Role of the elastin receptor complex (S-Gal/Cath-A/Neu-1) in skin repair and regeneration.

Abstract

Impaired elastic fiber assembly constitutes one major problem in skin wound healing. Recent data indicate that a ternary complex involving a splicing form of beta-galactosidase associated with cathepsin-A and neuraminidase-1 directs the transport of tropoelastin to the fibroblast plasma membrane and participates in the deposition of the elastin precursor onto a microfibrillar scaffold. In addition, this elastin receptor complex is ubiquitously expressed and also acts as a true receptor for elastin-derived peptides produced during the initial stage of wound repair following elastase-mediated proteolysis action. Among the peptides generated, those having a x.G.x.x.P.G. motif upregulate (i) keratinocyte migration, (ii) endothelial cell angiogenic phenotype, (iii) fibroblast proliferation, and (iv) induction of the expression of matrix metalloproteinases, type I collagen, and tropoelastin. All of these properties could accelerate the different stages of wound repair. Elastin-derived peptides from a chemical or a proteolytic digest of insoluble elastin alone or linked to the collagen scaffold significantly improve skin wound healing and dermal regeneration in vivo in several animal models. Such a beneficial influence has been recently extended to the treatment of burn patients. In this respect, recent investigations have focused on the design of elastin-derived peptides or elastin-building blocks, as obtained from peptide chemistry or by genetic engineering, to elaborate biocompatible elastin peptides, which are considered as ideal biomaterials for "catalyzing" skin repair and regeneration following injury.

• Authors: Frank Antonicelli, Georges Bellon, Sandrine Lorimier, William Hornebeck
• Journal: Wound repair and regeneration : official publication of the Wound Healing Society [and] the European Tissue Repair Society (Wound Repair Regen) 2009 Sep-Oct Vol. 17 Issue 5 Pg. 631-8 ISSN: 1524-475X [Electronic] United States
• PMID: 19769716 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Galactosides
• Receptors, Cell Surface
• Umbelliferones
• cyclohexenoesculetin-beta-galactoside
• elastin-binding proteins
• Elastin
• NEU1 protein, human
• Neuraminidase
• Cathepsin A

Topics

• Cathepsin A (metabolism)
• Elastin (physiology)
• Galactosides (metabolism)
• Humans
• Neuraminidase (metabolism)
• Receptors, Cell Surface (metabolism)
• Regeneration (physiology)
• Skin (metabolism)
• Skin Physiological Phenomena
• Umbelliferones (metabolism)
• Wound Healing (physiology)