title: Aminopeptidases function as endocytic receptors in the trophotaenial placenta of the goodeid fish, Ameca splendens (Teleostei: Atheriniformes).
abstract: Viviparity in goodeid teleosts is characterized by the elaboration of trophotaeniae, extraembryonic proctodaeal appendages facilitating maternal-embryonic nutrient transfer. The trophotaenial absorptive cells (TACs) express aminopeptidases (APs) such as APA, APN, gamma-glutamyltransferase (gamma-GT), dipeptidyl aminopeptidase (DAP) IV, and neutral endopeptidase (NEP) as inferred from the results of cleavage experiments with, respectively, Glu-alpha-(4M beta NA), Ala-(4M beta NA), Glu-gamma-(4M beta NA), Gly-Pro-(4M beta NA), and Gl-(Ala)(3)-(4M beta NA). Enzyme reaction product was localized to the apical and basolateral plasma membrane as well as to some intracellular compartments. In the accompanying report (Schindler, 2003) evidence is presented that the trophotaeniae of Ameca splendens embryos randomly, yet specifically, bind and ingest proteins as well as certain copolymers of amino acids. Present results demonstrate that endocytosis is significantly inhibitable by unspecific proteinase inhibitors, such as diisopropylphosphorofluoride, phenylmethanesulfonylfluoride, antipain, 1.10-phenanthroline, and dithiothreitol. The specific microbial AP inhibitors amastatin, bestatin, and phosphoramidon suppressed protein binding to TACs more effectively when added in combination than did either agent alone. Moreover, in the presence of 4M beta NA assay substrates of APs the capability of TACs to bind proteins was significantly reduced. Conversely, the rate at which 4M beta NA substrates were cleaved by trophotaenial APs was modified in the presence of proteins. Depending on protein concentrations the AP-catalyzed reactions either decreased or increased in velocity. Analysis of the enzyme kinetics by methods of linear transformation suggests that proteins bind to APs competitively, thereby adopting the role of enzyme inhibitors. On the other hand, protein binding to APs appears to be a signal to translocate enzymes from an internal pool to the surface membrane. In the presence of primaquine, the rate of AP-catalyzed cleavage of 4M beta NA substrates was significantly reduced. That can be put down to the fact that weak bases disrupt the recycling of endocytosed membrane constituents. In conclusion, there is evidence that APs in the trophotaenial placenta of A. splendens function as scavenger receptors mediating in the delivery of embryotrophic proteins for lysosomal degradation.
authors.affiliation: Institut für Anatomie, Universität Regensburg, Regensburg, Germany. jfs@ob.kamp.net
authors.forename: Joachim F
authors.initials: JF
authors.lastname: Schindler
mesh_terms: D000626:Aminopeptidases / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D004064:Digestive System / Q000166:cytology / Q000196:embryology / Q000201:enzymology*; D004625:Embryo, Nonmammalian / Q000166:cytology / Q000201:enzymology; D004705:Endocytosis / Q000502:physiology*; D020895:Enterocytes / Q000166:cytology / Q000201:enzymology*; D005260:Female; D005399:Fishes / Q000196:embryology* / Q000378:metabolism*; D008247:Lysosomes / Q000201:enzymology; D008431:Maternal-Fetal Exchange / Q000502:physiology; D010929:Placentation / Q000502:physiology; D011247:Pregnancy; D021381:Protein Transport / Q000502:physiology; D014327:Trophoblasts / Q000166:cytology / Q000201:enzymology
chemical_list: D000626:Aminopeptidases