title: Anteroposterior gradient of epithelial transformation during amphibian intestinal remodeling: immunohistochemical detection of intestinal fatty acid-binding protein.
abstract: To determine whether the remodeling of the well-organized intestinal epithelium during amphibian metamorphosis is regionally regulated along the anteroposterior axis of the intestine, we raised a polyclonal antibody against the Xenopus laevis intestinal fatty acid-binding protein (IFABP), which is known to be specifically expressed in intestinal absorptive cells, and examined immunohistochemically the differentiation, proliferation, and apoptosis of the epithelial cells throughout X. laevis small intestine. During pre- and prometamorphosis, IFABP-immunoreactive (ir) epithelial cells were localized only in the anterior half of the larval intestine. At the beginning of metamorphic climax, apoptotic cells detected by nick end-labeling (TUNEL) suddenly increased in number in the entire larval epithelium, concurrently with the appearance of adult epithelial primordia. Subsequently, the adult primordia in the anterior part of the intestine developed more rapidly by active cell proliferation than those in the posterior part, and replaced the larval epithelial cells earlier than those in the posterior part. IFABP-ir cells in the adult epithelium were first detectable at the tips of newly formed folds in the proximal part of the intestine. Thereafter, IFABP expression gradually progressed both in the anteroposterior direction and in the crest-trough direction of the folds. These results suggest that developmental processes of the adult epithelium in the X. laevis intestine are regionally regulated along the anteroposterior axis of the intestine, which is maintained throughout metamorphosis, and along the trough-crest axis of the epithelial folds, which is newly established during metamorphosis. Furthermore, the regional differences in IFABP expression along the anteroposterior axis of the intestine were reproduced in organ cultures in vitro. In addition, IFABP expression was first down-regulated and then reactivated in vitro when the anterior part, but not the posterior part, of the larval intestine was treated with thyroid hormone (TH) for extended periods. Therefore, it seems that, in addition to TH, an endogenous factor(s) localized in the intestine itself with an anteroposterior gradient participates in the development of the adult epithelium during amphibian metamorphosis.
authors.affiliation: Department of Histology and Neurobiology, Dokkyo University School of Medicine, Tochigi, Mibu, 321-02, Japan. i-oka@dokkyomed.ac.jp
authors.forename: A
authors.initials: A
authors.lastname: Ishizuya-Oka
authors.forename: S
authors.initials: S
authors.lastname: Ueda
authors.forename: S
authors.initials: S
authors.lastname: Damjanovski
authors.forename: Q
authors.initials: Q
authors.lastname: Li
authors.forename: V C
authors.initials: VC
authors.lastname: Liang
authors.forename: Y B
authors.initials: YB
authors.lastname: Shi
mesh_terms: D000818:Animals; D017209:Apoptosis; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D002454:Cell Differentiation; D002455:Cell Division; D015536:Down-Regulation; D004847:Epithelial Cells / Q000166:cytology / Q000378:metabolism; D004848:Epithelium / Q000254:growth & development / Q000378:metabolism; D050556:Fatty Acid-Binding Proteins; D018507:Gene Expression Regulation, Developmental; D007150:Immunohistochemistry; D007421:Intestine, Small / Q000254:growth & development* / Q000378:metabolism*; D007814:Larva / Q000254:growth & development / Q000378:metabolism; D008675:Metamorphosis, Biological; D018996:Myelin P2 Protein / Q000235:genetics / Q000378:metabolism*; D009363:Neoplasm Proteins; D009924:Organ Culture Techniques; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D029867:Xenopus Proteins; D014982:Xenopus laevis / Q000235:genetics / Q000254:growth & development* / Q000378:metabolism*
chemical_list: D002352:Carrier Proteins; D050556:Fatty Acid-Binding Proteins; D018996:Myelin P2 Protein; D009363:Neoplasm Proteins; D012333:RNA, Messenger; D029867:Xenopus Proteins; C493314:intestinal fatty acid binding protein, Xenopus