hsp70, hsp32, and grp78 are increased in thermally injured skin with and without antithrombin(human) concentrate infusion

J Burn Care Rehabil. 2000 May-Jun;21(3):213-9. doi: 10.1067/mbc.2000.105085.

Abstract

An acquired deficiency of antithrombin (AT), an anti-inflammatory protein, develops in patients with thermal injuries. Skin thermotolerance is regulated by heat shock protein (hsp) genes. hsp70, hsp32, hsp27, and glucose-regulated protein78 (grp78) were studied in burned and unburned human skin to determine whether correction of the AT deficiency modulated the intensity of expression of these proteins. Fifty-four human skin samples were prepared by Western blot analysis: 11 unburned and 22 burned control skin samples and 7 unburned and 14 burned skin samples from patients treated with AT(Human), or AT(H). The intensity of hsp32 expression in burned AT(H)-treated skin (P < .001) and in burned control skin (P < .01) was significantly increased compared with unburned control skin. The intensity of expression of hsp70 was statistically significant in burned AT(H)-treated skin compared with unburned control skin (P < .02), as was that of grp78 (P < .01). Thermally injured skin with or without AT(H) treatment had an increased expression of hsp70, hsp32, and grp78 compared with unburned control skin.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adolescent
  • Adult
  • Antithrombin III / pharmacology
  • Antithrombin III / therapeutic use*
  • Antithrombin III Deficiency / etiology
  • Antithrombin III Deficiency / physiopathology
  • Blotting, Western
  • Burns / complications
  • Burns / drug therapy
  • Burns / physiopathology*
  • Carrier Proteins / biosynthesis*
  • Endoplasmic Reticulum Chaperone BiP
  • Female
  • HSP70 Heat-Shock Proteins / biosynthesis
  • Heat-Shock Proteins / biosynthesis*
  • Humans
  • Male
  • Middle Aged
  • Molecular Chaperones / biosynthesis*

Substances

  • Carrier Proteins
  • Endoplasmic Reticulum Chaperone BiP
  • HSP70 Heat-Shock Proteins
  • HSPA5 protein, human
  • Heat-Shock Proteins
  • Molecular Chaperones
  • Antithrombin III