Cloning of a cDNA encoding cathepsin D from salamander, Hynobius leechii, and its expression in the limb regenerates.
Cathepsin D is a major lysosomal aspartic proteinase participating in the degradation or modification of intra- and extracellular matrix molecules, and its activity is known to increase in the process of tissue reorganization during the early phase of salamander limb regeneration. Here, we report the cloning of a salamander cathepsin D cDNA from Hynobius leechii and its expression profile in normal and retinoic acid (RA) treated limb regenerates. The gene expression of cathepsin D increased notably during the dedifferentiation stage and decreased gradually thereafter. Furthermore, RA that enhances dedifferentiation of regenerating salamander limb caused the elevation of cathepsin D expression both in terms of level and duration. These results suggest that cathepsin D plays important role(s) in the dedifferentiation process, and enhancement of cathepsin D expression might be closely related to RA-evoked pattern duplication.
Ju
B G
BG
Department of Life Science, Sogang University, Seoul, Korea.
Kim
W S
WS
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002402:Cathepsin D / Q000235:genetics*; D003001:Cloning, Molecular; D018076:DNA, Complementary; D005121:Extremities / Q000502:physiology; D020869:Gene Expression Profiling; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D012038:Regeneration / Q000502:physiology*; D017386:Sequence Homology, Amino Acid; D014212:Tretinoin / Q000494:pharmacology; D015854:Up-Regulation / Q000187:drug effects; D014562:Caudata / Q000235:genetics* / Q000502:physiology
D018076:DNA, Complementary; D014212:Tretinoin; D002402:Cathepsin D