ライフサイエンスコーパス: PMP22

1 nactivation of one of the two pmp22 alleles (pmp22(+/-)).

2 ased dosage of peripheral myelin protein 22 (PMP22).

3 ining the peripheral myelin protein 22 gene (Pmp22).

4 ludes the peripheral myelin protein 22 gene (PMP22).

5 yelin, such as peripheral myelin protein 22 (PMP22).

6 affected nerves contain abnormally localized PMP22.

7 ption of the tightly regulated expression of PMP22.

8 in which patients have only a single copy of PMP22.

9 among which is the peripheral myelin protein PMP22.

10 eptides from the myelin proteins P0, P2, and PMP22.

11 l be sensitive to subsequent upregulation of pmp22.

12 n, TrJ-PMP22 forms a heterodimer with the wt-PMP22.

13 tution in the second transmembrane domain of PMP22.

14 escribed recently, and 39% identity to human PMP22.

15 ra-transmembrane-spanning protein encoded by pmp22.

16 distinct from the peripheral myelin protein PMP22.

17 mal in vivo post-translational processing of PMP22.

18 is associated with increased gene dosage for PMP22.

19 duplication resulting in over-expression of PMP22.

20 ting that this region contains regulators of PMP22.

21 of genes encoding myelin proteins, including PMP22.

22 e encoding the peripheral myelin protein 22 (PMP22), a tetraspan protein in compact peripheral myelin

23 ulated in invasive breast cancers, including PMP22, ABCC3, AGR2, Sox3, TM4SF1, and p8 (NUPR1).

24 suggest that T118M PMP22 retains some normal PMP22 activity, allowing the formation of compact myelin

25 tophagy is able to suppress the formation of PMP22 aggregates in a toxin-induced cellular model, and

26 these characteristics, we hypothesized that PMP22 aggresomes are transitory, linking the proteasomal

27 trafficking of the product of the wild-type PMP22 allele.

28 HNPP) with an inactivation of one of the two pmp22 alleles (pmp22(+/-)).

29 rpose of this study was to determine whether PMP22 also controls the contractile phase associated wit

30 Wild-type Pmp22 also forms heterodimers with Tr and TrJ Pmp22, and

31 Peripheral myelin protein 22 (PMP22), also known as growth arrest-specific gene 3 (gas

32 antisense oligonucleotides (ASOs) to reduce PMP22 and ameliorated neuropathy in both mouse and rat m

33 During early stages of myelination, PMP22 and beta4 integrin are coexpressed at the cell sur

34 interacts with the 3' untranslated region of PMP22 and downregulates its expression.

35 the expression of Egr2 Tead1 directly binds Pmp22 and Egr2 enhancers early in development and Tead1

36 rve of Trembler J mice, which are mutant for pmp22 and have a demyelinating/hypomyelinating phenotype

37 e with RM (25 nm) improved the processing of PMP22 and increased the abundance and length of myelin i

38 c nerves and brains were coimmunostained for PMP22 and known junctional proteins including zonula occ

39 Mutational screening for the PMP22 and P0 genes and nerve biopsy are therefore merite

40 In these, no abnormality for the PMP22 and P0 genes was detected and a mutation at anothe

41 rearrangements that simultaneously duplicate PMP22 and RAI1, including nine potential complex genomic

42 duplication of peripheral myelin protein 22 (PMP22) and is the most common hereditary peripheral neur

43 sential myelin-associated genes as Mpz, Mbp, Pmp22, and Mag.

44 icates that the degradation of protein zero, PMP22, and myelin basic protein is augmented in TrJ nerv

45 nn cell differentiation markers (SOX10, CNP, PMP22, and NGFR) was down-regulated in MPNSTs whereas ne

46 mp22 also forms heterodimers with Tr and TrJ Pmp22, and these heterodimers traffic with their respect

47 Peripheral myelin protein 22 (PMP22), another member of the tetraspan web, is closely

48 munoreactive for both anti-occludin and anti-PMP22 antibodies.

49 ) and the peripheral myelin protein 22 gene (PMP22), appear to make aberrant proteins that accumulate

50 Duplication, deletion, or point mutations in PMP22 are associated with a host of demyelinating periph

51 s with CMT1A and determine whether levels of PMP22 are molecular markers of disease severity.

