Recombinant mussel proximal thread matrix protein promotes osteoblast cell adhesion and proliferation

BMC Biotechnology
Hee Young YooJeong Hyun Seo

Abstract

von Willebrand factor (VWF) is a key load bearing domain for mamalian cell adhesion by binding various macromolecular ligands in extracellular matrix such as, collagens, elastin, and glycosaminoglycans. Interestingly, vWF like domains are also commonly found in load bearing systems of marine organisms such as in underwater adhesive of mussel and sea star, and nacre of marine abalone, and play a critical load bearing function. Recently, Proximal Thread Matrix Protein1 (PTMP1) in mussel composed of two vWF type A like domains has characterized and it is known to bind both mussel collagens and mammalian collagens. Here, we cloned and mass produced a recombinant PTMP1 from E. coli system after switching all the minor codons to the major codons of E. coli. Recombinant PTMP1 has an ability to enhance mouse osteoblast cell adhesion, spreading, and cell proliferation. In addition, PTMP1 showed vWF-like properties as promoting collagen expression as well as binding to collagen type I, subsequently enhanced cell viability. Consequently, we found that recombinant PTMP1 acts as a vWF domain by mediating cell adhesion, spreading, proliferation, and formation of actin cytoskeleton. This study suggests that both mammalian cell adhesion and ma...Continue Reading

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Citations

Jul 6, 2018·Biotechnology Journal·Jia Wang, Thomas Scheibel
Mar 5, 2019·Chembiochem : a European Journal of Chemical Biology·Nediljko Budisa, Tobias Schneider

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Methods Mentioned

BETA
reverse
column chromatography
electrophoresis
confocal microscopy
PCR

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