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We (1) analyzed the structural basis of the fold and the classification of SCP2 domains; (2) identified structure-determined sequence features; (3) compared the lipid binding cavity of SCP2 and other lipid binding proteins; (4) surveyed proposed mechanisms of SCP2 mediated lipid transfer between membranes; and (5) uncovered a possible new function of the SCP2 domain as a protein-protein recognition device.
imported protein sterol carrier protein 2 (SCP2) occupies only a subregion of larger peroxisomes, highlighting the heterogeneous distribution of proteins even within the peroxisome.
Mice harboring a deletion of the Scp2 locus present a modulated diurnal accumulation of lipids in the liver and a perturbed activation of several signaling pathways including PPARalpha (show PPARA ELISA Kits), SREBP, LRH-1 (show NR5A2 ELISA Kits), TORC1 (show CRTC1 ELISA Kits) and its upstream regulators.
We conclude that SCP-2 is a low affinity binding protein for arachidonylethanolamine that can facilitate its cellular uptake but does not contribute significantly to intracellular sequestration of AEA.
The Peroxisomal targeting signal 1 in Scp2 is autonomous and is essential for binding to pex5 (show PEX5 ELISA Kits).
cellular SCP-2 not only binds and translocates cholesterol but also cholesterol hydroperoxides, thus expanding their redox toxicity and signaling ranges under oxidative stress conditions
Statistical analysis indicated that six genes, NFATC2, SCP2, CACNA1C, TCRA, POLE, and FAM3D, were associated with narcolepsy.
data for the first time showed that while the N-terminal membrane binding domain of SCP(2) was itself inactive in mediating intermembrane sterol transfer, it nevertheless potentiated the ability of SCP(2) to enhance sterol transfer
SCP2 in the cellular defense against oxidative damage and found that a fluorescent fatty acid analog bound to SCP2 is protected against H2O2/Cu2+-induced oxidative damage
Overexpression of human SCP-2 in murine fibroblasts significantly alters the sterol dynamics of caveolae/lipid rafts, but not nonlipid raft domains, to facilitate retention of cholesterol within the cell.
Thus, the loss of Scp-2/Scp-x contributed to a sex-dependent hepatic accumulation of dietary phytol and BCFA.
Individually ablating SCPx or SCP2/SCPx elicited concomitant upregulation of L-FABP (show FABP1 ELISA Kits).
Lack of a significant decrease in the flux of HDL-[(3)H]CE to biliary FC or bile acids in FABP1(-/-) mice indicates the likely compensation of its function by an as yet unidentified mechanism. Taken together, these studies demonstrate that FABP1 and SCP2 facilitate the preferential movement of HDL-CEs to bile for final elimination
Sterol Carrier Protein-2, a Nonspecific Lipid-Transfer Protein, in Intracellular Cholesterol Trafficking in Testicular Leydig Cells
L-FABP (show FABP1 ELISA Kits) was more important in hepatic retention of bile acids, while SCP-2/SCP-x more broadly affected biliary bile acid and phospholipid levels.
Loss of L-FABP (show FABP1 ELISA Kits) and SCP-2 (show CRISP3 ELISA Kits), or both induces hepatic lipid accumulation in female mice and mimics non-alcoholic fatty liver disease.
CTDSP2 induces p21(Cip1/Waf1 (show CDKN1A ELISA Kits)) through increasing the activity of Ras.
SCP-2/SCP-x may function more in formation and biliary secretion of bile acid, with less impact on hepatic uptake or biliary secretion of HDL (show HSD11B1 ELISA Kits)-cholesterol
liver fatty acid-binding protein, the single most prevalent hepatic cytosolic protein that binds cholesterol, was upregulated twofold in SCP-2 (show CRISP3 ELISA Kits) null hepatocytes
SCP-2 expression plays a significant role in HDL-mediated cholesterol efflux by regulating the size of rapid vs. slow cholesterol efflux pools and/or eliciting concomitant upregulation of L-FABP in cultured primary hepatocytes.
Knockdown of scp2 did not interfere with the patterning of the kidney along its proximo-distal axis, but dramatically decreased the size of the kidney, in particular the proximal tubules.
By trafficking cholesterol hydroperoxides and phospholipid hydroperoxides in addition to parent lipids, SCP2 may exacerbate cell injury under oxidative stress conditions. [sterol carrier protein 2, SCP2, nonspecific lipid transfer protein]
Arabidopsis SCP-2 is localised to peroxisomes and showed in vitro transfer activity of BODIPY-phosphatidylcholine (show SGMS1 ELISA Kits) (BODIPY-PC) from donor membranes to acceptor membranes.
This gene encodes two proteins (SCPx) and sterol carrier protein 2 (SCP2), as a result of transcription initiation from 2 independently regulated promoters. The transcript initiated from the proximal promoter encodes the longer SCPx protein, and the transcript initiated from the distal promoter encodes the shorter SCP2 protein, with the 2 proteins sharing a common C-terminus. Evidence suggests that the SCPx protein is a peroxisome-associated thiolase that is involved in the oxidation of branched chain fatty acids, while the SCP2 protein is thought to be an intracellular lipid transfer protein. This gene is highly expressed in organs involved in lipid metabolism, and may play a role in Zellweger syndrome, in which cells are deficient in peroxisomes and have impaired bile acid synthesis. Alternative splicing of this gene produces multiple transcript variants, some encoding different isoforms.
non-specific lipid-transfer protein
, propanoyl-CoA C-acyltransferase
, sterol carrier protein X
, carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2
, nuclear LIM interactor-interacting factor 2 (NLI-interacting factor 2) (Protein OS-4)
, small C-terminal domain phosphatase 2
, nonspecific lipid transfer protein
, Sterol carrier protein 2, liver
, sterol carrier protein 2
, sterol carrier protein-2
, SCP2 (STEROL CARRIER PROTEIN 2); oxidoreductase/ sterol carrier
, allergen Zea m 14
, sterol carrier protein 2, liver