52 The key dosage-sensitive genes RAI1 and PMP22 are respectively associated with PTLS and CMT1A.

53 mbrane protein peripheral myelin protein 22 (PMP22) are known to result in peripheral neuropathies su

54 t mutations in peripheral myelin protein 22 (PMP22) are linked to several inherited peripheral neurop

55 Together, these studies identify PMP22 as an early constituent of intercellular junctions

56 ecognizes the G150D and L16P mutant forms of PMP22 as defective through mechanisms closely related to

57 lin stability is also sensitive to levels of PMP22, as a 1.4 Mb duplication on human chromosome 17, r

58 cultured epithelial cells did not solubilize PMP22, as the majority of the protein remained in the de

59 nhancing compounds as therapeutic agents for PMP22-associated demyelinating neuropathies.

60 J condition leads to the most severe form of PMP22-associated neuropathies.

61 To begin to elucidate the role of PMP22 at cell junctions, we examined the temporal expres

62 These studies support a role for PMP22 at intercellular junctions of epithelia and may in

63 It was also seen that wild-type PMP22 binds Zn(II) and Cu(II) with micromolar affinity,

64 Recently, duplications upstream of PMP22, but not containing the gene itself, were reported

65 It is unknown whether PMP22 can be used as a biological marker of disease prog

66 sufficiency of peripheral myelin protein 22 (PMP22) causes hereditary neuropathy with liability to pr

67 ne mutation in peripheral myelin protein 22 (PMP22) causes the Trembler-J (TrJ) neuropathy in mice an

68 PMP22 cDNA produced by the reverse transcriptase-polymer

69 ed to express tTA, the LacZ reporter and the pmp22 cDNA were all very dependent on the position of in

70 , was reduced by greater than 50% in ARPE-19/PMP22 cells (P < 0.001).

71 e decrease in gel contraction by the ARPE-19/PMP22 cells was partially reversed through either PMP22

72 Like PMP22, CL-20 is likely to play important roles in the re

73 The presence of cytosolic PMP22 coincides with a decrease in proteasome activity a

74 Our study reveals a novel mechanism by which PMP22 deficiency affects nerve conduction not through re

75 Our previous study has shown that PMP22 deficiency causes an impaired propagation of nerve

76 ether the myelin instability associated with PMP22 deficiency could be mediated by involvement of the

77 Patients with PMP22 deficiency present with focal sensory and motor de

78 ion, which may hasten the induction of CB in Pmp22 deficiency.

79 ability to pressure palsies (HNPP) caused by PMP22 deficiency.

80 PMP22-deficient mice show strong beta-galactosidase reac

81 al lamina, are severely reduced in nerves of PMP22-deficient mice.

82 Furthermore, PMP22-deficient Schwann cells produce shortened myelin i

83 ccurrence of the 17p11.2 duplication and the PMP22 deletion in this patient likely reflects the relat

84 (p11.2p11.2) is a de novo event but that the PMP22 deletion is familial.

85 generation and fiber loss, and the affect of PMP22 deletion on axonal cytoskeleton is less deleteriou

86 uropathy with liability to pressure palsies (PMP22 deletion).

87 n peripheral nerves and cells from mice with PMP22 deletion, we assessed the organization of filament

88 neuropathy with liability to pressure palsy/PMP22 deletion.

89 EMP2 and PMP22 differentially regulate collagen gel contraction i

90 genomic interval encompassing both RAI1 and PMP22 do not share extensive homology; thus, duplication

91 rexpression of peripheral myelin protein 22 (PMP22) due to a genomic duplication.

92 Our findings indicate that the PMP22 duplication in Schwann cells results in an impairm

93 enetic subtypes, 111 participants with CMT1A/PMP22 duplication progressed by 1.8 +/- 4.2 (12% change

94 n protein 22 (PMP22) was increased in CMT1A (PMP22 duplication) and decreased in patients with heredi

95 most common genetic defect in Schwann cells (PMP22 duplication) causes the CMT1A phenotype and result

96 The most common CMT subtypes were CMT1A/PMP22 duplication, CMT1X/GJB1 mutation, CMT2A/MFN2 mutat

97 , sural nerve segments from individuals with PMP22 duplications or deletions, causing the reciprocal

98 wo transcription factors known to upregulate PMP22-EGR2 and SOX10-we found several enhancers in this

99 ties in the subcellular processing of excess PMP22 elicit a detectable response in human CMT1A fibrob

100 evolutionarily distant relatives called the PMP22/EMP/MP20/claudin, or pfam00822, superfamily.

