title: Restitution at the cellular level: regulation of the migrating phenotype.
abstract: Intestinal epithelial cells migrating across a mucosal defect are generally described as dedifferentiated, a term that suggests a loss of regulatory biology. Since cell biology may be more readily studied in established cell lines than in vivo, a model is developed using the human Caco-2 intestinal epithelial cell migrating across matrix proteins. This resembles in vivo models of mucosal healing in its sheet migration and loss of the brush border enzymes, which are conventional markers for intestinal epithelial differentiation. Immunohistochemical studies of migrating Caco-2 cells suggest, however, that the rearrangements of cytoskeletal, cell-cell and cell-matrix proteins during migration are not random but seem adapted to the migratory state. Indeed, Caco-2 migration may be substantially regulated by a variety of physiologic and pharmacologic stimuli and differentiation, measured by the specific activity of the intestinal epithelial brush border enzymes alkaline phosphatase and dipeptidyl dipeptidase, may be independently pharmacologically programmed during the stimulation or inhibition of cell motility.
authors.affiliation: Department of Surgery, Yale University School of Medicine, New Haven, Connecticut 06520-8062, USA. basson.marc_d.@west.haven.va.gov
authors.forename: M D
authors.initials: MD
authors.lastname: Basson
authors.forename: Z
authors.initials: Z
authors.lastname: Rashid
authors.forename: G A
authors.initials: GA
authors.lastname: Turowski
authors.forename: A B
authors.initials: AB
authors.lastname: West
authors.forename: N J
authors.initials: NJ
authors.lastname: Emenaker
authors.forename: S A
authors.initials: SA
authors.lastname: Sgambati
authors.forename: F
authors.initials: F
authors.lastname: Hong
authors.forename: D M
authors.initials: DM
authors.lastname: Perdikis
authors.forename: S
authors.initials: S
authors.lastname: Datta
authors.forename: J A
authors.initials: JA
authors.lastname: Madri
mesh_terms: D000199:Actins / Q000378:metabolism; D000469:Alkaline Phosphatase / Q000187:drug effects / Q000378:metabolism; D000818:Animals; D002454:Cell Differentiation / Q000187:drug effects; D002465:Cell Movement / Q000187:drug effects / Q000502:physiology*; D002478:Cells, Cultured; D003094:Collagen / Q000737:chemistry / Q000378:metabolism; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000187:drug effects / Q000378:metabolism; D004766:Enterostomy; D004815:Epidermal Growth Factor / Q000494:pharmacology; D004847:Epithelial Cells; D004848:Epithelium / Q000473:pathology / Q000648:ultrastructure; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007413:Intestinal Mucosa / Q000166:cytology / Q000473:pathology*; D007422:Intestines / Q000166:cytology* / Q000648:ultrastructure; D007583:Jejunum / Q000473:pathology / Q000601:surgery; D007797:Laminin / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D008871:Microvilli / Q000187:drug effects / Q000201:enzymology*; D010418:Pentagastrin / Q000494:pharmacology; D019894:Peptide YY; D010455:Peptides / Q000494:pharmacology; D010750:Phosphoproteins / Q000378:metabolism; D051381:Rats; D017207:Rats, Sprague-Dawley; D062826:Zonula Occludens-1 Protein
chemical_list: D000199:Actins; D007797:Laminin; D008565:Membrane Proteins; D010455:Peptides; D010750:Phosphoproteins; C569042:TJP1 protein, human; C569044:Tjp1 protein, rat; D062826:Zonula Occludens-1 Protein; D019894:Peptide YY; D004815:Epidermal Growth Factor; D003094:Collagen; D000469:Alkaline Phosphatase; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; D010418:Pentagastrin