrypsin deficiency (ATD), aberrant intracellular acc

146 y in patients with the classical form alpha1-antitrypsin deficiency (ATD).

147 es in 13 countries if they had severe alpha1 antitrypsin deficiency (serum concentration <11 muM) wit

148 Severe alpha1-antitrypsin deficiency (typically PiZZ homozygosity) is

149 Organoids from alpha1-antitrypsin deficiency and Alagille syndrome patients mi

150 enetic and nongenetic modifiers in ZZ alpha1-antitrypsin deficiency and other disorders of protein mi

151 The conference was titled "Alpha-1-Antitrypsin Deficiency and Other Liver Diseases Caused b

152 d-stage liver disease associated with alpha1-antitrypsin deficiency and underscore the contribution o

153 disease, genetic hemochromatosis and alpha-1 antitrypsin deficiency as we continue to elucidate the m

154 Severe alpha1-antitrypsin deficiency caused by the Z variant (Glu342Ly

155 ce is comparable to the frequency of alpha-1 antitrypsin deficiency documented in this population.

156 ive measure of disease progression in alpha1 antitrypsin deficiency emphysema than spirometry is, so

157 emochromatosis, Wilson's disease, and alpha1-antitrypsin deficiency grow significantly.

158 tor (A1PI) augmentation treatment for alpha1 antitrypsin deficiency has not been substantiated by a r

159 a progression in patients with severe alpha1 antitrypsin deficiency in a randomised controlled trial

160 tic correction of a mutation causing alpha-1 antitrypsin deficiency in patient-derived hPSCs.

161 Alpha-1-antitrypsin deficiency is a genetic condition associated

162 Alpha1-antitrypsin deficiency is a genetic disease that can aff

163 Alpha1-antitrypsin deficiency is a genetic disorder that affect

164 million individuals worldwide, where alpha-1-antitrypsin deficiency is a major genetic cause of the d

165 Antitrypsin deficiency is a primary cause of juvenile li

166 moking interactions, but only severe alpha 1-antitrypsin deficiency is a proven genetic risk factor f

167 alpha1-Antitrypsin deficiency is an inherited condition that ca

168 alpha1-Antitrypsin deficiency is one of the most common heritab

169 Alpha-1 antitrypsin deficiency shows that rare coding variants o

170 levels of which are associated with alpha-1 antitrypsin deficiency which leads to liver disease.

171 The association of alpha1-antitrypsin deficiency with the development of emphysema

172 om mutations in the genes SERPINA1 (alpha(1)-antitrypsin deficiency), JAG1 (Alagille syndrome), ATP8B

173 , amyotrophic lateral sclerosis, and alpha-1 antitrypsin deficiency).

174 re LTx could be analysed (COPD, 360; alpha-1-antitrypsin deficiency, 127; interstitial lung disease,

175 In the classical form of alpha(1)-antitrypsin deficiency, a mutant protein accumulates in

176 ulated in livers from patients with alpha(1)-antitrypsin deficiency, and the degree of up-regulation

177 ndividuals in the United States have alpha-1 antitrypsin deficiency, and the most common cause of thi

178 Wilson disease hemochromatosis and alpha-one antitrypsin deficiency, and the pivotal findings in publ

179 ommon causes include hemochromatosis, alpha1-antitrypsin deficiency, autoimmune hepatitis, and Wilson

180 conditions studied in further detail (alpha1-antitrypsin deficiency, familial hypercholesterolemia, a

181 he polymerization of AT, leading to alpha(1)-antitrypsin deficiency, has been studied extensively in

182 In alpha-1 antitrypsin deficiency, hepatocytes accumulate defective

183 compared data of patients with COPD, alpha-1-antitrypsin deficiency, interstitial lung disease, or cy

184 In alpha1-antitrypsin deficiency, intrahepatocyte accumulation of

185 form of "ER stress" that occurs in alpha(1)-antitrypsin deficiency, presumably determined by the agg

186 Yet, aside from alpha-1 antitrypsin deficiency, the genetic determinants of emph

187 PINA1) gene that is responsible for alpha(1)-antitrypsin deficiency.

188 ucher disease, cystic fibrosis and ZZ alpha1-antitrypsin deficiency.