101 Here, we examined Pmp22 enhancers as a function of cell type-specificity,

102 Pmp22 enhancers contain binding motifs for TEA domain (T

103 While Pmp22 enhancers marked by active histone modifications w

104 2s form complexes larger than dimers with Tr Pmp22 especially prone to aggregate into high molecular

105 data identify Tead1 as a novel regulator of Pmp22 expression during development in concert with Sox1

106 rding how other transcription factors induce Pmp22 expression during Schwann cell development and mye

107 s performed on the skin biopsies to quantify PMP22 expression in compact myelin.

108 PMP22 expression is highest in myelinating Schwann cells

109 PMP22 expression was measured by taking skin biopsies fr

110 genetic background and the level of LacZ or pmp22 expression was very variable between mice.

111 adult mice (which had previously had normal pmp22 expression) is followed by active demyelination wi

112 d co-activators Yap and Taz are required for Pmp22 expression, as well as for the expression of Egr2

113 induced during myelination, correlating with Pmp22 expression.

114 mal activity of the intronic site as well as PMP22 expression.

115 in mediating the developmental induction of Pmp22 expression.

116 ch of two peptides (250 microg) of the human PMP22 extracellular sequences.

117 for the first time the interaction of a GAS3/PMP22 family member with an integrin protein and suggest

118 Epithelial membrane protein-2 (EMP2), a GAS3/PMP22 family member, was recently identified as a putati

119 influence the energetics of Zn(II)-mediated PMP22 folding is proportional to the observed reduction

120 ects of these mutations on the energetics of PMP22 folding lie at the heart of the molecular basis of

121 ne A colonic carcinoma cells, epitope-tagged PMP22 forms a complex with beta4 integrin.

122 In addition, TrJ-PMP22 forms a heterodimer with the wt-PMP22.

123 y inherited form of CMT by a partial loss of PMP22 function.

124 d potential regulatory sequences upstream of PMP22, further supporting the contention that PMP22 is t

125 Ten Lewis rats were immunized with purified PMP22 fusion protein (50-100 microg) and eight controls

126 mice carrying increasing copies of the human PMP22 gene (one to seven) and expressing increasing leve

127 Duplications, deletions, or mutations in the PMP22 gene account for a set of dominantly inherited per

128 asts from two CMT1A pedigrees with confirmed PMP22 gene duplication were studied.

129 as to determine whether an extra copy of the PMP22 gene in CMT1A disrupts the normally coordinated ex

130 h levels of expression of the mouse or human PMP22 gene leading to severe demyelination.

131 ach of these CNVs includes either the entire PMP22 gene, or exon(s) only, or ultraconserved potential

132 drome, can occur because of deletions of the PMP22 gene.

133 Egr2 binding within the large intron of the Pmp22 gene.

134 the candidate peripheral myelin protein 22 (PMP22) gene detected a unique G-->C transversion in the

135 Alterations in peripheral myelin protein 22 (PMP22) gene expression are associated with a host of her

136 The peripheral myelin protein-22 (PMP22) gene is associated with the most common types of

137 eletion of the peripheral myelin protein 22 (PMP22) gene within 17p12 on the homologous chromosome.

138 ns in the peripheral myelin protein, 22 kDa (PMP22) gene, protein zero (P0) gene, early growth respon

139 involving the Peripheral Myelin Protein 22 (PMP22) gene, which is located within a 1.4-Mb duplicatio

140 h contains the peripheral myelin protein-22 (PMP22) gene.

141 ication of the peripheral myelin protein 22 (PMP22) gene.

142 tations in the peripheral myelin protein 22 (PMP22) gene.

143 Mutations or rearrangements in PMP22, GJB1, MPZ and MFN2 accounted for over 90% of the

144 In TrJ neuropathy nerves, PMP22 has an extended half-life and forms aggresome-like

145 to be a threshold below which expression of PMP22 has virtually no effect; below a ratio of human/mo

146 However, the function of PMP22 has yet to be defined.

147 The family members with deletions of PMP22 have abnormalities indicative of carpal tunnel syn

148 These data confirm that strategies to reduce PMP22 have potential as effective therapeutic approaches

149 The relative stability of a wt-mutant PMP22 heterodimer as compared with the wt-wt PMP22 homod

150 PMP22 heterodimer as compared with the wt-wt PMP22 homodimer may determine whether a particular mutat

151 odimers traffic with their respective mutant Pmp22 homodimers.

152 Expression of human PMP22 (hPMP22) slows cell growth and induces a flattened

153 PMP22-immunized animals developed antibodies to the fusi

154 the ankle were significantly reduced in the PMP22-immunized group (P < 0.05).

