Polycystin-1: immunoaffinity isolation and characterisation by mass spectrometry.
Polycystin-1 is a putative 460 kDa membrane protein with a unique structure and is possibly representative of a new family of proteins. Its structure suggests an involvement in cell signalling and cell-matrix interactions. The amino acid sequence of polycystin-1 has to date been predicted from its gene sequence. This, to our knowledge, is the first report of the isolation and analysis of polycystin-1 at the protein level using mass spectrometry to confirm its predicted structure. The availability of purified polycystin-1 will allow a new approach to unravelling the complexity of the cell-cell and cell-matrix interactions of this large molecule in normal cells and its perturbation in disease.
Malhas
A N
AN
Department of Biochemistry, School of Life Sciences, King's College London, London SE1 9NN, UK. ashraf.malhas@kcl.ac.uk
Abuknesha
R A
RA
Price
R G
RG
D015153:Blotting, Western; D002460:Cell Line; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D006863:Hydrogen-Ion Concentration; D013058:Mass Spectrometry / Q000379:methods*; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D015398:Signal Transduction; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D050396:TRPP Cation Channels; D014357:Trypsin / Q000378:metabolism
D011506:Proteins; D050396:TRPP Cation Channels; D014357:Trypsin