ABCB1 p.Phe37Ala
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PMID: 18936737
[PubMed]
Hendig D et al: "Gene expression profiling of ABC transporters in dermal fibroblasts of pseudoxanthoma elasticum patients identifies new candidates involved in PXE pathogenesis."
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Comment
62
Table 1 Main characteristics of dermal fibroblasts derived from PXE patients and healthy controls used in the present study Sample ID Gender Agea Biopsy source ABCC6 genotypeb Statusc Age at disease onseta Number of involved organs PXE patients P60F Female 58 Axilla c.37-1G4A (SSM) c.37-1G4A (SSM) hm 56 3 P229F Female 50 NA c.1171A4G (p.R391G) c.1208C4A (p.A413N) c.2252T4A (p.M751K) cht NA NA P265F Female 62 Cervix c.1132C4T (p.Q378X) c.3421C4T (p.R1141X) cht 16 3 P3M Male 57 Cervix c.3421C4T (p.R1141X) c.3883-6G4A (SSM) cht 46 5 P128M Male 51 Cervix c.3769_3770insC (p.L1259fsX1277) c.3769_3770insC (p.L1259fsX1277) hm 48 3 P308M Male 42 NA c.3421C4T (p.R1141X) c.-90ins14 (c)ht NA NA P341M Male 41 NA c.1552C4T (p.R518X) ND ht NA NA Healthy controls F37A Female 37 Abdomen - - - wt - - F42A Female 42 Abdomen - - - wt - - F52C Female 52 Cheek - - - wt - - M2FS Male 2 Foreskin - - - wt - - M45D Male 45 Face - - - wt - - M56D Male 56 Face - - - wt - - hm, homozygote; cht, compound heterozygote; ht, heterozygote; wt, wild type; SSM, splice site mutation; NA, not applicable; ND, nondetected.
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ABCB1 p.Phe37Ala 18936737:62:758
status: NEW
PMID: 14622130
[PubMed]
Jodoin J et al: "P-glycoprotein in blood-brain barrier endothelial cells: interaction and oligomerization with caveolins."
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74
The mutated DNA was subcloned into the mammalian expression vector pcineo (Promega) to generate plasmid F37A-MDR1.
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ABCB1 p.Phe37Ala 14622130:74:104
status: NEW206 In order to further study the interaction between P-gp and caveolin-1, two P-gp proteins mutated in the caveolin-binding motif were produced: YWAA-MDR1 and F37A-MDR1.
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ABCB1 p.Phe37Ala 14622130:206:156
status: NEW208 In the other mutant, Phe37 was replaced with Ala (F37A-MDR1); nucleotide changes in the mutant genes were confirmed by sequencing.
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ABCB1 p.Phe37Ala 14622130:208:21
status: NEWX
ABCB1 p.Phe37Ala 14622130:208:50
status: NEW210 Immunodetection of P-gp in Cos-7 cells transiently transfected with the wild-type (WT)-MDR1, YWAA-MDR1, and F37A-MDR1 showed that WT-MDR1 and P-gp mutants were expressed to the same extent (Fig. 7a).
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ABCB1 p.Phe37Ala 14622130:210:108
status: NEW214 Figure 7(b) shows that relative fluorescence increased fourfold in WT-MDR1-, YWAA-MDR1-, and F37A-MDR1-expressing cells as compared to untransfected and f/s-MDR1-transfected cells.
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ABCB1 p.Phe37Ala 14622130:214:93
status: NEW217 Compared with WT-MDR1-transfected cells, the interaction between P-gp and caveolin-1 is reduced by 27% and 48% in cells expressing YWAA-MDR1 and F37A-MDR1, respectively (Fig. 8b).
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ABCB1 p.Phe37Ala 14622130:217:145
status: NEW221 In YWAA-MDR1and F37A-MDR1-transfected cells, Hoechst 33342 accumulation is lower than in WT-MDR1-transfected cells, indicating that mutation of caveolin-binding motif present in MDR1 P-gp affected its transport activity (Fig. 8b).
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ABCB1 p.Phe37Ala 14622130:221:16
status: NEW222 We also observed that P-gp is mainly located in caveolae in Cos-7 cells transfected with either WT-MDR1, YWAA-MDR1 or F37A-MDR1 (Fig. 8c).
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ABCB1 p.Phe37Ala 14622130:222:118
status: NEW248 (a) P-gp and caveolin-1 were immunodetected by western blot analysis in Cos-7 cells untransfected (cells were exposed to FuGENE 6 transfection reagent) or transiently transfected with WT-MDR1, YWAA-MDR1, F37A-MDR1, and f/s-MDR1 (n ¼ 4).
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ABCB1 p.Phe37Ala 14622130:248:204
status: NEW270 (a) Cos7 cells untransfected or transiently transfected with WT-MDR1, YWAA-MDR1, F37A-MDR1, and f/s-MDR1 were lysed in lysis buffer and cell lysate (500 lg of protein) was immunoprecipitated (IP) with 3 lg of mAb directed against P-gp (C219) followed by immunodetection (ID) of caveolin-1 (n ¼ 3).
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ABCB1 p.Phe37Ala 14622130:270:81
status: NEW309 Western blot and FACS analysis show that P-gp and caveolin-1 were expressed at constant levels in WT-MDR1-, YWAA-MDR1-, and F37A-MDR1-transfected cells, excluding the possibility of variation in protein expression.
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ABCB1 p.Phe37Ala 14622130:309:124
status: NEW
PMID: 18485890
[PubMed]
Barakat S et al: "Regulation of brain endothelial cells migration and angiogenesis by P-glycoprotein/caveolin-1 interaction."
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52
After 24 h, the cells were transiently transfected, in serum-free medium, with FuGENE 6 transfection reagent using 1 or 2 lg of DNA (either WT, YWAA or F37A).
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ABCB1 p.Phe37Ala 18485890:52:152
status: NEW132 In the other mutant, F37A, Phe37 (F) was replaced with Ala.
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ABCB1 p.Phe37Ala 18485890:132:21
status: NEW141 The caveolin-1/P-gp interaction was reduced by 25 and 35%, respectively, for the YWAA and F37A mutations (Fig. 3C).
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ABCB1 p.Phe37Ala 18485890:141:90
status: NEW142 Hoechst dye accumulation was decreased by similar amounts 22 and 28%, respectively, for the YWAA and F37A mutant transfected cells compared to the wild-type- transfected cells (Fig. 3D).
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ABCB1 p.Phe37Ala 18485890:142:101
status: NEW161 However, in the case of the mutants YWAA and F37A, the length of the capillary-like tubular structure was increased by about 75% compared to the wild-type MDR1 transfected cells.
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ABCB1 p.Phe37Ala 18485890:161:45
status: NEW186 However, the migration of cells transfected with either YWAA or F37A MDR1 was increased by 75% compared to the wild-type MDR1 transfected cells.
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ABCB1 p.Phe37Ala 18485890:186:64
status: NEW