189 derlies emphysema in individuals with alpha1-antitrypsin deficiency.

190 inflammatory diseases associated with alpha1-antitrypsin deficiency.

191 the lung, namely cystic fibrosis and alpha-1-antitrypsin deficiency.

192 underlies misfolding diseases such as alpha1-antitrypsin deficiency.

193 ls with emphysema secondary to severe alpha1 antitrypsin deficiency.

194 al of A1PI treatment in patients with alpha1 antitrypsin deficiency.

195 iseases such as cystic fibrosis, and Alpha-1 antitrypsin deficiency.

196 noncoding gene regions may result in alpha-1-antitrypsin deficiency.

197 ces of emphysema distribution in non-alpha-1 antitrypsin-deficient smokers.

198 The 2.2 A structure of Thr114Phe alpha(1)-antitrypsin demonstrates that the effects of the mutatio

199 he designed tetrapeptides is the most potent antitrypsin depolymerizer yet found.

200 polymers formed by Z and His334Asp alpha(1)-antitrypsin despite the mutations directing their effect

201 matosis and iron overload disorders, alpha-1 antitrypsin disease, and exciting new therapeutic option

202 reditary iron overload disorders, and alpha1-antitrypsin disease-are the focus of this review.

203 Mutant Z alpha1-antitrypsin (E342K) accumulates as polymers within the e

204 corresponding to residues 359-374 of alpha1-antitrypsin, enhances gene expression from DNA nanoparti

205 CD3delta and misfolded Z variant of alpha-1-antitrypsin, established substrates of gp78.

206 connected to the main ER network in Z-alpha1-antitrypsin-expressing cells.

207 cies in reporter assays and improves alpha-1-antitrypsin expression prediction in primary human tissu

208 his regulation ultimately determines alpha-1-antitrypsin expression.

209 ranscriptional regulatory program of alpha-1-antitrypsin expression.

210 Z and shutter domain mutants of alpha(1)-antitrypsin form polymers with a shared epitope and so a

211 s for emphysema, infusion of purified alpha1 antitrypsin from pooled human plasma represents a specif

212 ene expression AAV2/9-mediated human alpha-1-antitrypsin gene expression in serum was approximately 6

213 The alpha-1-antitrypsin gene, SERPINA1, expresses an exceptional num

214 The Z mutant of alpha1-antitrypsin (Glu342Lys) causes a domain swap and the for

215 ons such as emphysema caused by human alpha1 antitrypsin (hAAT) deficiency.

216 Human alpha1-antitrypsin (hAAT) is an antiinflammatory, immune-modula

217 hepatocytes were derived from human alpha(1)-antitrypsin (hAAT) transgenic mice of the FVB strain.

218 Third, a mutant allele of human alpha1-antitrypsin (hAAT) was linked to Fah and resulted in pro

219 monotherapy with clinical-grade human alpha1-antitrypsin (hAAT), the major serum serine-protease inhi

220 The Z mutant of alpha(1)-antitrypsin has a point mutation Glu342Lys in the hinge

221 ved, such as aggregation of misfolded alpha1-antitrypsin in the endoplasmic reticulum, deficient LDL

222 ulation of the misfolded Z variant of alpha1-antitrypsin in the hepatocyte endoplasmic reticulum (ER)

223 tations increase the secretion of Z alpha(1)-antitrypsin in the native conformation, but the double m

224 polymerisation of wild-type native alpha(1)-antitrypsin in vitro and increase secretion in a Xenopus

225 best described for the Z variant of alpha(1)-antitrypsin in which the proinflammatory properties of p

226 Genetic variants other than in alpha-1 antitrypsin increase the risk of COPD.

227 ed in SU5416-treated rats given human alpha1-antitrypsin intravenously.

