ライフサイエンスコーパス: PMP22

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

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

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

4 duplication resulting in over-expression of PMP22.

5 restores the homeostatic profiles of MPZ and PMP22.

6 ting that this region contains regulators of PMP22.

7 of genes encoding myelin proteins, including PMP22.

8 affected nerves contain abnormally localized PMP22.

9 ption of the tightly regulated expression of PMP22.

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

11 among which is the peripheral myelin protein PMP22.

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

13 l be sensitive to subsequent upregulation of pmp22.

14 es to the ER, led to larger currents than WT PMP22.

15 by the HNPP-associated deletion encompassing PMP22.

16 is associated with increased gene dosage for PMP22.

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

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

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

20 dermal fibroblasts from patients with CMT1A, PMP22 aggregates have been observed.

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

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

23 ment 17p11.2-12, which results in a third WT PMP22 allele.

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

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

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

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

28 The absence of PMP22 also impaired ABCA1-mediated cholesterol efflux ca

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

30 lation of ion channels, we hypothesized that PMP22 alters ion channel activity.

31 eling identified overlapping distribution of PMP22 and ABCA1 at the Schwann cell plasma membrane and

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

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

38 On the basis of homology between PMP22 and proteins associated with modulation of ion cha

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

63 ve myelin gene Peripheral Myelin Protein 22 (PMP22) causes multiple forms of inherited peripheral neu

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

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

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

67 alities involve a functional interplay among PMP22, cholesterol, apolipoprotein E, and the major chol

68 Moreover, we found that PMP22 co-immunoprecipitated with stromal interaction mol

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

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

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

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

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

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

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

76 Nerves from PMP22-deficient mice contained abnormal lipid droplets,

77 PMP22-deficient mice show strong beta-galactosidase reac

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

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

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

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

82 neuropathy with liability to pressure palsy/PMP22 deletion.

83 nstrate that the ordered phase preference of PMP22 derives from global structural features associated

84 EMP2 and PMP22 differentially regulate collagen gel contraction i

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

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

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

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

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

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

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

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

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

94 Pmp22 enhancers contain binding motifs for TEA domain (T

95 While Pmp22 enhancers marked by active histone modifications w

96 2s form complexes larger than dimers with Tr Pmp22 especially prone to aggregate into high molecular

97 ical tetraspan peripheral myelin protein 22 (PMP22) exhibits a pronounced preference for, promotes th

98 ntitatively examine the relationship between PMP22 expression and trafficking efficiency in individua

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

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

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

102 stal super-enhancer domain was important for Pmp22 expression in vitro, with particular impact on a S

103 rophysiology, we show here that heterologous PMP22 expression increases the amplitude of currents sim

104 PMP22 expression is highest in myelinating Schwann cells

105 t loss of the super-enhancer in mice reduces Pmp22 expression throughout development and into adultho

106 PMP22 expression was measured by taking skin biopsies fr

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

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

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

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

111 in mediating the developmental induction of Pmp22 expression.

112 induced during myelination, correlating with Pmp22 expression.

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

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

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

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

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

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

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

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

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

122 er copy number variations, not including the Pmp22 gene, are sufficient to reduce gene expression and

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

124 surrounding Peripheral Myelin Protein 22, or PMP22 gene, which is classified as CMT1A.

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

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

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

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

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

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

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

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

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

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

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

136 odimers traffic with their respective mutant Pmp22 homodimers.

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

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

139 phology, supporting an unrecognized role for PMP22 in cellular lipid metabolism.

