Heat Shock Proteins in Diabetes and Wound Healing

Authors: Atalay, Mustafa; Oksala, Niku; Lappalainen, Jani; Laaksonen, David E.; Sen, Chandan K.; Roy, Sashwati

Source: Current Protein and Peptide Science, Volume 10, Number 1, February 2009 , pp. 85-95(11)

Publisher: Bentham Science Publishers

Buy & download fulltext article:

OR

Price: $63.10 plus tax (Refund Policy)

Abstract:

The heat shock proteins (HSPs), originally identified as heat-inducible gene products, are a highly conserved family of proteins that respond to a wide variety of stress. Although HSPs are among the most abundant intracellular proteins, they are expressed at low levels under normal physiological conditions, and show marked induction in response to various stressors. HSPs function primarily as molecular chaperones, facilitating the folding of other cellular proteins, preventing protein aggregation, or targeting improperly folded proteins to specific pathways for degradation. By modulating inflammation, wound debris clearance, cell proliferation, migration and collagen synthesis, HSPs are essential for normal wound healing of the skin. In this review, our goal is to discuss the role and clinical implications of HSP with respect to skin wound healing and diabetes. The numerous defects in the function of HSPs associated with diabetes could contribute to the commonly observed complications and delayed wound healing in diabetics. Several physical, pharmacological and genetic approaches may be considered to address HSP-directed therapies both in the laboratory and in the clinics.

Keywords: Heat shock proteins; wound healing; tissue protection; diabetes

Document Type: Research article

DOI: http://dx.doi.org/10.2174/138920309787315202

Publication date: 2009-02-01

Related content

Tools

Key

Free Content
Free content
New Content
New content
Open Access Content
Open access content
Subscribed Content
Subscribed content
Free Trial Content
Free trial content

Text size:

A | A | A | A
Share this item with others: These icons link to social bookmarking sites where readers can share and discover new web pages. print icon Print this page