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. 2002 Oct 1;21(19):5088–5096. doi: 10.1093/emboj/cdf525

Table I. Partial list of the proteins displaying >2-fold expression differences.

Category Protein namea L [Myc(–)]: H [Myc(+)] ratiob nb Notes Reference
Adhesion CD166/HDL-R L > H      
  ICAM-1 1:0.21 1    
  N-CAM 140 1:0.25 1   Guo et al. (2000)
  integrinβ1 1:0.40 ± 0.07 4    
  PINCH 1:0.37 ± 0.10 3 Integrin signaling Guo et al. (2000)
  ESL-1 1:0.37 ± 0.09 16 E-selectin ligand 1  
  LAMP1 1:0.45 1 Presents carbohydrate ligand to selectin Guo et al. (2000)
Rho pathway Rho A 1:0.49 ± 0.04 5 Induces the formation of actin stress fibers and focal adhesions  
  CDC42 1:0.48 ± 0.04 2 Induces the formation of actin stress fibers and focal adhesions  
  Rok α 1:0.23 ± 0.11 3 Induces the formation of actin stress fibers and focal adhesions  
Actin network α-actin 1:0.21 ± 0.04 3    
  β-actin 1:0.33 ± 0.06 11    
  cofilin 1:0.48 ± 0.08 11 Actin binding  
  profilin 1:0.46 ± 0.07 9 Actin binding  
  calponin 1:0.24 1 Actin/TPM/CaM binding  
  transgelin2 1:0.22 ± 0.06 7 Actin crosslinking/calponin family  
  t-plastin 1:0.21 ± 0.10 3 Actin bundling  
  sid23p 1:0.49 ± 0.03 9 Actin depolymerization factor  
  f-actin capping protein β 1:0.26 ± 0.05 8    
  Eplin α 1:0.30 1 Epithelial protein lost in neoplasia, localizes to filamentous actin and suppresses proliferation when overexpressed  
  ABP-280 1:0.18 ± 0.02 2 Endothelial actin binding protein  
  α-actinin 1 1:0.34 ± 0.09 11 Actin binding  
  α-actinin 4 1:0.40 ± 0.08 3 Actin binding  
  α-1 catenin 1:0.43 ± 0.03 2    
  β catenin 1:0.39 ± 0.11 4    
  talin 1:0.38 ± 0.08 16 Involved in connections of major cytoskeletal structures to the plasma membrane  
Protein synthesis 40S/60S ribosomal proteins (20 subunits) 1:2–3     Coller et al. (2000); Guo et al. (2000); Boon et al. (2001); Neiman et al. (2001); Schuhmacher et al. (2001)
  eIF2B δ 1:2.01 ± 0.26 2 Translation  
  DEAD box RNA helicase P47 1:3.23 ± 0.10 2 RNA helicase  
  DDX5 1:2.11 ± 0.03 8 RNA helicase  
  DDX17 1:2.56 ± 0.00 2 RNA helicase  
  DDX21 1:5.56 ± 0.00 2 RNA helicase  
  fibrillarin 1:3.64 ± 0.70 2 Ribosome biogenesis Coller et al. (2000)
  Nop56 1:2.56 1 rRNA processing and assembly  
  Nop58 1:4.03 ± 0.58 3 rRNA processing and assembly  
  Bop1 (block of proliferation 1) 1:3.13 1 rRNA processing and assembly  
Protein degradation Asn endopeptidose (legumain) 1:0.27 ± 0.00 3    
  aminopeptidase PILS L > H      
  Niban (calpain-like) 1:0.20 1    
  calpain 2 1:0.42 ± 0.07 2    
  calpain regulatory subunit 1:0.31 ± 0.00 2    
  cathepsin B 1:0.27 ± 0.06 7    
  cathepsin D 1:0.26 ± 0.00 2    
  cathepsin L 1:0.26 1    
  endooligopeptidase 1:0.29 ± 0.05 2    
  prothrombin L > H      
Metabolism Fatty acid synthase 1:2.99 ± 0.62 6   Schuhmacher et al. (2001)
  adenylate kinase 2 1:2.00 1 AMP + ATP → 2ADP  
  cad* 1:2.13 1 First, second and third steps of pyrimidine biosynthesis Schuhmacher et al. (2001)
  amidophosphoribosyl transferase (Pur 1) 1:9.10 1 First step of purine biosynthesis  
  adenosine 3 1:2.06 ± 0.06 2 Second, third and fifth steps of purine biosynthesis  
  Ade 2 (Pur 6) 1:2.45 ± 1.29 13 Sixth and seventh steps of purine biosynthesis  
  Ser hydroxymethyl transferase 1:3.23 1 Key enzyme in the biosynthesis of purines, lipids, hormones and other components  
  phosphoserine aminotransferase 1:5.56 ± 0.00 2 Biosynthesis of Ser and pyridoxine  
  Asn tRNA synthetase 1:2.04 1    
  ANT2 1:3.35 ± 0.67 4 Mitochondrial ATP translocase Guo et al. (2000)
Other Myc targets Ref-1/Ape 1:6.11 ± 0.79 3 Redox factor-1/apurinic-apyrimidic endonuclease Guo et al. (2000)
  MIF 1:2.37 ± 0.29 5 Macrophage migration inhibitory factor Guo et al. (2000)
  hsp60* 1:4.05 ± 1.13 9   Coller et al. (2000); Guo et al. (2000); Boon et al. (2001); Neiman et al. (2001)
  Tropomyosin α 1:0.26 ± 0.10 3   Coller et al. (2000); Guo et al. (2000)

aPreviously proposed direct Myc targets are marked with an asterisk. The proteins that were also identified by the previous microarray analyses are in bold and the relevant references are cited.

bThe ratio of light ICAT™ reagent-labeled peptide (L) [derived from Myc(–) cells] and heavy ICAT™ reagent-labeled peptide (H) [derived from Myc(+) cells] is shown together with the standard deviation based on the number of independent peptides (n) identified and quantified. For proteins that displayed obvious expression differences, but were difficult to quantify, the ratio is marked L < H or L > H.

The complete list of proteins displaying >2-fold expression differences can be found in the Supplementary data.