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Leucine proline-enriched proteoglycan

LEPRE1, P3H1, prolyl 3-hydroxylase 1, Growth Suppressor
This gene encodes an enzyme that is a member of the collagen prolyl hydroxylase family. These enzymes are localized to the endoplasmic reticulum and their activity is required for proper collagen synthesis and assembly. Mutations in this gene are associated with osteogenesis imperfecta type VIII. Three alternatively spliced transcript variants encoding different isoforms have been described. Other variants may exist, but their biological validity has not been determined. [provided by RefSeq, Aug 2011] (from NCBI)
Top mentioned proteins: cyclophilin B, COL1A1, HAD, FKBP65, fibrillin-1
Papers on LEPRE1
Proteomic analysis reveals novel common genes modulated in both replicative and stress-induced senescence.
Faraonio et al., Napoli, Italy. In J Proteomics, Nov 2015
We also performed functional studies by silencing nine of these genes in young cells, which demonstrated that RNA interference-mediated knockdown of LEPRE1, LIMA1/EPLIN, MAGOHA and MAGOHB induces a premature senescent phenotype in IMR90 cells.
Growth suppressor lingerer regulates bantam microRNA to restrict organ size.
Zhang et al., Shanghai, China. In J Mol Cell Biol, Oct 2015
Here, we identify Lingerer (Lig) as a growth suppressor using RNAi modifying screen in Drosophila melanogaster.
Bulbous epiphysis and popcorn calcification as related to growth plate differentiation in osteogenesis imperfecta.
Shapiro et al., Baltimore, United States. In Clin Cases Miner Bone Metab, May 2015
METHODS: Molecular analysis was performed for COL1A1, COL1A2, LEPRE1 and WNT1 genes.
Post-translationally abnormal collagens of prolyl 3-hydroxylase-2 null mice offer a pathobiological mechanism for the high myopia linked to human LEPREL1 mutations.
Eyre et al., Seattle, United States. In J Biol Chem, Apr 2015
P3H2 is a member of a family of genes that includes three isoenzymes of prolyl 3-hydroxylase (P3H), P3H1, P3H2, and P3H3.
Development of a high-throughput resequencing array for the detection of pathogenic mutations in osteogenesis imperfecta.
Han et al., China. In Plos One, 2014
The mutations in this disorder have been widely reported to be on various exonal hotspots of the candidate genes, including COL1A1, COL1A2, CRTAP, LEPRE1, and FKBP10, thus creating a great demand for precise genetic tests.
The Human IL-22 Receptor Is Regulated through the Action of the Novel E3 Ligase Subunit FBXW12, Which Functions as an Epithelial Growth Suppressor.
Weathington et al., Washington, D.C., United States. In J Immunol Res, 2014
Interleukin- (IL-) 22 signaling is protective in animal models of pneumonia and bacteremia by Klebsiella pneumoniae and mediates tissue recovery from influenza and Staph aureus infection.
Mutational characterization of the P3H1/CRTAP/CypB complex in recessive osteogenesis imperfecta.
Paula et al., Vitória, Brazil. In Genet Mol Res, 2014
The LEPRE1, CRTAP, and PPIB genes encode proteins that form the P3H1/CRTAP/CypB complex, which is responsible for posttranslational modifications of type I collagen.
What is new in genetics and osteogenesis imperfecta classification?
Zabel et al., Belo Horizonte, Brazil. In J Pediatr (rio J), 2014
After 2006, mutations were identified in the CRTAP, FKBP10, LEPRE1, PLOD2, PPIB, SERPINF1, SERPINH1, SP7, WNT1, BMP1, and TMEM38B genes, associated with recessive OI and mutation in the IFITM5 gene associated with dominant OI.
Osteogenesis imperfecta due to mutations in non-collagenous genes: lessons in the biology of bone formation.
Smith et al., Bethesda, United States. In Curr Opin Pediatr, 2014
RECENT FINDINGS: Bone-restricted interferon-induced transmembrane (IFITM)-like protein (BRIL) and pigment epithelium-derived factor (PEDF) defects cause types V and VI osteogenesis imperfecta via defective bone mineralization, while defects in cartilage-associated protein (CRTAP), prolyl 3-hydroxylase 1 (P3H1), and cyclophilin B (CYPB) cause types VII-IX osteogenesis imperfecta via defective collagen post-translational modification.
