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Extracellular and transmembrane region of a podocalyxin‐like protein 1 fragment identified from colon cancer cell lines
Author(s) -
Ito Tetsuo,
Maki Noboru,
Hazeki Osamu,
Sasaki Kazuki,
Nekooki Munenori
Publication year - 2007
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1016/j.cellbi.2007.06.017
Subject(s) - transmembrane protein , podocalyxin , extracellular , proteolysis , chemistry , cell culture , microbiology and biotechnology , cell , biology , biochemistry , podocyte , enzyme , receptor , genetics , proteinuria , kidney , endocrinology
Regulated intramembrane proteolysis of membrane proteins has been shown to play an important role in cell differentiation and in the pathogenesis of diseases. The aim of the present study was to identify novel peptides generated by intramembrane proteolysis. The peptides were identified in serum‐free cultured (SFC) media from various cell lines by surface‐enhanced laser desorption/ionization time‐of‐flight mass spectrometry (SELDI‐TOF‐MS). A 2315‐Da peptide found only in medium from SFC colon cancer cell lines was identified and shown to consist of a portion of both the extracellular and transmembrane regions of human podocalyxin‐like 1. This protein fragment was not found in lung or pancreatic cancer cell lines by immunoprecipitation‐SELDI tests using an antibody specific to this fragment, suggesting that this human podocalyxin‐like protein 1 fragment may be unique to colon cancer cell lines.