igfbp การใช้
- Hypoglycosylated IGFBP-3 may be seen after extended glucose starvation.
- Dysregulation of IGFBP-3 has been implicated in many cancers.
- In contrast, human hepatocytes do express IGFBP-3.
- However, IGFBP-3 gene expression in human liver is GH-independent.
- Proteins of the matrix metalloproteinase ( IGFBP ), and activates MMP9 by cleavage.
- IGF-1 binds to IGFBP-3 in a 1 : 1 molar ratio.
- The mechanisms regulating these contrasting effects of IGFBP-3 in vivo are not well understood.
- IGFBP-3 serves to prolong the action of IGF-1 in the human body.
- IGFBP-3, the most abundant protein, accounts for 80 % of all IGF binding.
- IGFBP-3 was first isolated, characterized, and quantitated in human plasma, in 1986.
- The serum proteins transferrin, fibronectin, and plasminogen are also known to bind IGFBP-3.
- IGFBP-3 shares with the other five high-affinity IGFBPs and a 3-domain structure:
- Rat liver IGFBP-3 mRNA is found in nonparenchymal cells including sinusoidal endothelium, but not in hepatocytes.
- Immunoassays for serum IGFBP-3 are often used as part of the diagnosis of childhood GH-deficiency.
- However, instead of the full length, functional protein, IGFBP-3 is found to be cleaved.
- IGFBP-3 can enter cells by both clathrin-mediated and caveolin-mediated endocytosis . possibly involving the transferrin receptor.
- IGFBP-3 is still made ( at a lower level ) by prostate cancer cells and secreted into the surrounding environment.
- IGFBP-3 enters the cell nucleus by a mechanism that is incompletely understood, but involves its binding to importin-?.
- In some studies circulating IGFBP-3 also appears to be nutritionally regulated, although this may not be seen at the mRNA level.
- IPLEX ( Mecasermin rinfabate ) is composed of recombinant human IGF-1 ( rhIGF-1 ) and its binding protein IGFBP-3.
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