140 ts support the notion that overexpression of PMP22 in CMT1A leads to a disproportionate increase in m

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

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

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

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

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

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

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

148 ether, these results reveal a novel role for PMP22 in regulating lipid metabolism and cholesterol tra

149 However, the role of PMP22 in Schwann cell physiology and the mechanisms by w

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

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

152 Excess or mutant PMP22 in the ER may elevate intracellular Ca(2+) levels,

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

154 These findings establish a critical role for PMP22 in the maintenance of cholesterol homeostasis in S

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

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

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

158 22 is increased, the amount of intracellular PMP22 increases to a greater extent than the amount of s

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

160 These results suggest that in the ER, PMP22 interacts with STIM1 and increases Ca(2+) influx t

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

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

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

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

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

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

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

168 t as expression of WT or disease variants of PMP22 is increased, the amount of intracellular PMP22 in

169 As PMP22 is localized to cholesterol-enriched membrane doma

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

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

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

173 PMP22 is robustly induced in Schwann cells in early post

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

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

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

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

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

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

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

181 Peripheral myelin protein 22 (PMP22) is an essential peripheral myelin protein because

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

183 of functional peripheral myelin protein 22 (PMP22) is associated with shortened lifespan in rodents

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

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

186 Schwann cells and nerves from PMP22 knock-out (KO) mice show deranged cholesterol dist

187 chwann cells and nerves from male and female PMP22 KO mice.

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

189 ng analysis showed reproducible elevation of PMP22 levels in CMT1A versus control skin biopsies, part

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

191 lop a novel method for precise evaluation of PMP22 levels in skin biopsies that can discriminate CMT1

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

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

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

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

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

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

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

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

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

201 ave been previously observed in heterozygous Pmp22 mice as well as sural biopsies from patients with

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

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

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

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

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

207 milar properties were recorded in WT but not pmp22 (-/-) mouse Schwann cells.

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

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

210 1A, but this approach did not show increased PMP22 mRNA in CMT1A patients compared to controls.

211 Quantitative PCR measurements of PMP22 mRNA in dermal nerves were performed using skin bi

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

213 Several candidate therapies reduce Pmp22 mRNA levels in CMT1A rodent models, but developmen

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

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

216 2 mRNA but decreased levels of MPZ, MBP, and Pmp22 mRNA.

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

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

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

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

221 Most PMP22 mutations alter the trafficking of the PMP22 prote

222 cell physiology and the mechanisms by which PMP22 mutations cause CMT are not well-understood.

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

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

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

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

227 it overlaps among distinct genetic models of PMP22 neuropathies.

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

229 Neither S-palmitoylation of PMP22 nor its putative cholesterol binding motifs are re

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

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

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

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

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

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

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

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

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

239 PMP22 overproducer C22 and spontaneous mutant Trembler J

240 ed ability of p.Asp411Gly EGR2 to activate a PMP22 (peripheral myelin protein 22) enhancer element co

241 In rodent models overexpressing the PMP22 (peripheral myelin protein 22) protein and in derm

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

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

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

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

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

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

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

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

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

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

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

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

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

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

256 regulation of ABCA1 and apoE, the absence of PMP22 resulted in reduced localization of the transporte

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

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

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

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

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

262 e for both transiently transfected cells and PMP22 stable expressing cells.

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

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

265 sing mutations that disrupt the stability of PMP22 tertiary structure reduce or eliminate this prefer

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

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

268 Here, we demonstrate that in the absence of PMP22, the cellular and electrophysiological properties

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

270 mutations in the first CMT associated gene, PMP22, the technological advancement in molecular geneti

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

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

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

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

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

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

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

278 We have developed methods to normalize PMP22 transcript levels to SC-specific genes that are no

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

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

281 This suggests that overexpression of PMP22 under CMT1A conditions overwhelms the endoplasmic

282 ere permissive in early development prior to Pmp22 upregulation.

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

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

285 Because PMP22 was originally identified in fibroblasts as growth

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

287 nerves from ABCA1 KO mice, the expression of PMP22 was significantly elevated and the subcellular pro

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 increase in misfolding and mistrafficking of PMP22, which is likely a contributor to disease patholog

293 reased membrane resistance in the absence of PMP22, which was consistent with a reduction in membrane

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.