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Proline/arginine-rich end leucine-rich repeat protein

PRELP, proline/arginine-rich end leucine-rich repeat protein
The protein encoded by this gene is a leucine-rich repeat protein present in connective tissue extracellular matrix. This protein functions as a molecule anchoring basement membranes to the underlying connective tissue. This protein has been shown to bind type I collagen to basement membranes and type II collagen to cartilage. It also binds the basement membrane heparan sulfate proteoglycan perlecan. This protein is suggested to be involved in the pathogenesis of Hutchinson-Gilford progeria (HGP), which is reported to lack the binding of collagen in basement membranes and cartilage. Alternatively spliced transcript variants encoding the same protein have been observed. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: fibromodulin, Lum, CAN, fibrillin-1, Decorin
Papers on PRELP
The small leucine-rich repeat proteoglycans in tissue repair and atherosclerosis.
Chakravarti et al., Lund, Sweden. In J Intern Med, Nov 2015
We focus on five SLRPs, decorin, biglycan, lumican, fibromodulin and PRELP, because these have been detected in atherosclerotic plaques or demonstrated to have a role in animal models of atherosclerosis.
Extracellular matrix disruption is an early event in the pathogenesis of skeletal disease in mucopolysaccharidosis I.
Clarke et al., Vancouver, Canada. In Mol Genet Metab, Feb 2015
These studies reveal significant decreases in six key structural and signaling extracellular matrix proteins; biglycan, fibromodulin, PRELP, type I collagen, lactotransferrin, and SERPINF1.
Proteins associated with pancreatic cancer survival in patients with resectable pancreatic ductal adenocarcinoma.
Brentnall et al., Seattle, United States. In Lab Invest, 2015
Immunohistochemistry analysis using an independent cohort of 145 PDAC confirmed that the higher abundance of ribosomal protein S8 (RPS8) and prolargin (PRELP) were correlated with STS and VLTS, respectively.
Genome-wide scan for selection signatures in six cattle breeds in South Africa.
Maiwashe et al., South Africa. In Genet Sel Evol, 2014
In addition, a number of candidate genes associated with the nervous system (WNT5B, FMOD, PRELP, and ATP2B), immune response (CYM, CDC6, and CDK10), production (MTPN, IGFBP4, TGFB1, and AJAP1) and reproductive performance (ADIPOR2, OVOS2, and RBBP8) were also detected as being under selection.
Protein-protein interaction network of gene expression in the hydrocortisone-treated keloid.
Fan et al., Shanghai, China. In Int J Dermatol, 2014
Furthermore, three critical genes in the module, including COL1A1, NID1, and PRELP, were screened in the PPI network analysis.
S100A6 and its extracellular targets in Wharton's jelly of healthy and preeclamptic patients.
Filipek et al., Warsaw, Poland. In Placenta, 2014
We have identified several proteins that might interact with S100A6, among them are lumican and PRELP, found in Wharton's jelly of healthy and preeclamptic patients, and IGFBP-1 identified, as an S100A6 target, only in preeclamptic tissue.
AAV-mediated expression of human PRELP inhibits complement activation, choroidal neovascularization and deposition of membrane attack complex in mice.
Kumar-Singh et al., Boston, United States. In Gene Ther, 2014
Here we investigate the potential of human proline/arginine-rich end leucine-rich repeat protein (PRELP) as an inhibitor of complement-mediated damage when delivered via the subretinal route using an AAV2/8 vector.
Proteomic identification of potential prognostic biomarkers in resectable pancreatic ductal adenocarcinoma.
Hammer et al., Cluj-Napoca / Kolozsv√°r, Romania. In Proteomics, 2014
Screening of data revealed a number of molecules that had already been related to PDAC such as galectin-1 (LEG1), major vault protein, adenylyl cyclase-associated protein 1 (CAP1), but also a potential new prognostic biomarker prolargin (PRELP).
Intrinsic multipotential mesenchymal stromal cell activity in gelatinous Heberden's nodes in osteoarthritis at clinical presentation.