Bone collagen: new clues to its mineralization mechanism from recessive osteogenesis imperfecta.
Weis et al., Seattle, United States. In Calcif Tissue Int, 2013
They include CRTAP, LEPRE1, and PPIB, which encode three proteins forming the prolyl 3-hydroxylase complex; PLOD2 and FKBP10, which encode, respectively, lysyl hydroxylase 2 and a foldase required for its activity in forming mature cross-links in bone collagen; SERPINH1, which encodes the collagen chaperone HSP47; SERPINF1, which encodes pigment epithelium-derived factor required for osteoid mineralization; and BMP1, which encodes the type I procollagen C-propeptidase.
New genes in bone development: what's new in osteogenesis imperfecta.
Blissett et al., Bethesda, United States. In J Clin Endocrinol Metab, 2013
Three recessive OI types arise from defects in any of the components of the collagen prolyl 3-hydroxylation complex (CRTAP, P3H1, CyPB), which modifies the collagen α1(I)Pro986 residue.
Collagen prolyl 3-hydroxylation: a major role for a minor post-translational modification?
Eyre et al., Seattle, United States. In Connect Tissue Res, 2012
Prolyl 3-hydroxylase-1 (P3H1), the enzyme responsible for converting proline to 3-hydroxyproline (3Hyp) in type I collagen, requires the coenzyme CRTAP for activity.
A founder mutation in LEPRE1 carried by 1.5% of West Africans and 0.4% of African Americans causes lethal recessive osteogenesis imperfecta.
Marini et al., Bethesda, United States. In Genet Med, 2012
0.4% of Mid-Atlantic African Americans and 1.48% West Africans carry mutation in LEPRE1 which causes lethal recessive osteogenesis imperfecta.
The identification of novel mutations in COL1A1, COL1A2, and LEPRE1 genes in Chinese patients with osteogenesis imperfecta.
Fu et al., Shanghai, China. In J Bone Miner Metab, 2012
Mutation analyses were performed for COL1A1, COL1A2, CRTAP, and LEPRE1 in a cohort of 58 unrelated Chinese patients with osteogenesis imperfecta.
A novel mutation in LEPRE1 that eliminates only the KDEL ER- retrieval sequence causes non-lethal osteogenesis imperfecta.
Hasegawa et al., Tokyo, Japan. In Plos One, 2011
This is the first report of a mutation in LEPRE1 that eliminates only the KDEL ER-retrieval sequence, whereas other functional domains remain intact
Lethal/severe osteogenesis imperfecta in a large family: a novel homozygous LEPRE1 mutation and bone histological findings.
Pals et al., Amsterdam, Netherlands. In Pediatr Dev Pathol, 2011
We report a large consanguineous Turkish family in which multiple individuals are affected with autosomal recessive lethal or severe osteogenesis imperfecta (OI) due to a novel homozygous LEPRE1 mutation
Prolyl 3-hydroxylase 1 null mice display abnormalities in fibrillar collagen-rich tissues such as tendons, skin, and bones.
Bächinger et al., Portland, United States. In J Biol Chem, 2010
Prolyl 3-hydroxylase 1 null mice display abnormalities in fibrillar collagen-rich tissues such as tendons, skin, and bones
Lack of cyclophilin B in osteogenesis imperfecta with normal collagen folding.
Marini et al., Bethesda, United States. In N Engl J Med, 2010
Mutations in type I collagen result in autosomal dominant osteogenesis imperfecta, whereas mutations in either of two components of the collagen prolyl 3-hydroxylation complex (cartilage-associated protein [CRTAP] and prolyl 3-hydroxylase 1 [P3H1]) cause autosomal recessive osteogenesis imperfecta with rhizomelia (shortening of proximal segments of upper and lower limbs) and delayed collagen folding.
Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta.
Marini et al., Bethesda, United States. In Nat Genet, 2007
CRTAP forms a complex with cyclophilin B and prolyl 3-hydroxylase 1, which is encoded by LEPRE1 and hydroxylates one residue in type I collagen, alpha1(I)Pro986.
CRTAP is required for prolyl 3- hydroxylation and mutations cause recessive osteogenesis imperfecta.
Lee et al., Houston, United States. In Cell, 2006
CRTAP can form a complex with P3H1 and cyclophilin B (CYPB), and Crtap-/- bone and cartilage collagens show decreased prolyl 3-hydroxylation.
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