AI Article Synopsis
- The study focuses on a modified insulin growth factor (BOMIGF) fused with interleukin-3 (IL-3) which enhances the migration of specific human hematopoietic cells (CD34+).
- When tested, a phosphatidylinositol-3 (PI-3) kinase inhibitor blocked this migration, indicating its crucial role in the process.
- In contrast, a Rho kinase inhibitor did not significantly affect migration, implying that the PI-3 kinase pathway is the primary mechanism driving the observed effects of the BOMIGF-IL-3 chimera.
Article Abstract
A chimera of an N-terminally modified insulin growth factor (IGF)-II, NQPQMVHTY-hIGF-II(9-67) (BOMIGF), fused to interleukin-3 (IL-3) significantly improved the migration of CD34(+) human hematopoietic cells with respect to the effects observed during co-stimulation with BOMIGF and IL-3. A phosphatidylinositol-3 (PI-3) kinase inhibitor specifically inhibited migration in the presence of the chimera, while no significant difference in the inhibition of migration was observed in the presence of a Rho kinase inhibitor. These results suggest a key role of the PI-3 kinase pathway in the potentiation of migration caused by the linkage of BOMIGF and IL-3.
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| http://dx.doi.org/10.1016/s0014-5793(02)03025-9 | DOI Listing |
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Potentiation of hematopoietic cell migration with an IGF-interleukin-3 fusion protein.
FEBS Lett
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Article Synopsis
- The study focuses on a modified insulin growth factor (BOMIGF) fused with interleukin-3 (IL-3) which enhances the migration of specific human hematopoietic cells (CD34+).
- When tested, a phosphatidylinositol-3 (PI-3) kinase inhibitor blocked this migration, indicating its crucial role in the process.
- In contrast, a Rho kinase inhibitor did not significantly affect migration, implying that the PI-3 kinase pathway is the primary mechanism driving the observed effects of the BOMIGF-IL-3 chimera.
Preparation of a recombinant chimaera of insulin-like growth factor II and interleukin 3 with high proliferative potency for haemopoietic cells.
Biochem J
September 1997
Endocrine Laboratory, Royal Victoria Hospital, Montreal, Canada.
We have found that a slightly modified insulin-like growth factor II (IGF II) consisting of a chimaera of bombyxin and human IGF II (BOMIGF) is properly secreted in insect cells by using the baculovirus expression system. Human interleukin 3 (IL-3) was attached to the C-terminal amino acid residue of BOMIGF with peptide linkers containing five or twelve residues. Only the chimaera with the 12-residue linker had biological activities of both IGF II and IL-3.
View Article and Find Full Text PDFThe influence of various insect cell lines, p10 and polyhedrin promoters in the production of secreted insulin-like growth factor-interleukin-3 chimeras in the baculovirus expression system.
J Biotechnol
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A technique for the optimal synthesis of secreted fusion proteins between insulin-like growth factors (IGFs) and cytokines is described. The cDNA of BOMIGF, a fusion protein between the insect insulin-like peptide bombyxin and IGF II, has been linked to the gene of interleukin-3. The BOMIGF-interleukin 3 fusion gene was cloned downstream of the promoter regions of the p10 and polyhedrin proteins within baculovirus transfer vectors.
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