155 Overexpression of PMP22 in ARPE-19 cells (ARPE-19/PMP22) resulted in incre

156 e analysis revealed novel point mutations in Pmp22 in both lines.

157 The extra copy of PMP22 in CMT1A results in disruption of the tightly regu

158 The levels of PMP22 in CMT1A were highly variable, but not in HNPP or

159 Increased levels of PMP22 in compact myelin of peripheral nerves have been d

160 The subcellular localization of PMP22 in cultured brain endothelia was confirmed by inte

161 emise for oxidation-dependent aggregation of PMP22 in dbdb mice.

162 abeling experiments show the accumulation of PMP22 in endosomal/lysosomal structures of TrJ Schwann c

163 In this report, we investigated the role of PMP22 in epithelial biology.

164 mp22s sequester the same amount of wild-type Pmp22 in heterodimers and heterooligomers.

165 ed for induction of high level expression of Pmp22 in Schwann cells but its activation elements have

166 Although the function of PMP22 in Schwann cells is unknown, the protein is found

167 tion of the wt-PMP22 to be retained with TrJ-PMP22 in the intermediate compartment of COS7 and Schwan

168 function via the accumulation of wt- and TrJ-PMP22 in the intermediate compartment.

169 Our findings support a novel role for PMP22 in the linkage of the actin cytoskeleton with the

170 appear to be closely linked to misfolding of PMP22 in the membrane of the endoplasmic reticulum (ER).

171 mutation, we labeled wild-type (wt-) and TrJ-PMP22 in the third loop of the protein with different ep

172 nvolving the peripheral myelin protein gene (PMP22) in human chromosome 17p12 are associated with neu

173 rexpression of peripheral myelin protein 22 (PMP22) in Schwann cells of the peripheral nervous system

174 We further demonstrate that PMP22 interacts with immunoglobulin domain-containing pr

175 Together, these data indicate that PMP22 is a binding partner in the integrin/laminin compl

176 nd distribution of cholesterol and ApoE when PMP22 is absent.

177 It appears that detergent-solubilized PMP22 is amenable to detailed structural characterizatio

178 These results indicate that PMP22 is capable of modulating several aspects of epithe

179 The correct gene dosage of PMP22 is critical; a duplication of PMP22 is the most co

180 In choroid epithelia, PMP22 is detected along with occludin and ZO-1 as early

181 PMP22 is highly helical and, in certain detergents, show

182 we show that the transport of the mutant TrJ-PMP22 is interrupted in the intermediate compartment, pr

183 As PMP22 is localized to cholesterol-enriched membrane doma

184 rane constituent of peripheral nerve myelin, PMP22 is localized to epithelial and endothelial cell-ce

185 adult heterozygous TrJ animals, the level of PMP22 is markedly decreased, similar to myelin basic pro

186 pact on PMP22 transcriptional regulation and PMP22 is not a suitable biomarker for CMT1A.

187 tion of the tight junction protein occludin, PMP22 is present at ZO-1 positive endothelial junctions

188 When overexpression of pmp22 is switched off in adult mice, correction begins w

189 MP22, further supporting the contention that PMP22 is the critical gene mediating the neuropathy phen

190 osage of PMP22 is critical; a duplication of PMP22 is the most common cause of the peripheral neuropa

191 these results demonstrate that a function of Pmp22 is to protect the nerve from mechanical injury.

192 Since peripheral myelin protein 22 (PMP22) is a key component of myelin sheath and has been

193 Peripheral myelin protein 22 (PMP22) is a short-lived Schwann cell (SC) protein that f

194 Peripheral myelin protein 22 (PMP22) is a tetraspan membrane glycoprotein, the misexpr

195 Peripheral myelin protein 22 (PMP22) is an integral membrane protein that is essential

196 Peripheral myelin protein 22 (PMP22) is associated with a subset of hereditary periphe

197 A gene within the 1.4-Mb region, PMP22, is responsible for these disorders through a gene

198 chromosome 17, resulting in three copies of PMP22, is the most common cause of the peripheral neurop

199 (classified as type 1A), while a deletion of PMP22 leads to another peripheral neuropathy, hereditary

200 ut not all patients with CMT1A, had elevated PMP22 levels in myelin compared with the controls.

201 Thus, variability of PMP22 levels, rather than absolute level of PMP22, may p

202 , and cultured epithelial cells, we detected PMP22-like immunoreactivity associated with markers of t

203 Two loci, GLUT4 and PMP22, located on HSA17p, were mapped by FISH to dog chr

204 atin immunoprecipitation analysis of the rat Pmp22 locus, we found a major peak of Egr2 binding withi

205 increase in carbonylation and aggregation of PMP22 may be associated with demyelination in dbdb mice.

