A Short Form of the Heparin-binding EGF-like Growth Factor with a Changed EGF Domain |
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Authors: | Luk'yanov E V Viedlokha A Kuyavskaya D V Olsnes S Kozlov Yu V |
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Institution: | (1) Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 117984, Russia;(2) Center of Medical Research, University of Oslo, Moscow, 117334, Russia;(3) Norwegian Radiation Hospital, Institute for Cancer Research, Oslo, 0310, Norway |
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Abstract: | In all secreted proteins related to the epidermal growth factor (EGF), EGF domains that occur in a mature factor are each encoded by two exons, and those that do not, by one exon. During splicing, additional exon 3a can be inserted between exons 3 and 4, which code for the EGF domain of the mature heparin-binding EGF-like growth factor (HB-EGF). The resulting mRNA codes for the short form of HB-EGF (SF HB-EGF), which retains the signal peptide, the propeptide, and the heparin-binding domain. However, its EGF domain lacks the C-terminal subdomain essential for the interaction with the EGF receptor (EGFR). Structural analysis suggested that SF HB-EGF is a secreted polypeptide that has high affinity for heparin but weakly, if at all, interacts with EGFR. Data obtained in three different systems indicated that SF HB-EGF possesses a mitogenic activity but utilizes a signal transduction pathway other than that of HB-EGF. |
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Keywords: | growth factors heparin-binding growth factor epidermal growth factor isoforms EGF domain receptors alternative splicing mitogenic activity |
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