Results 21 to 30 of about 1,083 (177)
A saposin deficiency model in Drosophila: Lysosomal storage, progressive neurodegeneration and sensory physiological decline [PDF]
Neurobiology of Disease, 2017 Saposin deficiency is a childhood neurodegenerative lysosomal storage disorder (LSD) that can cause premature death within three months of life.
Samantha J. Hindle +4 more
doaj +2 more sources
Journal of Biological Chemistry, 1994 Small (80-amino acid) glycoproteins or saposins are important for the in vivo function of several lysosomal hydrolases. Four saposins, A, B, C, and D, are encoded by a single locus termed prosaposin. Saposins C and A are thought to function in vivo as activators of acid beta-glucosidase.
X, Qi, T, Leonova, G A, Grabowski
exaly +3 more sources
Structural analysis of saposin C and B. Complete localization of disulfide bridges.
The Journal of biological chemistry, 1995 Saposins A, B, C, and D are a group of homologous glycoproteins derived from a single precursor, prosaposin, and apparently involved in the stimulation of the enzymatic degradation of sphingolipids in lysosomes. All saposins have six cysteine residues at similar positions.
A. M. Vaccaro +9 more
openaire +6 more sources
Altered autophagy in the mice with a deficiency of saposin A and saposin B [PDF]
Autophagy, 2013 Combined saposin A and saposin B deficiency (AB(-/-)) was created in mice by knock-in of point mutations into the saposin A and B domains of the Psap (encoding prosaposin) locus. PSAP is the precursor of saposin A, saposin B and two other members, saposin C and saposin D.
Ying, Sun, Gregory A, Grabowski
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Differential Membrane Interactions of Saposins A and C [PDF]
Journal of Biological Chemistry, 2001 Xiaoyang Qi, Gregory A Grabowski
exaly +2 more sources
Structure of saposin A lipoprotein discs [PDF]
Proceedings of the National Academy of Sciences, 2012 The saposins are small, membrane-active proteins that exist in both soluble and lipid-bound states. Saposin A has roles in sphingolipid catabolism and transport and is required for the breakdown of galactosylceramide by β-galactosylceramidase. In the absence of lipid, saposin A adopts a closed monomeric apo conformation typical of this family. To study
Konstantin, Popovic +3 more
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Saposin D: A sphingomyelinase activator [PDF]
Biochemical and Biophysical Research Communications, 1988 Saposin D, a newly discovered heat-stable, 10 kDa glycoprotein, was isolated from Gaucher spleen and purified to homogeneity. Chemical sequencing from its amino terminus demonstrated colinearity between its amino acid sequence and the deduced amino acid sequence of the fourth domain of prosaposin, the precursor of saposin proteins.
Morimoto, Satoshi +3 more
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Tissue-specific effects of saposin A and saposin B on glycosphingolipid degradation in mutant mice [PDF]
Human Molecular Genetics, 2013 Individual saposin A (A-/-) and saposin B (B-/-)-deficient mice show unique phenotypes caused by insufficient degradation of myelin-related glycosphingolipids (GSLs): galactosylceramide and galactosylsphingosine and sulfatide, respectively. To gain insight into the interrelated functions of saposins A and B, combined saposin AB-deficient mice (AB ...
Ying, Sun +10 more
openaire +2 more sources
Saposins: structure, function, distribution, and molecular genetics.
Journal of Lipid Research, 1992 Saposins A, B, C, and D are small heat-stable glycoproteins derived from a common precursor protein, prosaposin. These mature saposins, as well as prosaposin, activate several lysosomal hydrolases involved in the metabolism of various sphingolipids.
Y Kishimoto, M Hiraiwa, JS O'Brien
doaj +1 more source
Lysosomal Storage Diseases: Heterogeneous Group of Disorders [PDF]
BioImpacts, 2013 The name of lysosomal storage diseases stems from the fact that in this category of disorders specific undegraded materials are stored in the lysosomes.
David A. Wenger +2 more
doaj +1 more source