Results 11 to 20 of about 1,094 (157)

Saposin B is the dominant saposin that facilitates lipid binding to human CD1d molecules [PDF]

open access: yesProceedings of the National Academy of Sciences, 2007
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

Prosaposin: A Multifaceted Protein Orchestrating Biological Processes and Diseases [PDF]

open access: yesCells
Prosaposin (PSAP), a multifunctional protein, plays a central role in various biological processes and diseases. It is the precursor of lysosomal activating protein, which is important for lipid metabolism and glucose metabolism.
Xin Li, Liang Guo
doaj   +2 more sources

Accumulation of prosaposin and progranulin around the subfornical organ induces polydipsia in SAP-D-deficient mice [PDF]

open access: yesBiochemistry and Biophysics Reports
Prosaposin (PSAP), a precursor of saposins, is essential for lysosomal hydrolysis of sphingolipids. It binds with progranulin (PGRN) and transports from the Golgi to lysosomes, where it is processed into saposins.
Harumi Hisaki   +9 more
doaj   +2 more sources

Prosaposin/Saposin Expression in the Developing Rat Olfactory and Vomeronasal Epithelia [PDF]

open access: yesJournal of Developmental Biology
Prosaposin is a glycoprotein widely conserved in vertebrates, and it acts as a precursor for saposins that accelerate hydrolysis in lysosomes or acts as a neurotrophic factor without being processed into saposins.
Kai Kitamura   +5 more
doaj   +2 more sources

Prosaposin and its receptors GRP37 and GPR37L1 show increased immunoreactivity in the facial nucleus following facial nerve transection.

open access: yesPLoS ONE, 2020
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   +2 more sources

Seminolipid and its precursor/degradative product, galactosylalkylacylglycerol, in the testis of saposin A- and prosaposin-deficient mice [PDF]

open access: yesJournal of Lipid Research, 2003
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   +2 more sources

Saposins (sap) A and C activate the degradation of galactosylsphingosine [PDF]

open access: yesFEBS Letters, 2001
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
openaire   +3 more sources

SAPOSIN-LIKE PROTEINS IN ANTI-INFECTIOUS IMMUNE RESPONSE [PDF]

open access: yesИнфекция и иммунитет, 2014
. 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   +2 more sources

Storage of saposins A and D in infantile neuronal ceroid‐lipofuscinosis [PDF]

open access: yesFEBS Letters, 1993
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

Deficiency of Glucocerebrosidase Activity beyond Gaucher Disease: PSAP and LIMP-2 Dysfunctions [PDF]

open access: yesInt J Mol Sci
Glucocerebrosidase (GCase) is a lysosomal enzyme that catalyzes the breakdown of glucosylceramide in the presence of its activator saposin C (SapC). SapC arises from the proteolytical cleavage of prosaposin (encoded by PSAP gene), which gives rise to ...
Dardis A.   +9 more
core   +2 more sources

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