title: Identification of proteins differentially expressed in the conventional renal cell carcinoma by proteomic analysis.
abstract: Renal cell carcinoma (RCC) is one of the most malignant tumors in urology, and due to its insidious onset patients frequently have advanced disease at the time of clinical presentation. Thus, early detection is crucial in management of RCC. To identify tumor specific proteins of RCC, we employed proteomic analysis. We prepared proteins from conventional RCC and the corresponding normal kidney tissues from seven patients with conventional RCC. The expression of proteins was determined by silver stain after two-dimensional polyacrylamide gel electrophoresis (2D-PAGE). The overall protein expression patterns in the RCC and the normal kidney tissues were quite similar except some areas. Of 66 differentially expressed protein spots (p<0.05 by Student t-test), 8 different proteins from 11 spots were identified by MALDI-TOF-MS. The expression of the following proteins was repressed (p<0.05); aminoacylase-1, enoyl-CoA hydratase, aldehyde reductase, tropomyosin alpha-4 chain, agmatinase and ketohexokinase. Two proteins, vimentin and alpha-1 antitrypsin precursor, were dominantly expressed in RCC (p<0.05).
authors.affiliation: Department of Urologym, College of Medicine Gyeongsang National University, Jinju, Korea. seogee@gaechuk.gsnu.ac.kr
authors.forename: Jeong Seok
authors.initials: JS
authors.lastname: Hwa
authors.forename: Hyo Jin
authors.initials: HJ
authors.lastname: Park
authors.forename: Jae Hun
authors.initials: JH
authors.lastname: Jung
authors.forename: Sung Chul
authors.initials: SC
authors.lastname: Kam
authors.forename: Hyung Chul
authors.initials: HC
authors.lastname: Park
authors.forename: Choong Won
authors.initials: CW
authors.lastname: Kim
authors.forename: Kee Ryeon
authors.initials: KR
authors.lastname: Kang
authors.forename: Jea Seog
authors.initials: JS
authors.lastname: Hyun
authors.forename: Ky Hyun
authors.initials: KH
authors.lastname: Chung
mesh_terms: D000368:Aged; D000449:Aldehyde Reductase / Q000032:analysis; D000581:Amidohydrolases / Q000032:analysis; D002292:Carcinoma, Renal Cell / Q000378:metabolism* / Q000473:pathology; D015180:Electrophoresis, Gel, Two-Dimensional; D004746:Enoyl-CoA Hydratase / Q000032:analysis; D005260:Female; D005631:Fructokinases / Q000032:analysis; D006801:Humans; D007680:Kidney Neoplasms / Q000378:metabolism* / Q000473:pathology; D008297:Male; D008875:Middle Aged; D020543:Proteome / Q000032:analysis*; D040901:Proteomics / Q000379:methods*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014335:Tropomyosin / Q000032:analysis; D014512:Ureohydrolases / Q000032:analysis; D014746:Vimentin / Q000032:analysis; D000515:alpha 1-Antitrypsin / Q000032:analysis
chemical_list: D020543:Proteome; D014335:Tropomyosin; D014746:Vimentin; D000515:alpha 1-Antitrypsin; D000449:Aldehyde Reductase; D005631:Fructokinases; C021475:ketohexokinase; D000581:Amidohydrolases; C019672:aminoacylase I; D014512:Ureohydrolases; C498226:AGMAT protein, human; C019625:agmatinase; D004746:Enoyl-CoA Hydratase