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LRPPRC encodes a leucine-rich protein that has multiple pentatricopeptide repeats (PPR). Additionally we are shipping LRPPRC Antibodies (36) and LRPPRC Kits (7) and many more products for this protein.
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There were no significant correlations between LRP130, SIRT3, or PGC-1alpha mRNA expression in response to acute sprint-interval training. Changes in protein expression of LRP130, SIRT3, and PGC-1alpha 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 (show ULK1 Proteins) concomitant with high expression of LRPPRC may serve as useful markers for shorter biochemical progression (BCP (show OPN1SW Proteins))-free survival and overall survival in patients with metastatic prostate cancer (PCa (show FLVCR1 Proteins)) 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 (show BCL2 Proteins), upregulation of Bax (show BAX Proteins), and cleaved caspase-9 (show CASP9 Proteins) and caspase-3 (show CASP3 Proteins). This induces apoptosis through the mitochondria-mediated pathway in PCa (show FLVCR1 Proteins) cells.
LRPPRC functions as a checkpoint protein that prevents mitochondria from autophagy degradation and impact tumorigenesis.
Data suggest NT-Pgc-1alpha (alternative splicing isoform of nuclear protein Pgc-1alpha) 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 (rather than Pgc-1alpha) 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 Proteins) oxidase (COX (show CPOX Proteins)), and is involved in stabilizing of mitochondrial mRNAs encoding COX (show CPOX Proteins) transcripts.
LRP130 protein remodels mitochondria and stimulates fatty acid oxidation.
Our results demonstrate that LIF (show LIF Proteins) signaling via the gp130/JAK (show JAK3 Proteins)/STAT3 (show STAT3 Proteins) 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