Immunochemical Characterization of Two Activator Proteins Stimulating Enzymic Sphingomyelin Degradation in vitro Absence of One of them in a Human Gaucher Disease Variant

Christomanou, H.; Aignesberger, Annemarie; Linke, Reinhold P.

doi:10.1515/bchm3.1986.367.2.879

Cited by 151 publications

(73 citation statements)

References 23 publications

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“…Four proteins of this family, saposins A, B, C and D, are produced by partial proteolysis of a precursor protein, prosaposin [l]. Recently deficiencies of saposins C and B have been demonstrated in human genetic diseases including a variant form of Gaucher disease [2] and variants of metachromatic leukodystrophy [3], respectively. From amino acid sequence analyses, human saposin A has been shown to have two glycosylation sites to which N-linked oligosaccharides are attached [4], whereas saposins B, C and D have only one such site [l].…”

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confidence: 99%

Structural study of the oligosaccharide moieties of sphingolipid activator proteins, saposins A, C and D obtained from the spleen of a Gaucher patient

Ito

Takahashi

et al. 1993

European Journal of Biochemistry

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We have determined and compared the structures of the oligosaccharide moieties of saposin A, C and D purified from the spleen of a patient with Gaucher disease. These saposins, together with saposin B, are small glycoproteins, derived from separate domains of a single precursor, prosaposin, and are required for the lysosomal hydrolysis of various sphingolipids. The characteristic features of the oligosaccharide moieties of saposin A are (a) the predominance of a fucosylated trimannosyl core structure and (b) the occurrence of several different oligomannose‐type and N‐acetyllactosamine‐type oligosaccharides. Saposin C contains (a) a predominance of oligomannose‐type oligosaccharides and monoantennary oligosaccharides and (b) the presence of four different oligosaccharides having bisecting N‐acetylglucosamine residues (found only in this saposin). Saposin D is distinguished by the occurrence of oligomannose‐type oligosaccharides, which comprise nearly 90% of its total oligosaccharides. The possible reasons for the unique glycosylation of each saposin is discussed.

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confidence: 99%

Structural study of the oligosaccharide moieties of sphingolipid activator proteins, saposins A, C and D obtained from the spleen of a Gaucher patient

Ito

Takahashi

et al. 1993

European Journal of Biochemistry

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“…and ceroid-lipofuscinosis, 2) when the signs and symptoms are not typical for the suspected disease: adult-type gangliosidoses, and 3) when the biochemical evidence of storage and clinical histories does not coincide with the result of the in vitro enzyme assays: activator-deficient types of GM2 gangliosidosis, Gaucher disease and metachromatic leukodystrophy (2)(3)(4).…”

Section: Discussionmentioning

confidence: 99%

Ultrastructural pathology of rectum and skin biopsy specimens in lysosomal storage diseases.

Taniike

Yamano

Shimada

et al. 1990

Acta Histochem. Cytochem

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“…The antisera had ELISA titer of 1:950 and 1:900 (half-maximal A 405 of 3-fold serum dilutions on a 50-ng antigen coat) against SAP-A and SAP-C, respectively. Specificity of the antisera was assessed by ELISA, immunoblot and immunoprecipitation, and in the case of the anti-SAP-C antiserum by comparison with the rabbit anti-SAP-C antiserum described earlier (21).…”

Section: Materials-restrictionmentioning

confidence: 99%

Expression of the Three Alternative Forms of the Sphingolipid Activator Protein Precursor in Baby Hamster Kidney Cells and Functional Assays in a Cell Culture System

Henseler

Klein

Glombitza

et al. 1996

Journal of Biological Chemistry

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In order to determine the biological function of the three different SAP-B isoforms, SAP-precursor-deficient human fibroblasts were loaded with recombinant SAPprecursor proteins with or without 2-and 3-amino acid insertions, respectively, purified from the medium of the baby hamster kidney cells. They were found to stimulate at nanomolar concentrations the turnover of biosynthetically labeled ceramide, glucosylceramide, and lactosylceramide. Since the physiological function of SAP-B is to stimulate the degradation of sulfatide by arylsulfatase A (EC 3.1.6.1) and globotriaosylceramide by ␤-galactosidase (EC 3.2.1.23) loading studies with the respective exogenously labeled lipids on SAP-precursordeficient fibroblasts were performed. Addition of different purified SAP-precursors to the medium of the lipidloaded fibroblasts showed positive stimulation of the lipid degradation by all three SAP-B isoforms derived from the SAP-precursors. These findings establish that all three forms of the SAP-B can function as sulfatide/ globotriaosylceramide activator.

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Immunochemical Characterization of Two Activator Proteins Stimulating Enzymic Sphingomyelin Degradation in vitro Absence of One of them in a Human Gaucher Disease Variant

Cited by 151 publications

References 23 publications

Structural study of the oligosaccharide moieties of sphingolipid activator proteins, saposins A, C and D obtained from the spleen of a Gaucher patient

Structural study of the oligosaccharide moieties of sphingolipid activator proteins, saposins A, C and D obtained from the spleen of a Gaucher patient

Ultrastructural pathology of rectum and skin biopsy specimens in lysosomal storage diseases.

Expression of the Three Alternative Forms of the Sphingolipid Activator Protein Precursor in Baby Hamster Kidney Cells and Functional Assays in a Cell Culture System

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