This website uses cookies to ensure you get the best experience on our website.
- Table of Contents
Facts about Insulin-like growth factor-binding protein 5.
.
Human | |
---|---|
Gene Name: | IGFBP5 |
Uniprot: | P24593 |
Entrez: | 3488 |
Belongs to: |
---|
No superfamily |
IBP5IBP-5; IGF-binding protein 5; IGFBP5; IGFBP-5; insulin-like growth factor binding protein 5; insulin-like growth factor-binding protein 5
Mass (kDA):
30.57 kDA
Human | |
---|---|
Location: | 2q35 |
Sequence: | 2; NC_000002.12 (216672105..216695549, complement) |
Osteosarcoma, and at lower levels in liver, kidney and brain.
Secreted.
You may be wondering about the IGFBP5 marker and its uses. The IGFBP5 gene regulates the transcription of genes and increases the level of collagen and fibronectin in the extracellular matrix (ECM) fraction. Besides this, it is also a diagnostic marker. This article will discuss these two aspects of the gene. Read on to discover the best uses of the IGFBP5 gene in your body.
The IGFBP5 is a fibrotic marker. This blood test can help determine whether you have advanced fibrosis or not. This marker is related to other markers, such as THBS2, COLEC11, DCN, and COLEC163. Moreover, it can predict how much of your body is being used for medical resources. Therefore, it is important to identify any changes in the level of IGFBP5.
This gene belongs to the fibulin family and is mainly localized in the extracellular matrix and elastic basal fibers. It is involved in various biological processes, including cell metabolism, proliferation, differentiation, and extracellular matrix organization. It is known to be overexpressed during the remodeling of tissues, including cancer. In addition, it has also been linked to chronic diseases, such as fibrosis.
IPF is characterized by an increased agglomeration of fibroblasts with a profibrotic phenotype. Fibroblasts are the major source of extracellular matrix (ECM) in fibrotic regions of the lung. In IPF patients, lung fibroblasts exhibit enhanced expression of smooth muscle alpha actin, collagen I, and fibronectin. Furthermore, their ability to multiply is higher than that of normal lungs.
Physiological mechanisms of heart morphogenesis include the action of intrinsic and extrinsic cues from the ECM, which supports spatiotemporal regulation of diverse cellular processes. These cues are crucial to the development of in vitro culture systems that mimic the microenvironment of the heart and the development of improved therapies. In particular, the ECM supports the spatiotemporal regulation of vascular permeability, inflammatory mediators, and leukocyte recruitment and activation. Moreover, MMPs degrade the interstitial matrix and generate bioactive fragments, which contribute to the inflammatory cascade.
Several studies have shown that the polymerization of collagen has altered its growth regulatory properties. The presence of fibronectin in the extracellular matrix enhances adhesion-dependent cell growth and contraction. This property of collagen makes it a useful drug to increase the concentration of this substance. For this purpose, it is necessary to study fibronectin polymerization. In this study, cells with a low concentration of fibronectin were treated with 125I-fibronectin for two days and then incubated with 10 nM FITC-fibronectin for 24 hours.
It was found that fibronectin binding to integrin receptors is necessary for the stability of the extracellular matrix fibronectin fibril formation. FITC-fibronectin-null cells were incubated in culture medium containing FITC-fibronectin, and incubation with 20 nM FITC-fibronectin did not inhibit matrix reorganization.
The IGFBP5 protein mediates cell attachment and survival by regulating a variety of genes. Studies have shown that IGFBP-5 can prevent breast cancer growth in vitro and in vivo. Stable IGFBP5 expression inhibited tumor growth and reduced the levels of bcl-2 mRNA. However, intact IGFBP-5 or proteolytic fragments were not effective in inhibiting tumor growth. This suggests a novel intracrine mechanism for the action of IGFBP-5, including the fact that IGFBP-5 can block the action of TNFa on breast cancer cell lines by blocking NF-kB-mediated cell survival signals.
The NLS domain of IGFBP-5 is responsible for transport. It binds to the nuclear membrane and undergoes importin-b-mediated nuclear transport. However, further studies are necessary to understand the role of spatial regulation of IGFBP-5 in breast cancer pathobiology. The results from these studies suggest that it may be important for the development of therapies targeting breast cancer. The future of these therapeutics depends on this knowledge.
The IGFBP-5 protein is found in breast cancer tissue samples. Breast cancer cells with low IGFBP-5 levels have better outcomes. However, low IGFBP-5 mRNA levels are associated with higher chances of breast cancer metastasis. Other studies have shown that IGFBP-5 is involved in the progression of several other cancers. For this reason, IGFBP-5 is a potential drug for breast cancer.
The clinical utility of IGFBP-5 is unknown, but the expression level of the protein in cervical cells is increased in cervical intraepithelial neoplasia (CIN) and decreased in invasive cervical cancer (CC). The detection of IGFBP-5 and cFLIP may aid in the diagnosis of CIN and differentiating it from CC. However, more research is needed to confirm its usefulness as a diagnostic marker.
The mRNA and protein expression of IGFBP-5 in cervical cancer was significantly higher in patients with CIN than in those with the disease-free control group. Furthermore, the presence of IGFBP-5 was associated with the clinical stage, lymph node metastasis, and tumor differentiation. However, the exact mechanism behind the downregulation of IGFBP-5 in CC remains unclear. It may be a result of down-regulation of the HPV-encoded protein and reduced transcription of the IGFBP-5 mRNA.
The clinical significance of the IGFBP-5 gene in cardiovascular disease is unknown, but it is important to understand its role in the development of angioplasty. Increased IGFBP-5 protein expression is associated with the formation of neointimal tissue. Enhanced PAPP-A2 activity is important in wound healing, fracture healing, and osteoporosis. Increased bone formation and reduced bone resorption are important benefits of the treatment of osteoporosis.
IGFBP5 is a protein whose receptor is found in the pancreas. IGFs stimulate IGFBPs to phosphorylate serine on the cell surface. Phosphorylation of serine on the IGFBP-5 receptor was induced by affinity-purified IGFBP-5-(201--218) and 50 mg/ml l-lysine. Phosphorylated tryptic digests were separated by 2-dimensional thin-layer chromatography.
Mutant IGFBP5 enhances cell growth and motility in breast cancer cells. Mutation of NLS in IGFBP5 leads to localization of IGFBP5 in cytoplasm. This subcellular localization alters cell growth and migration functions. IGFBP5 expression is strongly dependent on the presence of IGFBP5.
IGFBP5 has stimulatory and inhibitory effects on cells. The molecule has been shown to regulate apoptotic molecules, activate signal transduction pathways, and regulate gene transcriptions. In addition, it is known to increase the production of collagen, elastin, and chondroitin synthesis. In addition, IGFBP5 can reduce inflammation in affected tissues. If you suspect that your body is producing IGFBP-5, it's important to know the exact function of this protein.
A recent study has demonstrated that the Boster Bio IGFBP5 marker is highly predictive of cancer. The test is based on the level of expression of IGFBP5, a key fibroblast growth factor, in cancer cells. The Boster Bio IGFBP5 marker is highly accurate and reliable. However, it is not as accurate as the circulating IGFBP3 or IGFBP4, which are both highly expressed in human cells.
PMID: 1850258 by Kiefer M.C., et al. Molecular cloning of a new human insulin-like growth factor binding protein.
PMID: 1709938 by Shimasaki S., et al. Identification of five different insulin-like growth factor binding proteins (IGFBPs) from adult rat serum and molecular cloning of a novel IGFBP-5 in rat and human.
*More publications can be found for each product on its corresponding product page