NDLI: Semi-synthesis of a HGF/SF kringle one (K1) domain scaffold generates a potent <i>in vivo</i> MET receptor agonist

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Semi-synthesis of a HGF/SF kringle one (K1) domain scaffold generates a potent in vivo MET receptor agonist

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Chemical Science Vol - 6 Issue - 2

Chemical Science Vol -5

Chemical Science Vol -4

Chemical Science Vol -3

Chemical Science Vol -2

Chemical Science Vol -1

Semi-synthesis of a HGF/SF kringle one (K1) domain scaffold generates a potent in vivo MET receptor agonist

Content Provider	Royal Society of Chemistry (RSC)
Author	Mougel, Alexandra Ollivier, Nathalie Raibaut, Laurent Melnyk, Oleg Leclercq, Bérénice Cianférani, Sarah Vicogne, Jérôme Marcoux, Julien Paquet, Charlotte Tulasne, David Adriaenssens, Eric Drobecq, Hervé Jonge, Hugo de Simonneau, Claire
Copyright Year	2015
Abstract	The development of MET receptor agonists is an important goal in regenerative medicine, but is limited by the complexity and incomplete understanding of its interaction with HGF/SF (Hepatocyte Growth Factor/Scatter Factor). NK1 is a natural occurring agonist comprising the N-terminal (N) and the first kringle (K1) domains of HGF/SF. In the presence of heparin, NK1 can self-associate into a “head to tail” dimer which is considered as the minimal structural module able to trigger MET dimerization and activation whereas isolated K1 and N domains showed a weak or a complete lack of agonistic activity respectively. Starting from these structural and biological observations, we investigated whether it was possible to recapitulate the biological properties of NK1 using a new molecular architecture of isolated N or K1 domains. Therefore, we engineered multivalent N or K1 scaffolds by combining synthetic and homogeneous site-specifically biotinylated N and K1 domains (NB and K1B) and streptavidin (S). NB alone or in complex failed to activate MET signaling and to trigger cellular phenotypes. Importantly and to the contrary of K1B alone, the semi-synthetic K1B/S complex mimicked NK1 MET agonist activity in cell scattering, morphogenesis and survival phenotypic assays. Impressively, K1B/S complex stimulated in vivo angiogenesis and, when injected in mice, protected the liver against fulminant hepatitis in a MET dependent manner whereas NK1 and HGF were substantially less potent. These data reveal that without N domain, proper multimerization of K1 domain is a promising strategy for the rational design of powerful MET agonists.
Starting Page	2110
Ending Page	2121
Page Count	12
File Format	HTM / HTML PDF
ISSN	20416520
Volume Number	6
Issue Number	3
Journal	Chemical Science
DOI	10.1039/c4sc03856h
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Subscribed
Subject Keyword	Kringle domain Agonist Wound healing Cell surface receptor Hepatocyte growth factor Liver Tachykinin receptor 1 Protein dimer Morphogenesis N-terminus Angiogenesis Streptavidin Heparin
Content Type	Text
Resource Type	Article
Subject	Chemistry

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Semi-synthesis of a HGF/SF kringle one (K1) domain scaffold generates a potent in vivo MET receptor agonist

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