Prosaposin and its receptors GRP37 and GPR37L1 show increased immunoreactivity in the facial nucleus following facial nerve transection. [PDF]
Neurotrophic factor prosaposin (PS) is a precursor for saposins A, B, C, and D, which are activators for specific sphingolipid hydrolases in lysosomes. Both saposins and PS are widely contained in various tissues.
Joji Kunihiro +11 more
doaj +3 more sources
Saposin B is the dominant saposin that facilitates lipid binding to human CD1d molecules [PDF]
CD1d molecules bind lipid antigens in the endocytic pathway, and access to the pathway is important for the development of CD1d-restricted natural killer T (NKT) cells. Saposins, derived from a common precursor, prosaposin, are small, heat-stable lysosomal glycoproteins required for lysosomal degradation of sphingolipids.
Weiming, Yuan +8 more
openaire +4 more sources
A Tetrameric Assembly of Saposin A: Increasing Structural Diversity in Lipid Transfer Proteins
Saposins are lipid transfer proteins required for the degradation of sphingolipids in the lysosome. These small proteins bind lipids by transitioning from a closed, monomeric state to an open conformation exposing a hydrophobic surface that binds and ...
Maria Shamin +3 more
doaj +2 more sources
Effect of saposins on acid sphingomyelinase [PDF]
The effect of saposins (A, B, C and D) on acid sphingomyelinase activity was determined using a crude human kidney sphingomyelinase preparation and a purified sphingomyelinase preparation from human placenta. Saposin D stimulated the activity of the crude enzyme by increasing its apparent Km and Vmax. values for sphingomyelin hydrolysis.
Yasuo Kishimoto +2 more
exaly +3 more sources
SAPOSIN-LIKE PROTEINS IN ANTI-INFECTIOUS IMMUNE RESPONSE
. Besides the multiple hydrolytic enzymes, lysosomes are equipped with proteins apt to activate sphyngo-lipids — saposins (SAP). SAP belong to a broad and diverse family of moderate-size (~80 AA) saposin-like proteins (SAPLIP) containing specific domains
V. V. Yeremeev, A. S. Apt
doaj +3 more sources
Sphingolipid activator proteins (saposins A, B, C, and D) are derived from a common precursor protein (prosaposin) and specifically activate in vivo degradation of glycolipids with short carbohydrate chains.
Keiko Tadano-Aritomi +4 more
doaj +3 more sources
Saposins (sap) A and C activate the degradation of galactosylsphingosine
As previously shown for [3H‐galactosyl]ceramide, the breakdown of [3H‐galactosyl]sphingosine was reduced in prosaposin‐deficient skin fibroblast homogenates. Galactosylsphingosine hydrolysis was also deficient in cell homogenates from Krabbe's disease (β‐galactocerebrosidase‐deficient) patients, but not acid β‐galactosidase‐deficient patients. Moreover,
Harzer, Klaus +2 more
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Saposin D acting on macrophage bacteriostatic function in experimental tuberculosis infection
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 +3 more
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Storage of saposins A and D in infantile neuronal ceroid‐lipofuscinosis
We have isolated storage cytosomes from brain tissue of patients with infantile neuronal ceroid‐lipofuscinosis. The purified storage bodies were subjected to compositional analysis which revealed a high content of proteins, accounting for 43% of dry weight. Saposins A and D, also known as sphingolipid activator proteins (SAPs), were shown to constitute
Tyynelä, Jaana +3 more
openaire +3 more sources
Temporal gene expression profiling reveals CEBPD as a candidate regulator of brain disease in prosaposin deficient mice [PDF]
Background Prosaposin encodes, in tandem, four small acidic activator proteins (saposins) with specificities for glycosphingolipid (GSL) hydrolases in lysosomes.
Ran Huimin +9 more
doaj +2 more sources

