Hostname: page-component-8448b6f56d-gtxcr Total loading time: 0 Render date: 2024-04-19T17:13:37.088Z Has data issue: false hasContentIssue false
  • English
  • Français

A gene (Neu-1) on chromosome 17 of the mouse affects acid α-glucosidase and codes for neuraminidase

Published online by Cambridge University Press:  14 April 2009

Josephine Peters ,
Dallas M. Swallow ,
Sandra J. Andrews  and
Lorraine Evans
Josephine Peters
Affiliation:
MRC Radiobiology Unit, Harwell, Didcot, Oxon, OX11 0RD, U.K.
Dallas M. Swallow
Affiliation:
MRC Human Biochemical Genetics Unit, Gallon Laboratory University College London, Wolfson House, 4 Stephenson Way, London NW1 2HE, U.K.
Sandra J. Andrews
Affiliation:
MRC Radiobiology Unit, Harwell, Didcot, Oxon, OX11 0RD, U.K.
Lorraine Evans
Affiliation:
MRC Human Biochemical Genetics Unit, Gallon Laboratory University College London, Wolfson House, 4 Stephenson Way, London NW1 2HE, U.K.
Rights & Permissions [Opens in a new window]

Summary

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

An electrophoretically detectable variant of acid α-glucosidase has been found in SM/J mice. This variant is attributable to excess sialylation of the enzyme and is determined by a gene, alpha-glucosidase processing, Aglp, on chromosome 17. In addition, as also reported by Potier, Lu Shun Yan & Womack (1979), SM/J mice are relatively deficient in neuraminidase and it appears that the low level of this enzyme in SM/J is determined by an autosomal codominant gene, neuraminidase-1, Neu-1. Preliminary data indicate that Neu-1 is also on chromosome 17. It seems probable that the several processing genes Apl, Aglp and Map-2 which are all closely linked on chromosome 17 are one and the same, a gene Neu-1 coding for neuraminidase.

Type
Research Article
Information
Genetics Research , Volume 38 , Issue 1 , August 1981 , pp. 47 - 55
Copyright
Copyright © Cambridge University Press 1981

References

REFERENCES

Champion, M. J. & Shows, T. B. (1977). Electrophoretic abnormalities of lysosomal enzymes in mucolipidosis fibroblast lines. American Journal of Human Genetics 29, 149–163.Google Scholar
Dizik, M. & Elliott, R. W. (1977). A gene apparently determining the extent of sialylation of lysosomal α-mannosidase in mouse liver. Biochemical Genetics 15, 31–46.CrossRefGoogle ScholarPubMed
Dizik, M. & Elliott, R. W. (1978). A second gene affecting the sialylation of lysosomal α-mannosidase in mouse liver. Biochemical Genetics 16, 247–260.CrossRefGoogle ScholarPubMed
Henthorn, P. & Daniel, W. (1978). Private communication. Mouse News Letter 59, 22.Google Scholar
Johnston, P. G. & Cattanach, B. M. (1981). Controlling elements in the mouse. IV. Evidence of non-random X-inactivation. Genetical Research. (In the Press.)CrossRefGoogle ScholarPubMed
Lallby, P. A. & Shows, T. B. (1977). Lysosomal acid phosphatase deficiency: liver specific variant in the mouse. Genetics 87, 305–317.Google Scholar
Lowden, J. A. & O'Brien, J. S. (1979). Sialidosis: a review of human neuraminidase deficiency. American Journal of Human Genetics 31, 1–18.Google ScholarPubMed
Paigen, K. (1979). Acid hydrolases as models of genetic control. Annual Review of Genetics 13, 417–466.CrossRefGoogle ScholarPubMed
Potier, M., Yan, D. Lu Shun & Womack, J. E. (1979). Neuraminidase deficiency in the mouse. FEBS Letters 108, 345–348.CrossRefGoogle ScholarPubMed
Rattazzi, M. C., Bernini, L. F., Fiorelli, G. & Mannucci, P. M. (1967). Electrophoresis of glucose-6-phosphate dehydrogenase - a new technique. Nature 213, 79–80.Google Scholar
Swallow, D. M.. Corney, G., Harris, H. & Hirschhorn, R. (1975). Acid α-glucosidase: A new polymorphism in man demonstrable by ‘affinity’ electrophoresis. Annals of Human Genetics 38, 391–406.CrossRefGoogle ScholarPubMed
Swallow, D. M., Evans, L., Stewart, G., Thomas, P. K. & Abrams, J. D. (1979). Sialidosis type I: cherry red spot-myoclonus syndrome with sialidase deficiency and altered electro-phoretic mobility of some enzymes known to be glycoproteins. II. Enzyme studies. Annals of Human Genetics 43, 27–35.CrossRefGoogle Scholar
Swallow, D. M., Gardiner, S. E., Harris, H., Arthur, E., Steel, C. M. & Evans, H. J. (1977). Lysosomal enzymes in human lymphoblastoid lines: unusual characteristics of RAJI and DAUDI. Annals of Human Genetics 41, 9–16.CrossRefGoogle ScholarPubMed
Swallow, D. M. & Harris, H. (1972). A new variant of the placental acid phosphatases: its implications regarding their subunit structures and genetical determination. Annals of Human Genetics 36, 141–152.CrossRefGoogle ScholarPubMed
Swallow, D. M., O'Brien, J. S., Hoogeveen, A. T. & Buck, D. W. (1981). Electrophoretic analysis of glycoprotein enzymes in the sialidoses and mucolipidoses. Annals of Human Genetics 44, 29–37.Google Scholar
Thomas, P. K., Abrams, J. D., Swallow, D. M. & Stewart, G. (1979). Sialidosis type I: Cherry red spot - myoclonus syndrome with sialidase deficiency and altered electrophoretic mobility of some enzymes known to be glycoproteins. Journal of Neurology, Neurosurgery and Psychiatry 42, 873–880.Google Scholar
Winter, R. M., Swallow, D. M., Baraitser, M. & Purkiss, P. (1980). Sialidosis type 2 (acid neuraminidase deficiency): clinical and biochemical features of another case. Clinical Genetics 18, 203–210.CrossRefGoogle ScholarPubMed
Wallace, M. E. (1976). Private communication. Mouse News Letter 55, 10.Google Scholar
Womack, J. E. & Eicher, E. M. (1977). Liver-specific lysosomal acid phosphatase deficiency (Apl) on mouse chromosome 17. Molecular and General Genetics 155, 315–317.CrossRefGoogle ScholarPubMed
Womack, J. E., Yan, D. Lu Shun & Potier, M. (1980). Gene for neuraminidase activity on mouse chromosome 17 near H-2: Pleiotropic effects on other hydrolases. Science. (In the Press.)Google Scholar
Womack, J. E. & Potier, M. (1979). Private communication. Mouse News Letter 61, 64.Google Scholar