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LRPPRC encodes a leucine-rich protein that has multiple pentatricopeptide repeats (PPR).
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To investigate the impact of the OXPHOS defect in the liver, aothors analyzed the mitochondrial phenotype in mice harboring an hepatocyte-specific inactivation of Lrpprc. Loss of LRPPRC in the liver caused a generalized growth delay, and typical histological features of mitochondrial hepatopathy.
There were no significant correlations between LRP130, SIRT3 (show SIRT3 ELISA Kits), or PGC-1alpha (show PPARGC1A ELISA Kits) mRNA expression in response to acute sprint-interval training. Changes in protein expression of LRP130, SIRT3 (show SIRT3 ELISA Kits), and PGC-1alpha (show PPARGC1A ELISA Kits) were positively correlated at several time points with large effect sizes, which suggest that the regulation of these proteins may be coordinated in human skeletal muscle.
LRPPRC displays a broad and strong RNA binding capacity in vitro in contrast to SLIRP that associates only weakly with RNA.
High expression of ULK1 concomitant with high expression of LRPPRC may serve as useful markers for shorter biochemical progression (BCP)-free survival and overall survival in patients with metastatic prostate cancer (PCa) after androgen deprivation therapy (ADT).
This is the first study to report hypermethylation of LRPPRC, RAB6C, and ZNF471 in squamous cell carcinoma of the tongue
LRPPRC knock-down in mammalian cells leads to an imbalance between mitochondria-encoded and nuclear-encoded subunits of complex IV
study identifies LRPPRC as an important disease-causing gene in an early-onset, multisystem and neurological mitochondrial disease.
LRPPRC levels were reduced in muscle cells and undetectable in liver from French Canadian Leigh Syndrome patients.
LRPPRC is a transcription factor related to ABCB1 expression and highlight the importance of epigenetic regulation in CML resistance.
Downregulation of LRPPRC expression resulted in the reduced expression of Bcl-2, upregulation of Bax, and cleaved caspase-9 and caspase-3. This induces apoptosis through the mitochondria-mediated pathway in PCa cells.
Data suggest NT-Pgc-1alpha (show PPARGC1A ELISA Kits) (alternative splicing isoform of nuclear protein (show HEMGN ELISA Kits) Pgc-1alpha (show PPARGC1A ELISA Kits)) is located in mitochondrial matrix in brown adipocytes, specifically enriched at D-loop region of mitochondrial DNA at promoter region of Lrpprc (leucine-rich PPR-motif containing protein); expression of NT-Pgc-1alpha (show PPARGC1A ELISA Kits) (rather than Pgc-1alpha (show PPARGC1A ELISA Kits)) in brown adipocytes appears to induce expression of electron transport chain complex proteins.
both LRPPRC and SLIRP are required for maintaining mt-mRNA steady-state levels independent of their roles in stabilizing the other partner of the LRPPRC-SLIRP complex.
Ectopic expression of LRPPRC in the mouse liver completely interdicted non-alcoholic fatty liver disease, including inflammation.
LRPPRC deficiency in Leigh syndrome causes an ATP synthase deficiency.
LRPPRC does not directly regulate mtDNA transcription but rather acts as a post-transcriptional regulator of mammalian mtDNA expression.
Heart-specific Lrpprc disruption causes mitochondrial cardiomyopathy with drastic reduction in steady-state mitochondrial mRNA levels. LRPPRC forms an RNA-dependent protein complex needed to maintain a mitochondrial pool of non-translated mRNAs.
These data strongly suggest that LRPPRC is involved in the maturation of cytochrome c (show CYCS ELISA Kits) oxidase (COX), and is involved in stabilizing of mitochondrial mRNAs encoding COX transcripts.
LRP130 protein remodels mitochondria and stimulates fatty acid oxidation.
Our results demonstrate that LIF (show LIF ELISA Kits) signaling via the gp130/JAK (show JAK3 ELISA Kits)/STAT3 (show STAT3 ELISA Kits) pathway is required for the initiation of the astrogliosis-like reaction of retinal Muller cells after optic nerve injury.
LRP130 may function in stabilizing minisatellite DNA sequences.
This gene encodes a leucine-rich protein that has multiple pentatricopeptide repeats (PPR). The precise role of this protein is unknown but studies suggest it may play a role in cytoskeletal organization, vesicular transport, or in transcriptional regulation of both nuclear and mitochondrial genes. The protein localizes primarily to mitochondria and is predicted to have an N-terminal mitochondrial targeting sequence. Mutations in this gene are associated with the French-Canadian type of Leigh syndrome.
130 kDa leucine-rich protein
, LRP 130
, leucine-rich PPR motif-containing protein, mitochondrial
, leucine-rich PPR-motif containing
, mitochondrial leucine-rich PPR motif-containing protein
, leucine rich protein 157
, leucine-rich protein 157
, leucine rich protein LRP130