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Blood, Vol. 109, Issue 10, 4383-4391, May 15, 2007
The thymic theme of acetylcholinesterase splice variants in myasthenia gravis
Blood Gilboa-Geffen et al.
109: 4383
Supplemental materials for: Gilboa-Geffen et al, Vol 109, Issue 10, 4383-4391
Files in this Data Supplement:
- Document 1. Common description for all the Supplemental Tables (PDF, 73.8 KB)
- Table S1. Biological Process (BP) changes compared between thymus data from MG patients undergoing therapeutic thymectomy due to severe thymic hyperplasia (MH; n = 5) to those of 1-week-old to 1-year-old controls (NB; n = 10) (XLS, 217 KB)
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The mean expression ratio calculated for each group and log2 ratio between MH/NB found for each transcript are shown. Functional analysis to identify overrepresented BP GO categories was performed as described.
- Table S2. Molecular Function (MF) changes compared between thymus data from MG patients undergoing therapeutic thymectomy due to severe thymic hyperplasia (MH; n=5) to those of 1-week-old to 1-year-old controls (NB; n = 10) (XLS, 202 KB)
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The mean expression ratio calculated for each group and log2 ratio between MH/NB found for each transcript are shown. Functional analysis to find over-represented MF GO categories was performed as described.
- Table S3. Biological Process (BP) changes compared between thymus data from MG patients undergoing therapeutic thymectomy due to mild thymic hyperplasia (ML; n = 4) to those of 1-week-old to 1-year-old controls (NB; n = 10) (XLS, 220 KB)
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The mean expression ratio calculated for each group and log2 ratio between ML/NB found for each transcript are shown. Functional analysis to identify over-represented BP GO categories was performed as described.
- Table S4. Molecular Function (MF) changes compared between thymus data from MG patients undergoing therapeutic thymectomy due to mild thymic hyperplasia (ML; n=4) to those of 1-week-old to 1-year-old controls (NB; n = 10) (XLS, 204 KB)
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The mean expression ratio calculated for each group and log2 ratio between ML/NB found for each transcript are shown. Functional analysis to identify overrepresented MF GO categories was performed as described.
- Table S5. Biological Process (BP) changes compared between expression data for thymuses removed from adult healthy controls (n=4) to those of 1-week-old to 1-year-old controls (NB; n=10) (XLS, 219 KB)
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The mean expression ratio calculated for each group and log2 ratio between ML/NB found for each transcript are shown. Functional analysis to identify over-represented BP GO categories was performed as described.
- Table S6. Molecular Function (MF) changes compared between expression data for thymuses removed from adult normal controls (n=4) to those of 1-week-old to 1-year-old controls (NB; n=10) (XLS, 206 KB)
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The mean expression ratio calculated for each group and log2 ratio between ML/NB found for each transcript are shown. Functional analysis to identify overrepresented MF GO categories was performed as described.
- Figure S1. The experimental paradigm (JPG, 51.9 KB)
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(A) The ACHE gene and its RT-PCR amplified domains. Shown is the schematic structure of the mammalian ACHE gene, with numbered exons presented as boxes and introns as connecting lines between them. RT-PCR primers (arrows) for amplifying the various AChE mRNA transcripts were designed in the noted positions along this gene. C indicates common domain, appearing in all variants; R, region unique for AChE-R mRNA; S, region characteristic of AChE-S mRNA. (B) The biochemical procedure used. Tissue homogenates were subfractionated into a low salt-soluble fraction (LS), enriched with cytoplasmic (Cyt) AChE; detergent-soluble fraction (DS), enriched with membrane-associated AChE (memb); and high-salt soluble fraction (HS), enriched with “tailed” AChE, all as detailed in “Materials and methods.” (C) The discriminative antibodies used. Shown is a scheme of the AChE polypeptide, with antibody cartoons at the relative positions to which antibodies used in our study were targeted. The N19-antibody recognizes an N-terminal domain common to all variants, whereas the anti-AChE-R antibody recognizes the C-terminal domain unique for the AChE-R variant.
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