title: Cathepsin L is essential for embryogenesis and development of Caenorhabditis elegans.
abstract: Cysteine proteases play critical biological roles in both intracellular and extracellular processes. We characterized Ce-cpl-1, a Caenorhabditis elegans cathepsin L-like cysteine protease. RNA interference with Ce-cpl-1 activity resulted in embryonic lethality and a transient delayed growth of larvae to egg producing adults, suggesting an essential role for cpl-1 during embryogenesis, and most likely during post-embryonic development. Cpl-1 gene (Ce-cpl-1:lacZ) is widely expressed in the intestine and hypodermal cells of transgenic worms, while the fusion protein (Ce-CPL-1::GFP) was expressed in the hypodermis, pharynx, and gonad. The CPL-1 native protein accumulates in early to late stage embryos and becomes highly concentrated in gut cells during late embryonic development. CPL-1 is also present near the periphery of the eggshell as well as in the cuticle of larval stages suggesting that it may function not only in embryogenesis but also in further development of the worm. Although the precise role of Ce-CPL-1 during embryogenesis is not yet clear it could be involved in the processing of nutrients responsible for synthesis and/or in the degradation of eggshell. Moreover, an increase in the cpl-1 mRNA is seen in the intermolt period approximately 4 h prior to each molt. During this process Ce-CPL-1 may act as a proteolytic enzyme in the processing/degradation of cuticular or other proteins. Similar localization of a related cathepsin L in the filarial nematode Onchocerca volvulus, eggshell and cuticle, suggests that some of the Ce-CPL-1 function during development may be conserved in other parasitic nematodes.
authors.affiliation: Laboratory of Molecular Parasitology, Lindsley F. Kimball Research Institute, New York Blood Center, New York, New York 10021, USA.
authors.forename: Sarwar
authors.initials: S
authors.lastname: Hashmi
authors.forename: Collette
authors.initials: C
authors.lastname: Britton
authors.forename: Jing
authors.initials: J
authors.lastname: Liu
authors.forename: David B
authors.initials: DB
authors.lastname: Guiliano
authors.forename: Yelena
authors.initials: Y
authors.lastname: Oksov
authors.forename: Sara
authors.initials: S
authors.lastname: Lustigman
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D017173:Caenorhabditis elegans / Q000196:embryology / Q000201:enzymology* / Q000254:growth & development; D056668:Cathepsin L; D002403:Cathepsins / Q000235:genetics* / Q000378:metabolism; D003546:Cysteine Endopeptidases; D004528:Egg Shell / Q000378:metabolism; D004625:Embryo, Nonmammalian / Q000502:physiology; D018507:Gene Expression Regulation, Developmental; D017930:Genes, Reporter; D008969:Molecular Sequence Data; D009024:Morphogenesis; D010957:Plasmids; D014176:Protein Biosynthesis; D012330:RNA, Double-Stranded / Q000235:genetics; D018510:RNA, Helminth / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D015183:Restriction Mapping; D020133:Reverse Transcriptase Polymerase Chain Reaction; D014170:Transformation, Genetic
chemical_list: D012330:RNA, Double-Stranded; D018510:RNA, Helminth; D011993:Recombinant Fusion Proteins; D002403:Cathepsins; D003546:Cysteine Endopeptidases; D056668:Cathepsin L