228 alpha1-Antitrypsin is a serine protease inhibitor produced in t

229 alpha(1)-Antitrypsin is a serine protease inhibitor secreted by h

230 Overexpression of Z alpha1-antitrypsin is known to induce polymer formation, prime

231 Although alpha1 antitrypsin is mainly produced in the liver, its main fu

232 Alpha(1)-antitrypsin is the most abundant circulating protease in

233 l shutter domain mutant (His334Asp; alpha(1)-antitrypsin King's) identified in a 6-week-old boy who p

234 , whereas low levels of circulating Z alpha1-antitrypsin lead to emphysema by loss of inhibition of n

235 C and cathepsin Z in liver lysates or alpha1-antitrypsin levels in plasma.

236 AV vectors expressing normal, M-type alpha-1 antitrypsin (M-AAT) to AAT-deficient subjects at various

237 duction of polymers by mutant S and Z alpha1-antitrypsin may have also provided protection against in

238 ition to its antielastolytic effects, alpha1-antitrypsin may have broader biological effects in the l

239 nated cells expressing liver-specific alpha1-antitrypsin messenger RNA, albumin and hepatocyte nuclea

240 poE, apoF, apoH, apoJ, apoL-1, apoM, alpha-1 antitrypsin, migration inhibitory factor-related protein

241 conformational transition within the alpha1-antitrypsin molecule and the formation of polymers that

242 nophore, or when a nonpolymerogenic alpha(1)-antitrypsin mutant accumulated in the ER.

243 alpha-synuclein, PolyQ protein, and alpha-1-antitrypsin mutant protein.

244 ective, proinflammatory properties of alpha1-antitrypsin mutants have become detrimental to cause the

245 For alpha-one antitrypsin, new information on the incidence of the dis

246 epatocyte accumulation of defective alpha(1)-antitrypsin occurs.

247 effective at ratios of compound to Z alpha1-antitrypsin of 2.5:1 and reduced the intracellular accum

248 ed mice via transgenic expression of alpha-1-antitrypsin or IL-37 preserved the function of B cell pr

249 protease is not highly susceptible to alpha1-antitrypsin or secretory leukocyte protease inhibitor, w

250 yloid burden--c-peptide, fibrinogen, alpha-1-antitrypsin, pancreatic polypeptide, complement C3, vitr

251 level structural information on the alpha(1)-antitrypsin polymer.

252 eration of an mAb (4B12) that blocked alpha1-antitrypsin polymerization in vitro at a 1:1 molar ratio

253 omoter (murine albumin enhancer/human alpha1-antitrypsin promoter) further enhanced transgene express

254 y active FoxO1 in the liver using the alpha1-antitrypsin promoter.

255 of the TGF-beta signaling pathway and alpha1-antitrypsin protein (a serine protease inhibitor) expres

256 se, inefficient secretion of a mutant alpha1-antitrypsin protein (AAT-Z) results in its accumulation

257 uORF-dependent changes suggest that alpha-1-antitrypsin protein expression levels are controlled at

258 regions in neuroserpin relative to alpha(1)-antitrypsin provides a basis for neuroserpin's increased

259 His334Asp alpha(1)-antitrypsin rapidly forms polymers that accumulate withi

260 n the alveoli of individuals with Z alpha(1)-antitrypsin-related emphysema.

261 ruction that is characteristic of Z alpha(1)-antitrypsin-related emphysema.

262 physema in some individuals despite alpha(1)-antitrypsin replacement therapy.

263 structural alveolar cell apoptosis by alpha1-antitrypsin represents a novel protective mechanism of t

264 The common Z mutant (Glu342Lys) of alpha(1)-antitrypsin results in the formation of polymers that ar

265 eins including Factor-VII[rs555212], Alpha-1-Antitrypsin[rs11846959], Interferon-Gamma Induced Protei

266 irculating bioactive peptide from the alpha1-antitrypsin serine protease inhibitor.

