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Anomalous dystroglycan in carcinoma cell lines
Author(s) -
Losasso Carmen,
Di Tommaso Francesca,
Sgambato Alessandro,
Ardito Raffaele,
Cittadini Achille,
Giardina Bruno,
Petrucci Tamara C.,
Brancaccio Andrea
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02157-8
Subject(s) - dystroglycan , alternative splicing , transmembrane protein , gene isoform , biology , microbiology and biotechnology , chemistry , extracellular matrix , laminin , receptor , biochemistry , gene
Dystroglycan is a receptor responsible for crucial interactions between extracellular matrix and cytoplasmic space. We provide the first evidence that dystroglycan is truncated. In HC11 normal murine and the 184B5 non‐tumorigenic mammary human cell lines, the expected β‐dystroglycan 43 kDa band was found but human breast T47D, BT549, MCF7, colon HT29, HCT116, SW620, prostate DU145 and cervical HeLa cancer cells expressed an anomalous ≈31 kDa β‐dystroglycan band. α‐Dystroglycan was udetectable in most of the cell lines in which β‐dystroglycan was found as a ≈31 kDa species. An anomalous ≈31 kDa β‐dystroglycan band was also observed in N ‐methyl‐ N ‐nitrosurea‐induced primary rat mammary tumours. Reverse transcriptase polymerase chain reaction experiments confirmed the absence of alternative splicing events and/or expression of eventual dystroglycan isoforms. Using protein extraction procedures at low‐ and high‐ionic strength, we demonstrated that both the 43 kDa and ≈31 kDa β‐dystroglycan bands harbour their transmembrane segment.