title: Enhanced expression of heat shock protein 47 in rat model of peritoneal fibrosis.
abstract: OBJECTIVE
  Peritoneal fibrosis is one of the serious complications of continuous ambulatory peritoneal dialysis therapy and is characterized by collagen accumulation. Heat shock protein 47 (HSP-47) is a collagen-specific molecular chaperon and is closely associated with collagen synthesis; however, the involvement of HSP-47 in the progression of peritoneal fibrosis is not fully understood.
  
  
  METHODS
  To examine the serial pathological alterations caused by peritoneal fibrosis, we made an experimental model of peritoneal fibrosis by daily intraperitoneal injection of chlorhexidine gluconate (CG) in rats for 28 days and examined the expression of HSP-47 together with that of types I and III collagen, alpha-smooth muscle actin (aSMA), and ED-1 (a marker for macrophages) using immunohistochemistry. Rats treated with saline containing 15% ethanol were used as the control group.
  
  
  RESULTS
  In the control group, the peritoneal tissue was slightly thickened and HSP-47 was expressed in the peritoneum at day 28. In the CG group, the peritoneal tissue serially became thickened and fibrotic. The expression of HSP-47 was evident in mesothelial cells and submesothelial connective tissue after day 7 of treatment with CG, and increased thereafter. The expression of types I and III collagen and aSMA was proportionally strengthened during our experiments. ED-1-positive cells were present in thickened areas with abundant proliferation of collagen fiber. The number of cells positive for ED-1 increased gradually and reached a maximum at day 21.
  
  
  CONCLUSIONS
  Our results indicate that, in a rat experimental model of peritoneal fibrosis, the expression of HSP-47 is associated with the progression of peritoneal fibrosis.
authors.affiliation: Second Department of Internal Medicine, Nagasaki University School of Medicine, Nagasaki, Japan.
authors.forename: Yoko
authors.initials: Y
authors.lastname: Mishima
authors.forename: Masanobu
authors.initials: M
authors.lastname: Miyazaki
authors.forename: Katsushige
authors.initials: K
authors.lastname: Abe
authors.forename: Yoshiyuki
authors.initials: Y
authors.lastname: Ozono
authors.forename: Kei
authors.initials: K
authors.lastname: Shioshita
authors.forename: Zhiyin
authors.initials: Z
authors.lastname: Xia
authors.forename: Takashi
authors.initials: T
authors.lastname: Harada
authors.forename: Takashi
authors.initials: T
authors.lastname: Taguchi
authors.forename: Takehiko
authors.initials: T
authors.lastname: Koji
authors.forename: Shigeru
authors.initials: S
authors.lastname: Kohno
mesh_terms: D000818:Animals; D002710:Chlorhexidine / Q000031:analogs & derivatives*; D018450:Disease Progression; D024022:Fibrillar Collagens / Q000378:metabolism; D005355:Fibrosis / Q000209:etiology* / Q000378:metabolism*; D050958:HSP47 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000096:biosynthesis*; D007150:Immunohistochemistry; D008297:Male; D023421:Models, Animal; D010529:Peritoneal Cavity / Q000473:pathology* / Q000503:physiopathology*; D010531:Peritoneal Dialysis, Continuous Ambulatory / Q000009:adverse effects*; D051381:Rats; D017208:Rats, Wistar
chemical_list: D024022:Fibrillar Collagens; D050958:HSP47 Heat-Shock Proteins; D006360:Heat-Shock Proteins; C494662:Serpinh1 protein, rat; C010882:chlorhexidine gluconate; D002710:Chlorhexidine