Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2004-2-9
pubmed:abstractText
We have analyzed the expression and function of Cecpz-1, a Caenorhabditis elegans cathepsin Z-like cysteine protease gene, during development of the worm. The cpz-1 gene is expressed in various hypodermal cells of all developmental stages and is specifically expressed in the gonads and the pharynx of adult worms. Disruption of cpz-1 function by RNA interference or cpz-1(ok497) deletion mutant suggests that cpz-1 has a role in the molting pathways. The presence of the native CPZ-1 protein in the hypodermis/cuticle of larval and adult stages and along the length of the pharynx of adult worms, as well as the cyclic expression of the transcript during larval development, supports such function. We hypothesize that the CPZ-1 enzyme functions directly as a proteolytic enzyme degrading cuticular proteins before ecdysis and/or indirectly by processing other proteins such as proenzymes and/or other proteins that have an essential role during molting. Notably, an impressive level of the CPZ-1 native protein is present in both the new and the old cuticles during larval molting, in particular in the regions that are degraded prior to shedding and ecdysis. The similar localization of the related Onchocerca volvulus cathepsin Z protein suggests that the function of CPZ-1 during molting might be conserved in other nematodes. Based on the cpz-1 RNA interference and cpz-1 (ok497) deletion mutant phenotypes, it appears that cpz-1 have additional roles during morphogenesis. Deletion of cpz-1 coding sequence or inhibition of cpz-1 function by RNA interference also caused morphological defects in the head or tail region of larvae, improperly developed gonad in adult worms and embryonic lethality. The CPZ-1 native protein in these affected regions may have a role in the cuticular and the basement membrane extracellular matrix assembly process. The present findings have defined a critical role for cathepsin Z in nematode biology.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
279
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6035-45
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:14630920-Amino Acid Sequence, pubmed-meshheading:14630920-Animals, pubmed-meshheading:14630920-Animals, Genetically Modified, pubmed-meshheading:14630920-Base Sequence, pubmed-meshheading:14630920-Caenorhabditis elegans, pubmed-meshheading:14630920-Cathepsin K, pubmed-meshheading:14630920-Cathepsins, pubmed-meshheading:14630920-DNA, Complementary, pubmed-meshheading:14630920-Gene Deletion, pubmed-meshheading:14630920-Gene Expression Regulation, Developmental, pubmed-meshheading:14630920-Genes, Reporter, pubmed-meshheading:14630920-Gonads, pubmed-meshheading:14630920-Microscopy, Fluorescence, pubmed-meshheading:14630920-Microscopy, Immunoelectron, pubmed-meshheading:14630920-Models, Genetic, pubmed-meshheading:14630920-Molecular Sequence Data, pubmed-meshheading:14630920-Mutation, pubmed-meshheading:14630920-Peptides, pubmed-meshheading:14630920-Pharynx, pubmed-meshheading:14630920-Phenotype, pubmed-meshheading:14630920-Promoter Regions, Genetic, pubmed-meshheading:14630920-RNA, Double-Stranded, pubmed-meshheading:14630920-RNA, Messenger, pubmed-meshheading:14630920-RNA Interference, pubmed-meshheading:14630920-Recombinant Proteins, pubmed-meshheading:14630920-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:14630920-Sequence Homology, Amino Acid, pubmed-meshheading:14630920-Time Factors, pubmed-meshheading:14630920-Transgenes
pubmed:year
2004
pubmed:articleTitle
The Caenorhabditis elegans cathepsin Z-like cysteine protease, Ce-CPZ-1, has a multifunctional role during the worms' development.
pubmed:affiliation
Laboratory of Molecular Parasitology, Lindsley F. Kimball Research Institute, New York Blood Center, New York 10021, USA. shashmi@nybloodcenter.org
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't