Relation of Rab26 to the amylase release from rat parotid acinar cells

Summary e secretion from rat parotid acinar cells is induced by the accumulation of cAMP in response to β-adrenergic agonists as well as by the elevation of intracellular Ca2+ in response to muscarinic cholinergic stimulation. Several proteins including the low molecular weight GTP-binding protein Rab may participate in these exocytic processes. In the current studies, we investigated the role of Rab26 in the process of amylase secretion. Secretory granules were separated by centrifugation on a Percoll-sucrose density gradient into mature and immature granule fractions. Rab26 and two other type III Rab proteins, Rab3D and Rab27, were present in the mature granule membrane fraction. Also, Rab26 was absent in immature granule membrane fractions. Isoproterenol-induced amylase release from streptolysin-O-permeabilised acinar cells was inhibited by an anti-Rab26 antibody, but this antibody had no effect on the Ca2+-induced release of amylase. Finally, in the early stage of β-adrenergic stimulation, Rab26 was condensed in the secretory granule membrane. These results indicate that Rab26 is involved in the recruitment of mature granules to the plasma membrane upon β-adrenergic stimulation.