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  • Title: Rapidly induced modulation of beta-N-acetylglucosaminidase activity in pancreatic islets.
    Author: Borelli MI, Alvarez V, de Gagliardino E, Couso R, Gagliardino JJ.
    Journal: Arch Int Physiol Biochim Biophys; 1994; 102(1):9-12. PubMed ID: 7516739.
    Abstract:
    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)
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