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IGFBPrP1 transfection inhibited cell growth, and induced G1 phase arrest and cellular senescence in HEC1A cells while gene silencing presented the adverse functional changes.
Serum IGFBP7 levels were raised during acute exacerbation in COPD (show ARCN1 Proteins) patients.
epithelial cells and leukocytes from the urinary sediment. CONCLUSION: The gene expression pattern of IGFBP7 and TIMP-2 (show TIMP2 Proteins) from urinary sediment, which contains desquamated renal tubular epithelial cells, did not correlate with [IGFBP7]x[TIMP-2 (show TIMP2 Proteins)] protein, indicating that IGFBP7 and TIMP-2 (show TIMP2 Proteins) measured in the NephroCheck(R) test originated predominantly from intact but stressed cells of the kidney itself
In patients with heart failure with preserved ejection fraction, IGFBP7 may be a novel biomarker of diastolic function and exercise capacity.
High IGFBP7 expression is associated with acute kidney injury.
NEAT1-associated paraspeckle proteins P54nrb (show NONO Proteins) and PSF have been reported as positive regulators of c-Myc (show MYC Proteins) translation through interaction with c-Myc (show MYC Proteins) IRES
Urine [TIMP-2 (show TIMP2 Proteins)]*[IGFBP7] is a promising candidate for early detection of AKI, especially in ruling-out AKI
Meta-analysis indicated that urinary [TIMP-2 (show TIMP2 Proteins)].[IGFBP7] may be a reliable biomarker for the early detection of acute kidney injury in adults.
TIMP-2 (show TIMP2 Proteins) is both expressed and secreted preferentially by cells of distal tubule origin, while IGFBP7 is equally expressed across tubule cell types yet preferentially secreted by cells of proximal tubule origin. In human kidney tissue, strong staining of IGFBP7 was seen in the luminal brush-border region of a subset of proximal tubule cells, and TIMP-2 (show TIMP2 Proteins) stained intracellularly in distal tubules.
study of polymorphisms of the porcine IGFBP7 promoter region in different pig breeds
analysis of how A-to-I RNA editing of the IGFBP7 transcript increases during aging in porcine brain tissues
Our findings define an immune component of the pleiotropic mechanisms through which IGFBP7 suppresses hepatocellular carcinoma
Study shows that IGFBP7 contributes significantly to mesenchymal stromal cells (MSC (show MSC Proteins))-mediated immune modulation, as is shown by decreasing ability of IGFBP7 knockdown in MSCs to restore proliferation and cytokine production in T-cells.
data suggest that IGFBP-7 was up regulated during EAE and inhibit the transition from OPCs to mature OLs, implying its use as a potential therapeutic target for the treatment of inflammatory demyelinating diseases
Our data suggest that loss of Igfbp7 induces precocious involution possibly through diminished cell survival signals.
Angiomodulin is necessary for cardiac commitment of embryonic stem cells (ESCs (show NR2E3 Proteins)) and its regulation depends on TAp63 isoform.
results show that Smarcb1 (show SMARCB1 Proteins) is required for transcriptional activation of Igfbp7 and show that re-introduction of Igfbp7 alone can hinder tumor development; results define a novel mechanism for Smarcb1 (show SMARCB1 Proteins)-mediated tumorigenesis
a model whereby IGFBP7 binds to unoccupied IGF1R (show IGF1R Proteins) and suppresses downstream signaling, thereby inhibiting protein synthesis, cell growth, and survival.
IGFBP7 has a novel role in mouse uterus: it is regulating uterine receptivity through Th1 (show HAND1 Proteins)/Th2 lymphocyte balance and decidualization.
fear extinction-induced IGF2/IGFBP7 signalling promotes the survival of 17-19-day-old newborn hippocampal neurons
Results demonstrate that the vascular-specific marker angiomodulin (AGM) modulates vascular remodeling in part by temporizing the proangiogenic effects of VEGF-A (show VEGFA Proteins).
This gene encodes a member of the insulin-like growth factor (IGF)-binding protein (IGFBP) family. IGFBPs bind IGFs with high affinity, and regulate IGF availability in body fluids and tissues and modulate IGF binding to its receptors. This protein binds IGF-I and IGF-II with relatively low affinity, and belongs to a subfamily of low-affinity IGFBPs. It also stimulates prostacyclin production and cell adhesion. Alternatively spliced transcript variants encoding different isoforms have been described for this gene, and one variant has been associated with retinal arterial macroaneurysm (PMID:21835307).
insulin-like growth factor-binding protein 7
, IGF-binding protein 7
, PGI2-stimulating factor
, prostacyclin-stimulating factor
, tumor-derived adhesion factor