Results 11 to 20 of about 1,124 (173)

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

Proceedings 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, Xiaoyang, Qi, Pansy, Tsang, Suk-Jo, Kang, Petr A, Illarionov, Petr A, Illaniorov, Gurdyal S, Besra, Jenny, Gumperz, Peter, Cresswell   +8 more
openaire   +4 more sources

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

FEBS 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, Hiraiwa, Masao, Paton, Barbara C   +2 more
openaire   +3 more sources

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

PLoS 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, Hiroaki Nabeka, Hiroyuki Wakisaka, Kana Unuma, Md Sakirul Islam Khan, Tetsuya Shimokawa, Farzana Islam, Takuya Doihara, Kimiko Yamamiya, Shouichiro Saito, Fumihiko Hamada, Seiji Matsuda   +11 more
doaj   +2 more sources

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

FEBS 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, Palmer, David N., Baumann, Marc, Haltia, Matti   +3 more
openaire   +3 more sources

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

Journal 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, Junko Matsuda, Hirokazu Fujimoto, Kunihiko Suzuki, Ineo Ishizuka   +4 more
doaj   +2 more sources

Saposin B binds and transfers phospholipids [PDF]

Journal of Lipid Research, 2006
Saposin B (Sap B) is a member of a family of four small glycoproteins, Sap A, B, C, and D. Like the other three saposins, Sap B plays a physiological role in the lysosomal degradation of sphingolipids (SLs). Although the interaction of Sap B with SLs has
Fiorella Ciaffoni, Massimo Tatti, Alessandra Boe, Rosa Salvioli, Arvan Fluharty, Sandro Sonnino, Anna Maria Vaccaro   +6 more
doaj   +5 more sources

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

Инфекция 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

Tracking of Prosaposin, a Saposin Precursor, in Rat Testis. [PDF]

J Histochem Cytochem, 2023
We tracked prosaposin (PSAP), a trophic factor, using an antibody specific to its proteolytic portion and an antibody to sortilin that traffics PSAP only to the lysosome. Immunostaining revealed that PSAP was distributed mainly on the basal side of seminiferous tubules, where many Sertoli cells and pachytene spermatocytes contained PSAP and its ...
Yamamiya K, Li X, Nabeka H, Khan S, Khan F, Wakisaka H, Saito S, Hamada F, Matsuda S.   +8 more
europepmc   +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, R. Salvioli, A. Barca, M. Tatti, R. Ciaffoni, MARAS, Bruno, R. Siciliano, F. Zappacosta, A. Amoresano, P. Pucci   +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
openaire   +2 more sources