Isolation of rat liver microtubule-associated proteins. Evidence for a family of microtubule-associated proteins with molecular mass of around 200,000 which distribute widely among mammalian cells.

Heat-stable microtubule-associated proteins (MAPs) were isolated from rat liver crude extract. The most prominent species showed a molecular mass close to that of bovine adrenal 190-kDa MAP (Kotani, S., Murofushi, H., Maekawa, S., Sato, C., and Sakai, H. (1986) Eur. J. Biochem. 156, 23-29), termed rat 190-kDa MAP. Immunological studies with antiserum against the rat 190-kDa MAP showed that this MAP exists in a variety of rat cells and tissues. The characteristics of the rat 190-kDa MAP, including molecular mass, heat stability, and distribution pattern, were very similar to those of bovine adrenal 190-kDa MAP. However, one-dimensional peptide mapping revealed considerable difference, and there is little mutual immunological cross-reactivity. We also identified in mouse neuroblastoma Neuro 2a cells a MAP of around 200 kDa which is considered to be MAP4 (Parysek, L. M., Asnes, C.F., and Olmsted, J.B. (1984) J. Cell Biol. 99, 1309-1315). MAP4 was slightly immunoreactive to both anti-(rat 190-kDa MAP) antiserum and anti-(bovine 190-kDa MAP) antiserum. Taking these results together, we conclude that mammalian tissues ubiquitously contain heat-stable MAPs of 200 kDa and that these 200-kDa MAPs should be considered as species-specific homologues.