Mannosidosis: Detection of the disease and of heterozygotes using serum and leucocytes

doi:10.1016/0006-291X(74)90841-9

Biochemical and Biophysical Research Communications

Volume 56, Issue 2, 23 January 1974, Pages 296-303

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Abstract

α-D-mannosidase activity in serum and leucocytes from normal individuals, patients with mannosidosis and their parents was measured at pH 4.4 and pH 6.0. When the results were expressed as total activity or specific activity at pH 4.4 in both tissues, or as a ratio of enzyme activity at the two pH conditions in serum, the disease could be diagnosed, but the heterozygotes could not be distinguished from the controls. However, all three groups could be recognised when acid α-mannosidase activity was related to total

activity in serum and leucocytes. The distribution of α-mannosidases, as separated by ion-exchange chromatography was different in each tissue. The serum profile was unique, all components having substantial “neutral” activities which are unaltered in mannosidosis and carriers.

References (12)

P.A. Öckerman
Lancet
(1967)
M. Carroll et al.
Biochem. Biophys. Res. Commun
(1972)
B. Kjellman et al.
J. Pediat
(1969)
N.E. Nordén et al.
J. Biol. Chem
(1973)
P.A. Öckerman et al.
Lancet
(1973)
I. Matsuda et al.
Clin. Chim. Acta
(1973)

There are more references available in the full text version of this article.

Cited by (29)

α-d-mannosidase forms in chicken liver
1984, International Journal of Biochemistry
- 1.
  1. Two forms (I and II) of α-d-mannosidase have been separated by ion-exchange chromatography on DEAE-cellulose from embryonic chicken liver. A third form (III), which is absent in embryos, was also separated from 4-day-old chickens.
- 2.
  2. The optimum pH of form I is at pH 5.0. Form II is named “neutral” because it shows maximal activity at pH 6.5. The optimum pH of form III is 4.5.
- 3.
  3. Forms I and III are heat-stable at 50°C for 1 hr. whereas form II is very unstable under these conditions.
- 4.
  4. Zn²⁺ and Mg²⁺have been found to increase the α-d-mannosidase activity of forms I and II. In contrast, Co²⁺ increases mannosidase I activity and inhibits form II from 18-day-old embryos.
- 5.
  5. α-Methyl-d-mannoside, $N- acetyl- d -mannosamine$ and d-mannosamine were found to be inhibitors of both forms I and II. “Neutral” mannosidase was also inhibited by chloride.
- 6.
  6. Competitive inhibition by d-mannose was also studied and K_i values are given.
α-d-Mannosidases in serum of patients with I-cell disease (ICD)
1981, Clinica Chimica Acta
The specific activity of α-d-mannosidase m serum of ICD-patients is considerably increased due to increased amounts of the component with optimal activity at pH 4.6 (acidic form). The intermediate form with pH optimum of 6.0 remains unaltered.
These conclusions were reached by using optimal conditions for differential assay of the α-d-mannosidases checked by partial separation of the components in serum by sucrose gradient centrifugation.
Plasma acid hydrolases in normal adults and children, and in patients with some lysosomal storage diseases
1978, Clinica Chimica Acta
Optimal assay conditions are described for plasma α-galactosidase, β-galactosidase, β-glucuronidase, α-mannosidase, α-glucosidase, N-acetyl-β-glucosamini-dase, a-fucosidase, N-acetyl-α-glucosaminidase, acid phosphatase and arylsulphatase A. The levels of these activities in normal adults and children, and the stabilities of the activities on storage at −20°C or 4°C, are reported. The levels of these enzymic activities in plasma from patients with Fabry, Pompe, Sanfilippo A, Sanfilippo B, Tay Sachs and Hunter diseases, GM₁-gangliosidosis and metachromatic leucodystrophy are described, and the possibility of using plasma hydrolase activities in the diagnosis of these conditions is discussed.
Abbreviated PR interval in mannosidosis
1978, The Journal of Pediatrics
Lysosomal glycosidase activities in human hair roots
1978, Clinica Chimica Acta
The levels of three lysosomal glycosidases, α-d-mannosidase, α-l-fucosidase and β-d-hexosaminidase have been determined in normal hair roots and in hair roots obtained from a patient with mannosidosis. The most active glycosidase in normal hair roots was β-d-hexosaminidase, followed by β-l-fucosidase and α-d-mannosidase. There was no α-d-mannosidase activity in the hair roots of the patient with mannosidosis. The significance of these results is discussed in relation to the detection of lysosomal storage diseases.
Comparative study on the activity, pH optimum and thermal stability of some glycosidases and acid phosphatase from pig and mule leukocytes
1978, Comparative Biochemistry and Physiology -- Part B: Biochemistry and
- 1.
  1. α-d-mannosidase, β-d-galactosidase, α-l-fucosidase, β-n-acetylgalactosaminidase, α-d-glucosidase and acid phosphatase activities were studied in circulating blood leukocytes from Sus scropha var. domestica L. (pig) and Equus asinus × caballus (mule) by spectrophotometric procedures using p-nitrophenyl derivatives as substrates and three different buffer solutions.
- 2.
  2. The highest specific activity corresponds to acid phosphatase. The specific activities of the glycosidases, all relatively close together in all cases, were low in comparison with that of phosphatase.
- 3.
  3. Generally, each of the above-mentioned enzymes shows one common peak for the pH optimum between 3.5 and 6.0, except α-d-glucosidase, which shows two peaks.
- 4.
  4. The pH optima values are generally similar in three buffer solutions employed.
- 5.
  5. Specific activities of the studied enzymes show a parallelism in leukocytes from both pig and mule. Also, this parallelism is observed in their pH optima values.
- 6.
  6. Thermal stability of α-d-mannosidase is high whereas that of acid phosphatase is low, in both materials. For other enzymes, differences in the thermal stability was observed according to their source.

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Biochemical and Biophysical Research Communications

Mannosidosis: Detection of the disease and of heterozygotes using serum and leucocytes

Abstract

Lancet

Biochem. Biophys. Res. Commun

J. Pediat

J. Biol. Chem

Lancet

Clin. Chim. Acta

α-d-mannosidase forms in chicken liver

α-d-Mannosidases in serum of patients with I-cell disease (ICD)

Plasma acid hydrolases in normal adults and children, and in patients with some lysosomal storage diseases

Abbreviated PR interval in mannosidosis

Lysosomal glycosidase activities in human hair roots

Comparative study on the activity, pH optimum and thermal stability of some glycosidases and acid phosphatase from pig and mule leukocytes