Tau protein is a member of the family of microtubule-associated proteins, which support microtubule polymerization and stability. Under pathological conditions, tau is a major constituent of neurofibrillary tangles in nerve cells of patients with Alzheimer's disease. Neurofibrillary tangles share some morphological, biochemical and immunological properties with cytoplasmic inclusions associated with other diseases, such as Mallory bodies in the livers of patients with alcoholic hepatitis and in corresponding mouse models. Recently a Mallory body component was identified that in molecular mass and isoelectric point resembles the abnormally phosphorylated tau of neurofibrillary tangles. There has been, however, so far no report describing the occurrence of tau in normal liver. We now demonstrate the expression of two tau isoforms containing three and four repeats, respectively, of the microtubule-binding domains in normal mouse liver and kidney. This finding provides evidence for a physiological role of tau in the liver and, consequently, the basis for the involvement of tau in pathological situations. (HEPATOLOGY 1994;20:1086-1089.)
Tau protein is a low molecular weight (50 to 70 kDa) member of the family of microtubule-associated proteins that is synthesized in neurons (1) and is abundant in the axonal compartment (2-5). Tau promotes the polymerization of microtubules (6, 7) and stabilizes them. The protein is a single gene product (8) that occurs in alternatively spliced isoforms with three or four repeats