267 with HLA-DP and the genes encoding alpha(1)-antitrypsin (SERPINA1) and proteinase 3 (PRTN3) (P=6.2x1

268 apolipoprotein A-1 [APOA1], 3.2-fold; alpha1-antitrypsin [SERPINA1], 2.5-fold; and complement C3 [C3]

269 ining an immobile matrix of polymeric alpha1-antitrypsin, small ER resident proteins can diffuse free

270 nology to identify interactors with Z alpha1-antitrypsin that comply with both requirements.

271 cy, hepatocytes accumulate defective alpha-1 antitrypsin that misfolds.

272 peptide corresponding to a portion of alpha1-antitrypsin that potently inhibits entry of HIV-1 into h

273 ody also increased the secretion of Z alpha1-antitrypsin that retained inhibitory activity against ne

274 ism and the cellular processing of alpha one antitrypsin, the highlights reviewed in this article wil

275 and the high risk of patients lacking alpha1-antitrypsin to develop emphysema, much interest has focu

276 The transition of native Z alpha(1)-antitrypsin to polymers inactivates its anti-proteinase

277 ltiply charged states at m/z 72,160 ([alpha1-antitrypsin + trypsin + H](+)) and 86,585 ([IgG + protei

278 or the detection of several proteins (alpha1-antitrypsin, trypsin, IgG, protein G) and their complexe

279 on of weak protein complexes, such as alpha1-antitrypsin-trypsin and IgG-protein G complexes, at the

280 ([IgG + protein G + 2H](2+)) for the alpha1-antitrypsin-trypsin and IgG-protein G complexes, respect

281 t which N-linked glycans of misfolded alpha1-antitrypsin variant NHK were trimmed.

282 D MAIN RESULTS: Transduction of human alpha1-antitrypsin via replication-deficient adeno-associated v

283 fications, affecting Lys292 in mouse alpha-1-antitrypsin, was detected in the corresponding lysine of

284 -latent transition of another serpin, alpha1-antitrypsin, which does not readily go latent.

285 est pathogenic gene mutation yields Z-alpha1-antitrypsin, which has a propensity to self-associate fo

286 YP2E1) by measuring the expression of alpha1-antitrypsin, which is controlled by these promoters and

287 Unlike other serpins such as alpha(1)-antitrypsin, wild-type neuroserpin will polymerize under

288 Wild-type alpha(1)-antitrypsin will form polymers upon incubation at modera

289 A variant of alpha(1)-antitrypsin with an E342K (Z) mutation (ATZ) has propens

290 luble secretory proteins (albumin and alpha1-antitrypsin) with that of supramolecular cargoes (e.g.,

291 polymers underlies the retention of alpha(1)-antitrypsin within hepatocytes and of neuroserpin within

292 ular accumulation of misfolded mutant alpha1-antitrypsin Z (ATZ) in hepatocytes causes hepatic damage

293 terized by accumulation of the mutant alpha1-antitrypsin Z (ATZ) variant inside cells, causing hepati

294 tracellular accumulation of misfolded alpha1-antitrypsin Z in respiratory epithelial cells of the PiZ

295 ted that the accumulation of mutant alpha(1)-antitrypsin Z in the ER specifically activates the autop

296 ers affecting the accumulation of the alpha1-antitrypsin Z mutant (ATZ) in a Caenorhabditis elegans m

297 ith the hepatic levels of insoluble alpha(1)-antitrypsin Z protein.

298 enic for the common misfolded variant alpha1-antitrypsin Z, is a model of respiratory epithelial cell

299 tical role in disposal of insoluble alpha(1)-antitrypsin Z.

300 ause of this disease is homozygosity for the antitrypsin-Z variant (ATZ).