A short form of the heparin-binding EGF-like growth factor with a changed EGF domain

作者：Luk'yanov EV^*; Viedlokha A; Kuyavskaya DV; Olsnes S; Kozlov YV

来源：Molecular Biology, 2002, 36(1): 58-64.

DOI：10.1023/A:1014246423243

• growth factors
• heparin-binding growth factor
• epidermal growth factor
• isoformis
• EGF domain
• receptors
• alternative splicing
• mitogenic activity

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.

• 出版日期2002-2