Abstract
Upon release from keratinocytes, 14-3-3 sigma (also known as stratifin) acts on the dermal fibroblast and modulates its production of extracellular matrix proteins. Subsequent to the recent identification as a receptor responsible for stratifin-mediated matrix turnover in dermal fibroblasts, aminopeptidase N has been implicated in the regulation of epidermal-dermal communication and expression of key matrix proteases and adhesion molecules. In light of the growing importance of aminopeptidase N in modulation of the fibroblast phenotype, the present study evaluates the potential of targeting the ectoenzyme in cutaneous repair, and demonstrates that neutralization of aminopeptidase N led to acceleration of wound closure. This was attributed to at least in part an increase of collagen deposition and fibroblast contractility in the granulation tissue. These findings confirmed the important role of aminopeptidase N in post-injury tissue remodeling and wound contraction.
Publication types
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Research Support, Non-U.S. Gov't
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Retracted Publication
MeSH terms
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Actins / metabolism
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Administration, Topical
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Animals
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Antibodies, Neutralizing / administration & dosage*
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CD13 Antigens / antagonists & inhibitors*
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CD13 Antigens / immunology
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CD13 Antigens / metabolism
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Cells, Cultured
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Collagen / metabolism
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Enzyme Activation
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Female
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Humans
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Imidazoles / pharmacology
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MAP Kinase Signaling System
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Male
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Mice
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Mice, Inbred BALB C
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Molecular Targeted Therapy
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Phosphorylation
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Protein Processing, Post-Translational / drug effects
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Pyridines / pharmacology
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Skin / drug effects*
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Skin / metabolism
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Skin / pathology
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Skin / physiopathology
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Wound Healing / drug effects*
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p38 Mitogen-Activated Protein Kinases / antagonists & inhibitors
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p38 Mitogen-Activated Protein Kinases / metabolism
Substances
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Acta2 protein, mouse
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Actins
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Antibodies, Neutralizing
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Imidazoles
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Pyridines
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Collagen
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p38 Mitogen-Activated Protein Kinases
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CD13 Antigens
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4-(4-fluorophenyl)-2-(4-hydroxyphenyl)-5-(4-pyridyl)imidazole