Literature DB >> 11758679

Are there useful biochemical markers of disease activity in lysosomal storage diseases?

B Winchester1.   

Abstract

The primary biochemical consequence of a defect in a gene encoding a functional component of the lysosomal system is disruption of the catabolism or processing of macromolecules in the lumen of the lysosome. Transport of the resulting digestion products through the lysosomal membrane may also be affected. This leads to the accumulation of specific metabolites within the lysosomes of affected cells. The nature of these storage products depends upon the functional protein affected and the cell type. The accumulation of storage products is progressive and leads to hypertrophy of the lysosomal system, the hallmark of lysosomal storage diseases (LSDs). Subsequent cell necrosis or, possibly, exocytosis results in the appearance in body fluids of the storage products and components of the lysosomes at much higher concentrations than seen in normal unaffected individuals. Measurement of these increased levels of metabolites and proteins provides disease-specific and generic biochemical markers for LSDs. Secondary changes in metabolism and cellular function may also produce characteristic changes in the levels of metabolites or proteins, which can also be used as markers of the disease process. Although the rate of appearance of these biochemical markers in an individual will depend upon the underlying mutation in the gene and on other genetic and environmental factors, it provides a good indicator of the progression of the disease. As the novel forms of treatment being developed may reverse the hypertrophy of the lysosomal system, biochemical markers could also be used to monitor the reversal of pathology and the efficacy of treatment.

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Year:  2001        PMID: 11758679     DOI: 10.1023/a:1012415706901

Source DB:  PubMed          Journal:  J Inherit Metab Dis        ISSN: 0141-8955            Impact factor:   4.982


  24 in total

1.  Characterization of lysosomal hydrolases that are elevated in Gaucher's disease.

Authors:  K D Moffitt; J P Chambers; W F Diven; R H Glew; D A Wenger; D F Farrell
Journal:  Arch Biochem Biophys       Date:  1978-09       Impact factor: 4.013

2.  Distribution of saposin proteins (sphingolipid activator proteins) in lysosomal storage and other diseases.

Authors:  S Morimoto; Y Yamamoto; J S O'Brien; Y Kishimoto
Journal:  Proc Natl Acad Sci U S A       Date:  1990-05       Impact factor: 11.205

3.  Quantification of mRNAs encoding proteins of the glycosphingolipid catabolism in mouse models of GM2 gangliosidoses and sphingolipid activator protein precursor (prosaposin) deficiency.

Authors:  A Potratz; S Hüttler; U Bierfreund; R L Proia; K Suzuki; K Sandhoff
Journal:  Biochim Biophys Acta       Date:  2000-11-15

4.  Pathologic gene expression in Gaucher disease: up-regulation of cysteine proteinases including osteoclastic cathepsin K.

Authors:  M T Moran; J P Schofield; A R Hayman; G P Shi; E Young; T M Cox
Journal:  Blood       Date:  2000-09-01       Impact factor: 22.113

5.  Diagnosis of lysosomal storage disorders: evaluation of lysosome-associated membrane protein LAMP-1 as a diagnostic marker.

Authors:  P J Meikle; D A Brooks; E M Ravenscroft; M Yan; R E Williams; A E Jaunzems; T K Chataway; L E Karageorgos; R C Davey; C D Boulter; S R Carlsson; J J Hopwood
Journal:  Clin Chem       Date:  1997-08       Impact factor: 8.327

6.  Plasma chitotriosidase activity in Gaucher disease patients who have been treated either by bone marrow transplantation or by enzyme replacement therapy with alglucerase.

Authors:  E Young; C Chatterton; A Vellodi; B Winchester
Journal:  J Inherit Metab Dis       Date:  1997-08       Impact factor: 4.982

7.  Increased excretion of a glucose-containing tetrasaccharide in the urine of a patient with glycogen storage disease type II (Pompe's disease).

Authors:  P Hallgren; G Hansson; K G Henriksson; A Häger; A Lundblad; S Svensson
Journal:  Eur J Clin Invest       Date:  1974-12-05       Impact factor: 4.686

8.  The human chitotriosidase gene. Nature of inherited enzyme deficiency.

Authors:  R G Boot; G H Renkema; M Verhoek; A Strijland; J Bliek; T M de Meulemeester; M M Mannens; J M Aerts
Journal:  J Biol Chem       Date:  1998-10-02       Impact factor: 5.157

9.  Biochemical studies on a case of feline mannosidosis.

Authors:  L J Burditt; K Chotai; S Hirani; P G Nugent; B G Winchester; W F Blakemore
Journal:  Biochem J       Date:  1980-09-01       Impact factor: 3.857

10.  Marked elevation of plasma chitotriosidase activity. A novel hallmark of Gaucher disease.

Authors:  C E Hollak; S van Weely; M H van Oers; J M Aerts
Journal:  J Clin Invest       Date:  1994-03       Impact factor: 14.808

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