Literature DB >> 10492132

Expression of SPARC (secreted protein, acidic and rich in cysteine) in healing intestinal anastomoses and short bowel syndrome in rats.

P Puolakkainen1, M Reed, P Vento, E H Sage, T Kiviluoto, E Kivilaakso.   

Abstract

Due to the proposed functions in soft tissue repair, we evaluated the spatial and temporal distribution of SPARC, a counteradhesive, matricellular glycoprotein in healing intestinal anastomoses and short bowel syndrome (SBS) in rats. Intestinal anastomoses were performed in the jejunum of male Wistar rats. SBS was induced by resecting 70% of the small bowel. In situ hybridization was performed to localize SPARC mRNA and immunohistochemical studies for locating the SPARC protein. The granulation tissue in the anastomotic area exhibited immunoreactivity for SPARC at all time points. The level of expression was maximal at seven to nine days. Endothelial cells of capillaries, smooth muscle cells, fibroblastic cells, and macrophages, as well as mesothelial cells on the serosal surface, were stained. The immunoreactivity was mostly intracellular. SPARC mRNA transcripts were localized to the edges of the anastomotic area at days 1 and 4 and on the newly formed granulation tissue later. The expression of SPARC mRNA was maximal at seven days and decreased thereafter. Both in normal controls and in SBS, SPARC was expressed in endothelial cells of submucosal capillaries and in smooth muscle cells but not in epithelium. Based on the restricted temporal and spatial distribution during the healing of intestinal anastomoses and in SBS we propose that SPARC plays a significant role in intestinal repair and adaptation.

Entities:  

Mesh:

Substances:

Year:  1999        PMID: 10492132     DOI: 10.1023/a:1026602708263

Source DB:  PubMed          Journal:  Dig Dis Sci        ISSN: 0163-2116            Impact factor:   3.199


  40 in total

Review 1.  Extracellular proteins that modulate cell-matrix interactions. SPARC, tenascin, and thrombospondin.

Authors:  E H Sage; P Bornstein
Journal:  J Biol Chem       Date:  1991-08-15       Impact factor: 5.157

2.  Neutrophil-dependent decrease in early wound margin strength.

Authors:  T Jonsson; H Högström
Journal:  Arch Surg       Date:  1991-11

3.  Accelerated healing of incisional wounds in rats induced by transforming growth factor-beta.

Authors:  T A Mustoe; G F Pierce; A Thomason; P Gramates; M B Sporn; T F Deuel
Journal:  Science       Date:  1987-09-11       Impact factor: 47.728

Review 4.  The biology of SPARC, a protein that modulates cell-matrix interactions.

Authors:  T F Lane; E H Sage
Journal:  FASEB J       Date:  1994-02       Impact factor: 5.191

5.  Regulation of the expression of a secreted acidic protein rich in cysteine (SPARC) in human fibroblasts by transforming growth factor beta. Comparison of transcriptional and post-transcriptional control with fibronectin and type I collagen.

Authors:  J L Wrana; C M Overall; J Sodek
Journal:  Eur J Biochem       Date:  1991-04-23

6.  Expression of SPARC in normal and fibrotic livers.

Authors:  E Frizell; S L Liu; A Abraham; I Ozaki; M Eghbali; E H Sage; M A Zern
Journal:  Hepatology       Date:  1995-03       Impact factor: 17.425

7.  Distribution of the calcium-binding protein SPARC in tissues of embryonic and adult mice.

Authors:  H Sage; R B Vernon; J Decker; S Funk; M L Iruela-Arispe
Journal:  J Histochem Cytochem       Date:  1989-06       Impact factor: 2.479

8.  TGF-beta 1 induces the expression of type I collagen and SPARC, and enhances contraction of collagen gels, by fibroblasts from young and aged donors.

Authors:  M J Reed; R B Vernon; I B Abrass; E H Sage
Journal:  J Cell Physiol       Date:  1994-01       Impact factor: 6.384

9.  The extracellular glycoprotein SPARC interacts with platelet-derived growth factor (PDGF)-AB and -BB and inhibits the binding of PDGF to its receptors.

Authors:  E W Raines; T F Lane; M L Iruela-Arispe; R Ross; E H Sage
Journal:  Proc Natl Acad Sci U S A       Date:  1992-02-15       Impact factor: 11.205

Review 10.  Intestinal adaptation in short-bowel syndrome.

Authors:  M J Lentze
Journal:  Eur J Pediatr       Date:  1989-01       Impact factor: 3.183

View more
  5 in total

Review 1.  Intestinal mucosal adaptation.

Authors:  Laurie Drozdowski; Alan B R Thomson
Journal:  World J Gastroenterol       Date:  2006-08-07       Impact factor: 5.742

Review 2.  Morphological, kinetic, membrane biochemical and genetic aspects of intestinal enteroplasticity.

Authors:  Laurie A Drozdowski; M Tom Clandinin; Alan B R Thomson
Journal:  World J Gastroenterol       Date:  2009-02-21       Impact factor: 5.742

3.  Indomethacin and retinoic acid modify mouse intestinal inflammation and fibrosis: a role for SPARC.

Authors:  Borut Klopcic; Amber Appelbee; Warren Raye; Frances Lloyd; James C I Jooste; Cynthia Heather Forrest; Ian Craig Lawrance
Journal:  Dig Dis Sci       Date:  2008-06       Impact factor: 3.199

4.  Compromised production of extracellular matrix in mice lacking secreted protein, acidic and rich in cysteine (SPARC) leads to a reduced foreign body reaction to implanted biomaterials.

Authors:  Pauli Puolakkainen; Amy D Bradshaw; Themistoklis R Kyriakides; May Reed; Rolf Brekken; Thomas Wight; Paul Bornstein; Buddy Ratner; E Helene Sage
Journal:  Am J Pathol       Date:  2003-02       Impact factor: 4.307

Review 5.  Small bowel review: Diseases of the small intestine.

Authors:  Alan B R Thomson; Laurie Drozdowski; Claudiu Iordache; Ben K A Thomson; Severine Vermeire; M Tom Clandinin; Gary Wild
Journal:  Dig Dis Sci       Date:  2003-08       Impact factor: 3.487

  5 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.