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Review
. 2018 Oct 10;4(1):107-113.
doi: 10.1016/j.bioactmat.2018.09.001. eCollection 2019 Mar.

Review: Bioengineering approach for the repair and regeneration of peripheral nerve

Joshua Moskow  1   2 , Bryan Ferrigno  1 , Nikhil Mistry  1 , Devina Jaiswal  1   2 , Ketan Bulsara  3 , Swetha Rudraiah  1   4 , Sangamesh G Kumbar  1   2
Affiliations
Review

Review: Bioengineering approach for the repair and regeneration of peripheral nerve

Joshua Moskow et al. Bioact Mater. .

Erratum in

Abstract

Complex craniofacial surgeries of damaged tissues have several limitations, which present complications and challenges when trying to replicate facial function and structure. Traditional treatment techniques have shown suitable nerve function regeneration with various drawbacks. As technology continues to advance, new methods have been explored in order to regenerate damaged nerves in an effort to more efficiently and effectively regain original function and structure. This article will summarize recent bioengineering strategies involving biodegradable composite scaffolds, bioactive factors, and external stimuli alone or in combination to support peripheral nerve regeneration. Particular emphasis is made on the contributions of growth factors and electrical stimulation on the regenerative process.

Keywords: Composite materials; Electrical stimulation; Growth factor; Peripheral nerve regeneration.

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Figures

Image 1
Graphical abstract
Fig. 1
Fig. 1
Structural representation of a nerve in the peripheral nervous system. Highlighted are the fascicle structures all encased in the Epineurial Sheath.
Fig. 2
Fig. 2
Flow Chart of the various nerve treatment strategies.
Fig. 3
Fig. 3
Receptor Tyrosine Kinase (RTKs) mechanism. It is a transmembrane protein spanning the length of the membrane. Initially, it is inactive, with each monomer (red) having an open substrate binding site, and the tyrosine kinase domains (yellow) are un-phosphorylated and inactive. After substrate (green) binds, the monomers aggregate, dimerize, and the tyrosine kinase domains cross-phosphorylate each other, they are now active (purple). Finally, relay proteins (pink) bind to the activated, phosphorylated tyrosine kinase domains, and undergo conformational changes that ultimately lead to transduction cascades and cellular events (black shape).
See this image and copyright information in PMC

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