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Recombinant Human IGF-I背景介绍
The IGFs are mitogenic, polypeptide growth factors that stimulate the proliferation and survival of various cell types, including muscle, bone, and cartilage tissue in vitro. IGFs are predominantly produced by the liver, although a variety of tissues produce the IGFs at distinctive times. The IGFs belong to the Insulin gene family, which also contains insulin and relaxin. The IGFs are similar to insulin by structure and function, but have a much higher growth-promoting activity than insulin. IGF-II expression is influenced by placenta lactogen, while IGF-I expression is regulated by growth hormone. Both IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR), but IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contain N-terminal and C-terminal propeptide regions. Recombinant Human IGF-I and IGF-II are globular proteins containing 70 and 67 amino acids, respectively, and 3 intra-molecular disulfide bonds. The calculated molecular weight of Recombinant Human IGF-I is 7.6 kDa.
Source:E.coli
Synonyms:Insulin-like Growth Factor-I, Somatamedin C, IGF-IA
AA Sequence:
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA
Purity:≥ 98% by SDS-PAGE gel and HPLC analyses.
Biological Activity:The ED50 was determined by a cell proliferation assay using FDC-P1 cells is ≤ 2.0 ng/ml, corresponding to a specific activity of ≥ 5 x 105 units/mg.
文献索引：
IGF-1 regulates astrocytic phagocytosis and inflammation through the p110α isoform of PI3K in a sex-specific manner
Abstract
Insulin-like growth factor-I (IGF-I) signaling plays a key role in neuroinflammation. Here we show that IGF-1 also regulates phagocytosis of reactive astrocytes through p110α isoform of phosphatidylinositol 3-kinase (PI3K), differentially in both sexes. Systemic bacterial lipopolysaccharide (LPS)-treatment increased the expression of GFAP, a reactive astrocyte marker, in the cortex of mice in both sexes and was blocked by IGF-1 only in males. In primary astrocytes, LPS enhanced the mRNA expression of Toll-like receptors (TLR2,4) and proinflammatory factors: inducible nitric oxide synthase (iNOS), chemokine interferon-γ-inducible protein-10 (IP-10) and cytokines (IL-1β, IL-6, and IL-10) in male and female. Treatment with IGF-1 counteracted TLR4 but not TLR2, iNOS, and IP10 expression in both sexes and cytokines expression in males. Furthermore, reactive astrocyte phagocytosis was modulated by IGF-1 only in male astrocytes. IGF-1 was also able to increase AKT-phosphorylation only in male astrocytes. PI3K inhibitors, AG66, TGX-221, and CAL-101, with selectivity toward catalytic p110α, p110β, and p110δ isoforms respectively, reduced AKT-phosphorylation in males. All isoforms interact physically with IGF-1-receptor in both sexes. However, the expression of p110α is higher in males while the expression of IGF-1-receptor is similar in male and female. AG66 suppressed the IGF-1 effect on cytokine expression and counteracted the IGF-1-produced phagocytosis decrease in male reactive astrocytes. Results suggest that sex-differences in the effect of IGF-1 on the AKT-phosphorylation could be due to a lower expression of the p110α in female and that IGF-1-effects on the inflammatory response and phagocytosis of male reactive astrocytes are mediated by p110α/PI3K subunit.
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