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Secreted phosphoprotein 2, 24kDa

spp24, secreted phosphoprotein 24, SPP-2, hSPP2, Secreted phosphoprotein 24 kDa
This gene encodes a secreted phosphoprotein that is a member of the cystatin superfamily. [provided by RefSeq, Oct 2008] (from NCBI)
Top mentioned proteins: CAN, fibrillin-1, ACID, HAD, OUT
Papers on spp24
Low Mass Blood Peptides Discriminative of Inflammatory Bowel Disease (IBD) Severity: A Quantitative Proteomic Perspective.
Leong et al., Australia. In Mol Cell Proteomics, Jan 2016
Peptides differentiating controls from IBD originate from secreted phosphoprotein 24 (SPP24, p = 0.000086, 0.009); whereas those in remission and healthy can be differentiated in UC by SPP24 (p = 0.00023, 0.001), α-1-microglobulin (AMBP, p = 0.006) and CD by SPP24 (p = 0.019, 0.05).
Fibroblastic synoviocytes secrete plasma proteins via α2 -macroglobulins serving as intracellular and extracellular chaperones.
Murray et al., Los Angeles, United States. In J Cell Biochem, Nov 2015
Using Western blotting, qPCR, and mass spectrometry, we found that Hig-82 lapine fibroblastic synovicytes cultured under serum-free conditions expressed and secreted plasma proteins, including the cytokine-binding protein secreted phosphoprotein 24 kDa (Spp24) and many of the proteases and protease inhibitors found in SF.
The bone matrix protein secreted phosphoprotein 24 kD (Spp24): bone metabolism regulator and starting material for biotherapeutic materials.
Brochmann Murray et al., Los Angeles, United States. In Histol Histopathol, May 2015
Secreted phosphoprotein 24 kD (Spp24) is a bone matrix protein that appears to be derived primarily from the liver and delivered to other tissues in a protective complex.
A carboxy terminal BMP/TGF-β binding site in secreted phosphoprotein 24 kD independently affects BMP-2 activity.
Murray et al., Shanghai, China. In J Cell Biochem, Apr 2015
Secreted phosphoprotein 24 kD (spp24) is a bone matrix protein isolated during attempts to identify osteogenic proteins.
Secreted phosphoprotein 24 kD inhibits nerve root inflammation induced by bone morphogenetic protein-2.
Daubs et al., Shanghai, China. In Spine J, Mar 2015
PURPOSE: To investigate the direct neurotoxic effects of BMP-2 and test the hypotheses that the use of BMP binding proteins, such as secreted phosphoprotein 24 kD (Spp24), can reduce or eliminate these effects.
Identification of plasma protein markers common to patients with malignant tumour and Abnormal Savda in Uighur medicine: a prospective clinical study.
Abudula et al., Ürümqi, China. In Bmc Complement Altern Med, 2014
ELISA detection showed significant upregulation of plasma SAA1 and SPP24 and downregulation of PIGR and FASN in ASt compared with nASt and NC (p < 0.05).
Analysis of differential gene expression profiles in Caenorhabditis elegans knockouts for the v-SNARE master protein 1.
Holgado et al., United States. In J Neurosci Res, 2014
Analyses of microarray experiments performed using three independent biological samples per strain and three technical replicas and dye swaps showed induction of genes coding for major sperm proteins and repression of SPP-2 in vsm-1 mutants.
Effects of the bone morphogenetic protein binding protein spp24 (secreted phosphoprotein 24 kD) on the growth of human lung cancer cells.
Wang et al., Los Angeles, United States. In J Orthop Res, 2011
Secreted phosphoprotein 24 kDa (spp24) has been shown to bind to both BMP-2 and TGF-β and to markedly inhibit the osteogenic properties of rhBMP-2.
Full-length spp24, but not its 18.5-kDa proteolytic fragment, inhibits bone-healing in a rodent model of spine fusion.
Wang et al., Los Angeles, United States. In J Bone Joint Surg Am, 2011
We developed a synthetic adjuvant therapy based on the sequence of a BMP-binding protein, secreted phosphoprotein-24 (spp24), which enhances the effects of BMPs and ameliorates the adverse reactions.
Prevention of hydrogen peroxide-induced oxidative stress in HDF cells by peptides derived from seaweed pipefish, Syngnathus schlegeli.
Kim et al., Pusan, South Korea. In Peptides, 2011
Two new peptides derived from seaweed pipefish Syngnathus schlegeli, SPP-1(QLGNLGV) and SPP-2 (SVMPVVA) were assessed for their ability to prevent hydrogen peroxide induced oxidative stress in human dermal fibroblasts (HDFs).
Alanine-scanning mutations of the BMP-binding domain of recombinant secretory bovine spp24 affect cytokine binding.
Brochmann et al., Los Angeles, United States. In Connect Tissue Res, 2010
Secreted phosphoprotein 24 kDa (spp24) is a bone morphogenetic protein (BMP)/transforming growth factor-β cytokine-binding protein.
The stromal processing peptidase of chloroplasts is essential in Arabidopsis, with knockout mutations causing embryo arrest after the 16-cell stage.
Jarvis et al., Leicester, United Kingdom. In Plos One, 2010
Two independent mutant Arabidopsis lines with T-DNA insertions in the SPP gene were analysed (spp-1 and spp-2).
Carboxy terminus of secreted phosphoprotein-24 kDa (spp24) is essential for full inhibition of BMP-2 activity.
Murray et al., Los Angeles, United States. In J Orthop Res, 2010
Secreted phosphoprotein-24 kDa (spp24) is a bone morphogenetic protein (BMP)-binding protein isolated from bone.
Bone morphogenetic protein-2 activity is regulated by secreted phosphoprotein-24 kd, an extracellular pseudoreceptor, the gene for which maps to a region of the human genome important for bone quality.
Murray et al., Los Angeles, United States. In Metabolism, 2009
spp24 contains at least 2 single nucleotide polymorphisms. Given its mechanism of action and sequence variability, SPP24 may be an interesting candidate for future studies of the genetic regulation of bone mass.
The signal peptide peptidase is required for pollen function in Arabidopsis.
Schnell et al., Amherst Center, United States. In Plant Physiol, 2009
Homozygous plants carrying a T-DNA insertion mutation in AtSPP, spp-2, could not be recovered, and transmission of the mutant allele through pollen was reduced to less than 2% in reciprocal cross experiments.
Sphingosine 1-phosphate phosphatase 2 is induced during inflammatory responses.
Billich et al., Vienna, Austria. In Cell Signal, 2007
This study provides detailed insights into the regulation of SPP2 gene expression and suggests that SPP2 might be a novel player in pro-inflammatory signalling.
Characterization of the human secreted phosphoprotein 24 gene (SPP2) and comparison of the protein sequence in nine species.
Dalgleish et al., Leicester, United Kingdom. In Matrix Biol, 2004
Results describe the localization of the human secreted phosphoprotein 24 gene, its structure and the start of transcription in liver.
Identification and characterization of a novel human sphingosine-1-phosphate phosphohydrolase, hSPP2.
Igarashi et al., Sapporo, Japan. In J Biol Chem, 2003
characterization of SPP2, another member of the SPP family that may play a role in attenuating intracellular S1P signaling.
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