Rapidly induced modulation of beta-N-acetylglucosaminidase activity in pancreatic islets.

The aim of this work was to determine the possible rapid modulatory effect of glucose on the activity of pancreatic islet lysosomal enzymes. For this purpose, beta-N-acetylglucosaminidase and beta-galactosidase activities were measured in homogenates of isolated rat islets after a 5, 15, 30 or 60-min exposure to either 3.3 or 16.6 mM glucose. The enzyme activities were determined spectrofluorometrically by means of their respective 4-methylumbelliferyl derivatives as substrates. beta-N-acetylglucosaminidase activity measured in freshly isolated non-incubated islets was 5.482 +/- 0.281 mumol/mg protein/h at 37 degrees C. In islets incubated with 3.3 mM glucose, this activity dropped significantly after 5 min and remained almost constant until the end of the incubation period. In islets incubated with 16.6 mM glucose, beta-N-acetylglucosaminidase activity also decreased significantly at 5 min, and attained its lowest value after 15 min of incubation. After this interval, the activity began to recover and thereafter gained a value close to that measured in non-incubated islets by 60 minutes' time. Despite this ultimate recovery, the enzyme activities measured were significantly lower than those found in islets incubated with 3.3 mM glucose. beta-galactose activity in freshly isolated non-incubated islets was 0.515 +/- 0.094 mumol/mg protein/h at 37 degrees C. This value remained almost unchanged throughout the incubation period in the presence of either 3.3 or 16.6 mM glucose. These results show that beta-N-acetylglucosaminidase activity, a lysosomal hydrolase of pancreatic rat islets,--and only this enzyme--is modulated by glucose.(ABSTRACT TRUNCATED AT 250 WORDS)