Results 21 to 30 of about 1,094 (157)

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, R. Salvioli, A. Barca, M. Tatti, R. Ciaffoni, MARAS, Bruno, R. Siciliano, F. Zappacosta, A. Amoresano, P. Pucci   +9 more
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Saposin D acting on macrophage bacteriostatic function in experimental tuberculosis infection

Инфекция и иммунитет, 2021
The protection against tuberculosis infection is largely determined by the ability of host tissue macrophages to limit the growth and spread of mycobacteria. Able to multiply within the host macrophages, mycobacteria have developed a number of protective
G. S. Shepelkova, V. V. Evstifeev, A. E. Ergeshov, V. V. Yeremeev   +3 more
doaj   +1 more source

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, John, Holyoake, Régis, Pomès, Gilbert G, Privé   +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, Martin, Brian M., Kishimoto, Yasuo, O'Brien, John S.   +3 more
openaire   +3 more sources

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, Matt, Zamzow, Huimin, Ran, Wujuan, Zhang, Brian, Quinn, Sonya, Barnes, David P, Witte, Kenneth D R, Setchell, Michael T, Williams, Charles V, Vorhees, Gregory A, Grabowski   +10 more
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Modelling saposin deficiency in Drosophila: progressive neurodegeneration, storage and physiological decline [PDF]

, 2010
Saposin deficiency is a lysosomal storage disorder (LSD) characterised by the lysosomal accumulation of sphingolipids. The disorder is caused by mutations in the prosaposin gene, which encodes 4 activator proteins: saposins A - D.
Hindle, Samantha Hindle
core   +6 more sources

Quantitative Studies on the Interaction between Saposin-like Proteins and Synthetic Lipid Membranes

Methods and Protocols, 2022
Members of the saposin-fold protein family and related proteins sharing a similar fold (saposin-like proteins; SAPLIP) are peripheral-membrane binding proteins that perform essential cellular functions. Saposins and SAPLIPs are abundant in both plant and
Suzanne I. Sandin, Eva de Alba
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, Paola Luzi, Mohammad A. Rafi   +2 more
doaj   +1 more source

Role of sphingolipids in the transport of prosaposin to the lysosomes

Journal of Lipid Research, 1999
Prosaposin is the precursor of four lysosomal saposins that promote the degradation of glycosphingolipids (GSLs) by acidic hydrolases. GSLs contain a hydrophobic ceramide moiety, which acts as a membrane anchor, and a hydrophilic oligosaccharide chain ...
Stephane Lefrancois, Lorraine Michaud, Michel Potier, Suleiman Igdoura, Carlos R. Morales   +4 more
doaj   +1 more source

Structure of human saposin A at lysosomal pH [PDF]

Acta Crystallographica Section F Structural Biology Communications, 2015
The saposins are essential cofactors for the normal lysosomal degradation of complex glycosphingolipids by acid hydrolase enzymes; defects in either saposin or hydrolase function lead to severe metabolic diseases. Saposin A (SapA) activates the enzyme β-galactocerebrosidase (GALC), which catalyzes the breakdown of β-D-galactocerebroside, the principal ...
Hill, Chris H, Read, Randy J, Deane, Janet E   +2 more
openaire   +2 more sources