Literature DB >> 2110365

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

S Morimoto1, Y Yamamoto, J S O'Brien, Y Kishimoto.   

Abstract

Saposins (A, B, C, and D) are small glycoproteins required for the hydrolysis of sphingolipids by specific lysosomal hydrolases. Concentrations of these saposins in brain, liver, and spleen from normal humans as well as patients with lysosomal storage disease were determined. A quantitative HPLC method was used for saposin A, C, and D and a stimulation assay was used for saposin B. In normal tissues, saposin D was the most abundant of the four saposins. Massive accumulations of saposins, especially saposin A (about 80-fold increase over normal), were found in brain of patients with Tay-Sachs disease or infantile Sandhoff disease. In spleen of adult patients with Gaucher disease, saposin A and D accumulations (60- and 17-fold, respectively, over normal) were higher than that of saposin C (about 16-fold over normal). Similar massive accumulations of saposins A and D were found in liver of patients with fucosidosis (about 70- and 20-fold, respectively, over normal). Saposin D was the primary saposin stored in the liver of a patient with Niemann-Pick disease (about 30-fold over normal). Moderate increases of saposins B and D were found in a patient with GM1 gangliosidosis. Normal or near normal levels of all saposins were found in patients with Krabbe disease, metachromatic leukodystrophy, Fabry disease, adrenoleukodystrophy, I-cell disease, mucopolysaccharidosis types 2 and 3B, or Jansky-Bielschowsky disease. The implications of the storage of saposins in these diseases are discussed.

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Year:  1990        PMID: 2110365      PMCID: PMC53927          DOI: 10.1073/pnas.87.9.3493

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  24 in total

1.  FORMATION OF THE MEMBRANOUS CYTOPLASMIC BODIES IN TAY-SACHS DISEASE: AN IN VITRO STUDY.

Authors:  S SAMUELS; N K GONATAS; M WEISS
Journal:  J Neuropathol Exp Neurol       Date:  1965-04       Impact factor: 3.685

2.  The activator of cerebroside-sulphatase. A model of the activation.

Authors:  G Fischer; H Jatzkewitz
Journal:  Biochim Biophys Acta       Date:  1978-01-27

3.  Requirement of an activator for the hydrolysis of sphingoglycolipids by glycosidases of human liver.

Authors:  S C Li; C C Wan; M Y Mazzotta; Y T Li
Journal:  Carbohydr Res       Date:  1974-05       Impact factor: 2.104

4.  [A cerebrosidesulfatase from swine kidney].

Authors:  E Mehl; H Jatzkewitz
Journal:  Hoppe Seylers Z Physiol Chem       Date:  1964

5.  beta-Glucosidase activator protein from bovine spleen ("coglucosidase").

Authors:  B L Berent; N S Radin
Journal:  Arch Biochem Biophys       Date:  1981-04-15       Impact factor: 4.013

6.  Neurite induction in mature cortical neurones in feline GM1-ganglioside storage disease.

Authors:  K P Purpura; H J Baker
Journal:  Nature       Date:  1977-04-07       Impact factor: 49.962

7.  Alterations in neuron morphology in feline mannosidosis. A Golgi study.

Authors:  S U Walkley; W F Blakemore; D P Purpura
Journal:  Acta Neuropathol       Date:  1981       Impact factor: 17.088

8.  AB variant of infantile GM2 gangliosidosis: deficiency of a factor necessary for stimulation of hexosaminidase A-catalyzed degradation of ganglioside GM2 and glycolipid GA2.

Authors:  E Conzelmann; K Sandhoff
Journal:  Proc Natl Acad Sci U S A       Date:  1978-08       Impact factor: 11.205

9.  Concentrations of an activator protein for sphingolipid hydrolysis in liver and brain samples from patients with lysosomal storage diseases.

Authors:  K Inui; D A Wenger
Journal:  J Clin Invest       Date:  1983-11       Impact factor: 14.808

10.  A protein activator of galactosylceramide beta-galactosidase.

Authors:  D A Wenger; M Sattler; S Roth
Journal:  Biochim Biophys Acta       Date:  1982-09-14
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  21 in total

Review 1.  Are there useful biochemical markers of disease activity in lysosomal storage diseases?

Authors:  B Winchester
Journal:  J Inherit Metab Dis       Date:  2001       Impact factor: 4.982

Review 2.  The early and late processing of lysosomal enzymes: proteolysis and compartmentation.

Authors:  A Hasilik
Journal:  Experientia       Date:  1992-02-15

3.  Effect of saposins on acid sphingomyelinase.

Authors:  M Tayama; S Soeda; Y Kishimoto; B M Martin; J W Callahan; M Hiraiwa; J S O'Brien
Journal:  Biochem J       Date:  1993-03-01       Impact factor: 3.857

4.  Synthesis and characterization of a bioactive 82-residue sphingolipid activator protein, saposin C.

Authors:  S Weiler; W Carson; Y Lee; D B Teplow; Y Kishimoto; J S O'Brien; J A Barranger; J M Tomich
Journal:  J Mol Neurosci       Date:  1993       Impact factor: 3.444

5.  Cytotoxicity and Selectivity in Skin Cancer by SapC-DOPS Nanovesicles.

Authors:  Shadi Abu-Baker; Zhengtao Chu; Ashley M Stevens; Jie Li; Xiaoyang Qi
Journal:  J Cancer Ther       Date:  2012-08

6.  Proteomic analysis of mouse models of Niemann-Pick C disease reveals alterations in the steady-state levels of lysosomal proteins within the brain.

Authors:  David E Sleat; Jennifer A Wiseman; Istvan Sohar; Mukarram El-Banna; Haiyan Zheng; Dirk F Moore; Peter Lobel
Journal:  Proteomics       Date:  2012-11-22       Impact factor: 3.984

7.  Distribution of saposins (sphingolipid activator proteins) in tissues of lysosomal storage disease patients.

Authors:  M Tayama; J S O'Brien; Y Kishimoto
Journal:  J Mol Neurosci       Date:  1992       Impact factor: 3.444

8.  Developmental and tissue-specific expression of prosaposin mRNA in murine tissues.

Authors:  Y Sun; D P Witte; G A Grabowski
Journal:  Am J Pathol       Date:  1994-12       Impact factor: 4.307

9.  Isolation of proliferation factor of immature T-cell clone in concanavalin A-stimulated splenocyte culture supernatant.

Authors:  Yasuhiro Kohama; Shinji Shinoda; Katsunobu Hagihara; Takeshi Hashimoto; Asuka Yamaguchi; Akihiro Nakamura; Takahiro Tsuchiya; Kazutake Tsujikawa; Hiroshi Yamamoto
Journal:  Immunology       Date:  2003-06       Impact factor: 7.397

10.  Replacement of alpha-galactosidase A in Fabry disease: effect on fibroblast cultures compared with biopsied tissues of treated patients.

Authors:  Jana Keslová-Veselíková; Helena Hůlková; Robert Dobrovolný; Befekadu Asfaw; Helena Poupetová; Linda Berná; Jakub Sikora; Lubor Golán; Jana Ledvinová; Milan Elleder
Journal:  Virchows Arch       Date:  2008-03-20       Impact factor: 4.064

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