McGonagle et al., In Arthritis Res Ther, 2013
Gene cluster analysis showed that HN-MSCs were more closely related to SF- than normal or OA BM-MSCs with significantly higher expression of synovium-related gene markers such as bone morphogenic protein 4 (BMP4), bone morphogenetic protein receptor type 1A (BMPR1A), protein/leucine-rich end leucine-rich repeat protein (PRELP), secreted frizzled-related protein 4 (SFRP4), and tumor necrosis factor alpha-induced protein 6 (TNFAIP6) (P <0.05).
Proline/arginine-rich end leucine-rich repeat protein N-terminus is a novel osteoclast antagonist that counteracts bone loss.
Teti et al., L'Aquila, Italy. In J Bone Miner Res, 2013
(hbd) PRELP is a peptide corresponding to the N-terminal heparin binding domain of the matrix protein proline/arginine-rich end leucine-rich repeat protein (PRELP).
Female-specific hypertension loci on rat chromosome 13.
Moreno et al., Milwaukee, United States. In Hypertension, 2013
The congenic interval of the protective line 9F strain contains 3 genes (Optc, Prelp, and Fmod), and the hypertensive line 9E contains 1 additional gene (Btg2).
Proline/arginine-rich end leucine-rich repeat protein converts stem cells to ligament tissue and Zn(II) influences its nuclear expression.
Nagata et al., Kurume, Japan. In Stem Cells Dev, 2013
Proline/arginine-rich end leucine-rich repeat protein (PRELP) was identified in ligament-specific locations by liquid chromatography-tandem mass spectrometry.
A proline/arginine-rich end leucine-rich repeat protein (PRELP) variant is uniquely expressed in chronic lymphocytic leukemia cells.
Mellstedt et al., Stockholm, Sweden. In Plos One, 2012
Proline/arginine-rich end leucine-rich repeat protein (PRELP) belongs to the small leucine-rich proteoglycan (SLRP) family, normally expressed in extracellular matrix of collagen-rich tissues.
PRELP protein inhibits the formation of the complement membrane attack complex.
Blom et al., Lund, Sweden. In J Biol Chem, 2012
PRELP may down-regulate complement attack at basement membranes and on damaged cartilage and therefore limit pathological complement activation in inflammatory disease such as RA.
Spatial and temporal regulation of gene expression in the mammalian growth plate.
Nilsson et al., Bethesda, United States. In Bone, 2010
Prelp were present exclusively in the proliferative zone of in growth plate cartilage of 1-week-old rats.
The glycosaminoglycan-binding domain of PRELP acts as a cell type-specific NF-kappaB inhibitor that impairs osteoclastogenesis.
Teti et al., L'Aquila, Italy. In J Cell Biol, 2009
PRELP has a role in skeletal remodeling.
The consequence of PRELP overexpression on skin.
Roughley et al., Montréal, Canada. In Matrix Biol, 2007
PRELP overexpression leads to a connective tissue phenotype in the skin, where the organization of collagen fibrils in the dermis was perturbed and the thickness of the hypodermal fat layer was diminished.
Small leucine rich repeat proteoglycans (SLRPs) in the human sclera: identification of abundant levels of PRELP.
Rada et al., Providence, United States. In Mol Vis, 2005
Relative abundance of PRELP mRNA and protein inhuman sclera, and observed age-related variation in scleral PRELP expression suggests that PRELP may play critical role in regulating biomechanical properties of scleral extracellular matrix.
PRELP, collagen, and a theory of Hutchinson-Gilford progeria.
Lewis, Austin, United States. In Ageing Res Rev, 2003
Proline/arginine-rich end leucine-rich repeat protein (PRELP) a small leucine-rich proteoglycan (SLRP), binds type I collagen to basement membranes and type II collagen to cartilage.
Noncollagenous, nonproteoglycan macromolecules of cartilage.
Azizan et al., Tampa, United States. In Cell Mol Life Sci, 1999
The putative roles of these proteins range from involvement in matrix organization or matrix-cell signaling (PRELP, chondroadherin, cartilage oligomeric protein and cartilage matrix protein) through to molecules that are likely to be involved with modulation of the chondrocyte phenotype (CD-RAP, CDMPs, chondromodulin and pleiotrophin).
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