title: Morphological data indicate a stress response at the oral border of strangulated small intestine in horses.
abstract: Strangulation colic often leads to surgery. We aimed to document the molecular response in the non-resected intestine in these horses using quantitative Western blot analysis, and immunohistochemistry. The expression of hypoxia-inducible factor 1-alpha (HIF1α) was investigated together with two molecular pathways initiated after protein destruction: proteasome degradation via ubiquitin chain formation and protein restoration via molecular chaperones such as inducible heat shock protein 70 (HSP70). In addition, the expression of c-fos and c-jun could indicate an early proinflammatory response. Ubiquitin, HSP70, c-jun and c-fos protein levels did not differ between the control and colic samples nor were they related to the clinical outcome in case of strangulation colic. However, the immunohistochemical distribution of several of these proteins (ubiquitin, HSP70 and c-jun) differed significantly between colic and control samples. The elevated presence of ubiquitin in the enterocytes' nucleus, of HSP70 in the smooth muscle cells' nucleus and of c-jun in enteric neurons suggest protective and degenerative pathways are activated in the apparently healthy non-resected tissue in case of strangulation obstruction, perhaps providing a molecular and morphological basis for the development of complications like post-operative ileus.
authors.affiliation: Laboratory of Veterinary Anatomy, University of Antwerp, Universiteitsplein 1, 2610 Antwerp, Belgium.
authors.forename: K
authors.initials: K
authors.lastname: De Ceulaer
authors.forename: C
authors.initials: C
authors.lastname: Delesalle
authors.forename: R
authors.initials: R
authors.lastname: Van Elzen
authors.forename: L
authors.initials: L
authors.lastname: Van Brantegem
authors.forename: A
authors.initials: A
authors.lastname: Weyns
authors.forename: C
authors.initials: C
authors.lastname: Van Ginneken
mesh_terms: D000818:Animals; D001706:Biopsy / Q000662:veterinary; D015153:Blotting, Western / Q000662:veterinary; D003085:Colic / Q000378:metabolism / Q000473:pathology / Q000662:veterinary*; D004268:DNA-Binding Proteins / Q000378:metabolism; D017615:Enteric Nervous System / Q000378:metabolism / Q000473:pathology / Q000648:ultrastructure; D020895:Enterocytes / Q000378:metabolism / Q000473:pathology* / Q000648:ultrastructure; D005260:Female; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism; D006734:Horse Diseases / Q000378:metabolism / Q000473:pathology*; D006736:Horses; D045823:Ileus / Q000209:etiology / Q000662:veterinary; D007150:Immunohistochemistry / Q000662:veterinary; D007410:Intestinal Diseases / Q000378:metabolism / Q000473:pathology / Q000662:veterinary*; D007421:Intestine, Small / Q000378:metabolism / Q000473:pathology*; D008297:Male; D009130:Muscle, Smooth / Q000378:metabolism / Q000473:pathology / Q000648:ultrastructure; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D013312:Stress, Physiological; D025801:Ubiquitin / Q000378:metabolism
chemical_list: D004268:DNA-Binding Proteins; D018840:HSP70 Heat-Shock Proteins; D025801:Ubiquitin; D046988:Proteasome Endopeptidase Complex