206 PMP22 levels, rather than absolute level of PMP22, may play an important role in the pathogenesis of

207 In agreement, PMP22 message is elevated in P1 rat brain microvasculatu

208 , we did not observe any correlation between PMP22 messenger RNA levels and the different clinical an

209 We did not find increased PMP22 messenger RNA levels in skin and sural nerve biops

210 Finally, we analysed PMP22 messenger RNA levels in sural nerve biopsies.

211 Utilizing Pmp22(+) (/) (-) mice as a model of HNPP, we evaluated m

212 ntly shorter in pmp22(+/-) mice than that in pmp22(+/+) mice.

213 time for the CB was significantly shorter in pmp22(+/-) mice than that in pmp22(+/+) mice.

214 ncisures do not form properly in nerves from PMP22(-/-) mice, and the expression and localization of

215 erefore, we speculate that mutant, misfolded PMP22 might overload the proteasome and promote aggresom

216 We found that PMP22 mRNA but not protein is detectable in oligodendroc

217 oligonucleotides (ASOs) effectively suppress PMP22 mRNA in affected nerves in 2 murine CMT1A models.

218 rthermore, we demonstrated that reduction of PMP22 mRNA in skin biopsies from ASO-treated rats is a s

219 es were analysed by real time PCR to measure PMP22 mRNA levels.

220 in approximately 1.5-fold elevated levels of PMP22 mRNA, exhibit reduced mitotic potential, and displ

221 2 mRNA but decreased levels of MPZ, MBP, and Pmp22 mRNA.

222 heral nerves; however, significant levels of PMP22 mRNAs can be detected in a variety of non-neural t

223 , for normal SC cell function, the levels of PMP22 must be tightly regulated.

224 A number of disease-linked PMP22 mutants fail to undergo normal trafficking beyond

225 ment of cells in tissue culture that express PMP22 mutants.

226 Most PMP22 mutations alter the trafficking of the PMP22 prote

227 ion of wild-type Pmp22 with those of the two Pmp22 mutations found in Trembler (Tr) and Trembler J (T

228 P0)(+) and peripheral myelin protein 22-kDa (PMP22)(+) myelin, normally only produced by Schwann cell

229 In the absence of PMP22, myelination of peripheral nerves is delayed, and

230 Pmp22(+/-) nerves showed intact tomacula with no segment

231 it overlaps among distinct genetic models of PMP22 neuropathies.

232 ide an explanation for certain phenotypes of PMP22 neuropathy mice that cannot be accounted for by dy

233 PMP22 now deserves consideration as an autoantigen in hu

234 ferentiation, particularly in neural (Epha4, Pmp22, Nrp1, Gap43, Ndn) and smooth muscle differentiati

235 In this mouse model, overexpression of pmp22 occurs specifically in Schwann cells of the periph

236 n the dominant-negative effect of the mutant Pmp22 on wild-type Pmp22 trafficking.

237 n in peripheral nerve myelin and to evaluate PMP22 over-expression in patients with CMT1A and determi

238 pproaches are currently aiming at correcting PMP22 over-expression.

239 ated a transgenic mouse model in which mouse pmp22 overexpression can be regulated.

240 contrast, myelination is nearly normal when pmp22 overexpression is switched off throughout life by

241 tion observed by increasing EMP2 expression, PMP22 overexpression led to increased AKT activation.

242 f CMT1A have been used to show that reducing Pmp22 overexpression mitigates several aspects of a CMT1

243 PMP22 overproducer C22 and spontaneous mutant Trembler J

244 nd, but not the first, extracellular loop of PMP22 perturb the recovery of TER and paracellular flux.

245 nstrated that peripheral myelin gene MPZ and PMP22 promoter activities, transcripts, and protein leve

246 nd Y153TER in the other mutant truncates the Pmp22 protein by seven amino acids.

247 To date, PMP22 protein expression and localization in non-neural

248 rupts the normally coordinated expression of PMP22 protein in peripheral nerve myelin and to evaluate

249 PMP22 mutations alter the trafficking of the PMP22 protein in Schwann cells, and this different traff

250 he expression levels and localization of the PMP22 protein in the TrJ mouse have not been previously

251 dendrocytes, whereas Schwann cells producing PMP22 protein lack miR-9.

252 bilities and the level of over-expression of PMP22 protein or mRNA in patients with CMT1A.

