Abstract
Backgroundvon 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.ResultsHere, 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.ConclusionsThis study suggests that both mammalian cell adhesion and marine underwater adhesion exploits a strong vWF-collagen interaction for successful wet adhesion. In addition, vWF like domains containing proteins including PTMP1 have a great potential for tissue engineering and the development of biomedical adhesives as a component for extra-cellular matrix.
Highlights
In order for mussels to live and adapt in an environment that has mechanical challenges due to waves and currents, they are able to attach themselves to the surface in both dry and wet states through byssus
Proximal Thread Matrix Protein1 (PTMP1) has the molecular weight of 48.5 kDa and the protein upon moderately post-translational modified by glycans, was observed to have two sequence stretches with homology to the group of von Willebrand factor type A domains [8, 9]. vWF is a large multimeric glycoprotein presented in blood plasma, endothelial cells, and subendothelial matrix of the vessel. vWF is widely distributed as a functional domain in other extracellular protein superfamilies including integrins which are involved in binding various macromolecular ligands for instance collagens, laminins, and glycosaminoglycans such as heparin and hyaluronan. vWF has four types of domain, i.e. domains A, B, C, and D
In summary, we mass produced and purified PTMP1 originated from M. galloprovicialis in E. coli system in order to look at its possibility as a component for the extracellular matrix (ECM)
Summary
In order for mussels to live and adapt in an environment that has mechanical challenges due to waves and currents, they are able to attach themselves to the surface in both dry and wet states through byssus. The byssus threads are mostly composed of proteins and each of the threads has three different parts, i.e. a flexible and elastic proximal part, a rigid and stiff distal part and an adhesive plaque at the end [1, 2]. The change of the mechanical properties of the byssus thread is not sudden but gradual due to the mechanical gradient of thread collagenous protein called preCols [3]. The distal portion of the byssus is dominated by the densely packed collagen bundles, while the proximal portion of the byssus has only 30 % of collagen and the rest is the matrix protein, which enables the proximal portion of the byssus for cyclic stress at a fixed strain. The proximal thread has prominent strain stiffening property while the distal thread has stress softening property in which the matrix protein plays an important
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