Tumour-related enzyme alterations in the clear cell type of human renal cell carcinoma identified by two-dimensional gel electrophoresis.
To identify tumour-related enzyme alterations we have used 2D-gels to analyse the proteome from dissected malignant and benign kidney areas from patients with clear-cell-type renal carcinoma. The expression of 12 proteins was diminished in tumour. Four proteins were characterized by mass spectrometry and were identified as enoyl-CoA hydratase, alpha-glycerol-3-phosphate dehydrogenase, aldehyde dehydrogenase 1 and aminoacylase-I.
Balabanov
S
S
Department of Medical Biochemistry and Molecularbiology, University of Greifswald, Germany.
Zimmermann
U
U
Protzel
C
C
Scharf
C
C
Klebingat
K J
KJ
Walther
R
R
D000444:Aldehyde Dehydrogenase / Q000378:metabolism*; D000581:Amidohydrolases / Q000378:metabolism*; D001483:Base Sequence; D002292:Carcinoma, Renal Cell / Q000201:enzymology* / Q000473:pathology; D017931:DNA Primers; D015180:Electrophoresis, Gel, Two-Dimensional; D004746:Enoyl-CoA Hydratase / Q000378:metabolism*; D005993:Glycerolphosphate Dehydrogenase / Q000378:metabolism*; D006801:Humans; D007680:Kidney Neoplasms / Q000201:enzymology* / Q000473:pathology; D010449:Peptide Mapping
D017931:DNA Primers; D005993:Glycerolphosphate Dehydrogenase; D000444:Aldehyde Dehydrogenase; D000581:Amidohydrolases; C019672:aminoacylase I; D004746:Enoyl-CoA Hydratase