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 beta -dystraglycan 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 approximate to 31 kDa beta -dystroglycan band, alpha -Dystroglycan was udetectable in most of the cell lines in which beta -dystroglycan was found as a approximate to 31 kDa species, An anomalous approximate to 31 kDa beta -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 approximate to 31 kDa beta -dystroglycan bands harbour their transmembrane segment. (C) 2000 Federation of European Biochemical Societies, Published by Elsevier Science B,V, All rights reserved.