Human Molecular Genetics, Vol 7, 115-121, Copyright © 1998 by Oxford University Press
SA Igdoura, C Gafuik, C Mertineit, F Saberi, AV Pshezhetsky, M Potier, JM Trasler and RA Gravel
Lysosomal sialidase occurs in a multienzyme complex that also contains
beta-galactosidase and cathepsin A. We previously cloned the human
lysosomal sialidase cDNA and characterized mutations in human sialidosis
patients. Here, we report the cloning and expression of the mouse lysosomal
sialidase cDNA and gene. The 1.77 kb cDNA encodes an open reading frame of
408 amino acids which shows high homology to the human lysosomal sialidase
(80%), the rat cytosolic sialidase (65%) and viral and bacterial sialidases
(50-55%). The sialidase gene is approximately 4 kb long and contains six
exons. The five introns range in size from 96 to 1200 bp. Northern blot
analysis revealed high expression of multiple sialidase transcripts in
kidney and epididymis, moderate levels in brain and spinal cord, and low
levels in adrenal, heart, liver, lung and spleen. Transient expression of
the cDNA clone in sialidase-deficient SM/J mouse fibroblasts and human
sialidosis fibroblasts restored normal levels of sialidase activities in
both cell types. Immunocytochemically expressed sialidase co-localized with
a lysosomal marker, LAMP2, confirming its lysosomal nature. Since sialidase
activity requires its association with beta-galactosidase and cathepsin A,
the expression of mouse sialidase within human sialidosis cells underlines
the structural similarity between mouse and human enzymes and suggests that
the mechanism for complex formation and function is highly conserved.
ARTICLES
Cloning of the cDNA and gene encoding mouse lysosomal sialidase and correction of sialidase deficiency in human sialidosis and mouse SM/J fibroblasts
Montreal Children's Hospital Research Institute and Department of Biology, McGill University, Montreal, Quebec, Canada.
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