253 ro oxidation-induced aggregation of purified PMP22 protein supported the premise for oxidation-depend

254 The growth arrest-specific-3 (GAS3)/PMP22 proteins are members of the four-transmembrane (te

255 of these proteins is poorly understood, GAS3/PMP22 proteins have been implicated in the control of gr

256 consequences are a physiologic role of GAS3/PMP22 proteins.

257 anisms as a predominant mechanism underlying PMP22-RAI1 contiguous gene duplications and provides fur

258 Mechanistic studies of Pmp22 regulation identified enhancers regulated by the S

259 xpression of PMP22 in ARPE-19 cells (ARPE-19/PMP22) resulted in increased collagen adhesion.

260 These findings suggest that T118M PMP22 retains some normal PMP22 activity, allowing the f

261 cts the elongation and migration deficits of PMP22(-/-) Schwann cells, suggesting that the observed f

262 se cleavage site, a Strep tag, and the human PMP22 sequence.

263 ots from the group of animals immunized with PMP22 showed sparse infiltration of mononuclear cells, o

264 cells was partially reversed through either PMP22 siRNA or by blockade of AKT.

265 myelin are sensitive to increased amounts of pmp22 such that they rapidly demyelinate.

266 afficking-incompetent mutants with wild-type PMP22, such that both the wild-type protein and the muta

267 is highly conserved among CL-20, EMP-1, and PMP22, suggesting a functional role for this region.

268 ability of two human disease mutant forms of PMP22 that are also the basis for mouse models of periph

269 whether peripheral nerve myelin protein-22 (PMP22), the gene for which is duplicated in hereditary m

270 mbrane protein peripheral myelin protein 22 (PMP22), the intracellular misfolding of which is known t

271 odels, we discovered that, in the absence of PMP22, the migration and adhesion capacity of Schwann ce

272 the differences in aggregation of Tr and TrJ Pmp22, these two mutant Pmp22s sequester the same amount

273 Overexpression of pmp22 throughout life (in the absence of tetracycline) c

274 served the targeting of exogenous myc-tagged PMP22 to apical cell junctions in polarized epithelia an

275 This interaction causes a fraction of the wt-PMP22 to be retained with TrJ-PMP22 in the intermediate

276 existing data regarding the relationship of PMP22 to CMTD may be useful to explain phenotypes of sev

277 tcome measures, underscoring the weakness of PMP22 to mirror the phenotypic variability of patients w

278 result both from decreased trafficking of wt-PMP22 to the plasma membrane and from a toxic gain of fu

279 elationship of peripheral myelin protein 22 (PMP22) to Charcot-Marie-Tooth disease (CMTD) type 1A.

280 tive effect of the mutant Pmp22 on wild-type Pmp22 trafficking.

281 shows that ascorbic acid does not impact on PMP22 transcriptional regulation and PMP22 is not a suit

282 icant differences in the levels of any known PMP22 transcripts in treated or untreated patients with

283 ere permissive in early development prior to Pmp22 upregulation.

284 Indeed, PMP22 was found to be carbonylated and aggregated in sci

285 Upon disruption of intercellular contacts, PMP22 was internalized into vesicles that were immunorea

286 Because PMP22 was originally identified in fibroblasts as growth

287 ollowing TEV cleavage of the fusion partner, PMP22 was purified and its structural properties were ex

288 Peripheral myelin protein 22 (PMP22) was increased in CMT1A (PMP22 duplication) and de

289 To investigate the potential roles of PMP22, we engineered a novel knock-out (-/-) mouse line

290 To characterize the molecular defects in PMP22, we examined the structure and stability of two hu

291 ce carrying a leucine-to-proline mutation in PMP22 were studied.

292 er of the peripheral myelin protein 22 gene (PMP22), which lies within the critical region.

293 er of the peripheral myelin protein-22 gene, PMP22, which maps within the critical region.

294 e by replacing the first two coding exons of pmp22 with the lacZ reporter.

295 er, we compared the aggregation of wild-type Pmp22 with those of the two Pmp22 mutations found in Tre

296 ycin (RM) could facilitate the processing of PMP22 within neuropathic SCs and enhance their capacity

297 Relative expression of EMP2 or PMP22 within the tetraspan web drives a cellular respons

298 c retention of peripheral myelin protein 22 (PMP22) within Schwann cells (SCs) is associated with a g

299 nn cells (SCs) produce the highest levels of PMP22, yet the function of the protein in peripheral ner

300 e embryonic rat brain are immunoreactive for PMP22, ZO-1, and beta-catenin but not occludin.