Decreased serum β-D-mannosidase activity in diabetic patients, in comparison with other glycosidases

Bernard, M.; Brochet, Christine; Percheron, F

doi:10.1016/0009-8981(85)90188-3

Cited by 6 publications

(3 citation statements)

References 7 publications

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“…The greatest increase over control occurred at 8 weeks of the disease. Our results confirm and extend another report which also showed increased plasma lysosomal enzyme activity in streptozotocin diabetic rats (24) andhumans (2,12). The pathophysiological significance of the increased blood activities of lysosomal enzymes is not well understood; however, it has previously been thought that these enzymes may originate from liver (24) and kidney (7).…”

Section: Discussionsupporting

confidence: 94%

“…Kuo et al (9) have reported similar results, again in the genetically diabetic mouse, examining the lysosomal protease cathepsin D. The purpose of the present study was to extend these findings and further characterize the nature of lysosomal enzyme alterations in a model of Type I diabetes. We have chosen t(~ examine cardiac lysosomal enzyme changes in streptozotocin-induced diabetes in rats since previous investigators (24) have shown similar qualitative changes in serum enzyme activities in this diabetic model and in diabetic humans (2,12). This is not the case with genetically diabetic mice (24) which have plasma lysosomal enzyme activities which are qualitatively opposite from those observed in human diabetics.…”

Section: Introductionmentioning

confidence: 87%

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Alterations in heart and serum lysosomal activities in streptozotocin-induced diabetes

1987

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Alterations in the cardiac tissue and serum acid hydrolase activities were studied in chronic streptozotocin-induced diabetes in rats. No changes were observed in total cardiac tissue homogenate lysosomal enzyme activities at 4 weeks of diabetes but there were significant alterations in the distribution of selected enzymes. Significant decreases in nonsedimentable beta-N-acetylglucosaminidase (NAG) and beta-galactosidase (Gal) activities were observed at 4 weeks of diabetes. At 8 weeks of the disease, decreased activities of NAG and Gal were observed in heart homogenates but no changes were apparent in alpha-mannosidase (Man) or acid phosphatase activities. Nonsedimentable activities of NAG and both sedimentable and nonsedimentable activities of Gal were decreased at 8 weeks. At 16 weeks of the diabetic condition, increased activities of NAG, Gal and acid phosphatase were observed. This increase at 16 weeks of the disease was due to an increase in sedimentable enzyme activity. At all times of diabetes, serum enzyme activities were significantly increased. Insulin treatment reversed all of the observed changes in tissue homogenates, but serum levels were not completely reversed. These results suggest that cardiac lysosomal hydrolases are probably only involved in the later stages of the diabetic cardiomyopathy when extensive ultrastructural derangements are evident. The present evidence also suggests that the heart may be a source of serum hydrolase activities.

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Section: Discussionsupporting

confidence: 94%

Section: Introductionmentioning

confidence: 87%

Alterations in heart and serum lysosomal activities in streptozotocin-induced diabetes

1987

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“…Some likely preserved features of the catalytic domains were deduced, despite the low levels of sequence identity. Another observed pathological variation of the enzyme, which manifests itself in a signi®cantly decreased serum activity in 64 diabetic patients, remains to be investigated (Bernard et al, 1985).…”

Section: Introductionmentioning

confidence: 97%

Crystallization and preliminary X-ray study of β-mannosidase fromTrichoderma reesei

Aparício

Eneiskaya

Kulminskaya

et al. 2000

Acta Crystallogr D Biol Cryst

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Hereditary fructose intolerance mimicking a biochemical phenotype of mucolipidosis: A review of the literature of secondary causes of lysosomal enzyme activity elevation in serum

Ferreira

Devaney

Hofherr

et al. 2016

American J of Med Genetics Pt A

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We describe a patient with failure to thrive, hepatomegaly, liver dysfunction, and elevation of multiple plasma lysosomal enzyme activities mimicking mucolipidosis II or III, in whom a diagnosis of hereditary fructose intolerance (HFI) was ultimately obtained. She presented before introduction of solid foods, given her consumption of a fructose-containing infant formula. We present the most extensive panel of lysosomal enzyme activities reported to date in a patient with HFI, and propose that multiple enzyme elevations in plasma, especially when in conjunction with a normal plasma α-mannosidase activity, should elicit a differential diagnosis of HFI. We also performed a review of the literature on the different etiologies of elevated lysosomal enzyme activities in serum or plasma. © 2016 Wiley Periodicals, Inc.

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Decreased serum β-D-mannosidase activity in diabetic patients, in comparison with other glycosidases

Cited by 6 publications

References 7 publications

Alterations in heart and serum lysosomal activities in streptozotocin-induced diabetes

Alterations in heart and serum lysosomal activities in streptozotocin-induced diabetes

Crystallization and preliminary X-ray study of β-mannosidase fromTrichoderma reesei

Hereditary fructose intolerance mimicking a biochemical phenotype of mucolipidosis: A review of the literature of secondary causes of lysosomal enzyme activity elevation in serum

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