hch-1, a gene required for normal hatching and normal migration of a neuroblast in C. elegans, encodes a protein related to TOLLOID and BMP-1.

Hishida, Ryuichi; Ishihara, Takeshi; Kondo, Kazunori; Izui, Katsura

doi:10.1002/j.1460-2075.1996.tb00786.x

Cited by 59 publications

(48 citation statements)

References 60 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Another astacin-like protein (HCH-1) was shown to be inization of the egg-derived astacin family member, named AEA. A more comprehensive investigation considering other tissues volved in the hatching process of the nematode Caenorhabditis elegans [23], but unlike the above-mentioned proteins it has an of the adult crayfish and animals under different physiological conditions has not been carried out. To a certain degree our additional function in cell differentiation.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Cloning and characterization of a cDNA coding for Astacus embryonic astacin, a member of the astacin family of metalloproteases from the crayfish Astacus astacus

Geier¹,

Zwilling²

1998

European Journal of Biochemistry

View full text Add to dashboard Cite

The astacin family of zinc endopeptidases was named after the digestive enzyme astacin isolated from the crayfish Astacus astacus. Employing a reverse transcription/PCR strategy with degenerate oligonucleotide primers specific for two signature seqences of the astacin family, we have isolated a 1602-bp cDNA from embryos of developing A. astacus eggs, which was designated Astacus embryonic astacin (AEA). This cDNA was found to code for an astacin-like protease domain which accounts for the N-terminal half of the predicted protein. The C-terminal half mainly consists of two complement subcomponent C1r/ C1s/embryonic sea urchin protein Uegf/bone morphogenetic protein 1 (CUB) domains. The metalloprotease domain displays an amino acid sequence identity of 42% with astacin. A higher sequence similarity was found to astacin family members that act as hatching enzymes in different species, e.g. chorioallantoic membrane protein 1 (CAM-1 ; from quail) and Xenopus hatching enzyme (formerly UVS.2), both of which show 54% identity, and high and low choriolytic enzymes (HCE and LCE) from the teleost Oryzias latipes (52% and 48% identity, respectively). A relationship to astacin-like hatching enzymes is further supported by a phylogenetic analysis of the protease domains. Expression of AEA mRNA in developing embryos was found to be restricted to unhatched juveniles (larvae) during the last 8 days before hatching. AEA transcripts could not be detected in various tissues of adult animals or in eggs and embryos from an earlier developmental stage. AEA expression starts about 8 days prior to hatching, followed by a strong (18-fold) induction with a maximum at day 4 before hatching. Newly hatched juveniles were found not to express the AEA mRNA.Keywords : Astacus astacus; astacin; metalloprotease; gene expression ; hatching enzyme.The astacin family of zinc endopeptidases [1Ϫ3] was named genetic organization [7], represents the only astacin family member with a purely digestive function, contributing to the deafter the digestive enzyme astacin, isolated from the stomachlike cardia of the freshwater crayfish Astacus astacus [4]. As-gradation of protein diet in the crayfish stomach. All other members of this protease family may be classified by their function tacin family members are characterized by the consensus sequences HEXXHXXGFXHEXXRXDRD, containing the zinc-into one of three groups. The membrane-bound meprins [8,9] found in the small intestine and kidney of mammals are believed binding motif, and SXMHY, the so-called Met turn. These highly conserved regions are part of a 200-amino-acid sequence, to be involved in the processing of biologically active peptides.A second class of astacins comprises morphogenetically active which constitutes the entire mature crayfish astacin. All other astacin family members [with the exception of the fish hatching proteins found in many vertebrate and invertebrate species, e.g. BMP-1 [10, 11] or tolloid [12, 13]. Astacin-like enzymes have enzymes high and low choriolytic enzymes (HCE and LCE)] [...

show abstract

Section: Resultsmentioning

confidence: 99%

“…HCH-1 from C. elegans is not contained in the hatching en- the hatching process, it seems to be multifunctional and acts also 481. in the control of cell migration [23]. In contrast to all other as-13.…”

mentioning

confidence: 99%

Cloning and characterization of a cDNA coding for Astacus embryonic astacin, a member of the astacin family of metalloproteases from the crayfish Astacus astacus

Geier¹,

Zwilling²

1998

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…A degradative function for NAS-37 is consistent with the known function of the related class V Astacin metalloprotease nas-34. nas-34 is also known as hch-1, because mutations in this gene have been found to cause delayed hatching from the eggshell (Hishida et al, 1996). Because these mutations can be suppressed by exogenously applied proteinases, it has been suggested that this gene encodes a C. elegans enzyme responsible for degrading eggshell proteins at hatching.…”

Section: Discussionmentioning

confidence: 99%

A conserved metalloprotease mediates ecdysis inCaenorhabditis elegans

et al. 2004

View full text Add to dashboard Cite

Molting is required for progression between larval stages in the life cycle of nematodes. We have identified four mutant alleles of a Caenorhabditis elegans metalloprotease gene, nas-37, that cause incomplete ecdysis. At each molt the cuticle fails to open sufficiently at the anterior end and the partially shed cuticle is dragged behind the animal. The gene is expressed in hypodermal cells 4 hours before ecdysis during all larval stages. The NAS-37 protein accumulates in the anterior cuticle and is shed in the cuticle after ecdysis. This pattern of protein accumulation places NAS-37 in the right place and at the right time to degrade the cuticle to facilitate ecdysis. The nas-37 gene has orthologs in other nematode species,including parasitic nematodes, and they undergo a similar shedding process. For example, Haemonchus contortus molts by digesting a ring of cuticle at the tip of the nose. Incubating Haemonchus larvae in extracted exsheathing fluids causes a refractile ring of digested cuticle to form at the tip of the nose. When Haemonchus cuticles are incubated with purified NAS-37, a similar refractile ring forms. NAS-37 degradation of the Haemonchus cuticle suggests that the metalloproteases and the cuticle substrates involved in exsheathment of parasitic nematodes are conserved in free-living nematodes.

show abstract

“…There are 39 Nematode AStacin (NAS) metalloproteases in the free-living nematode, C. elegans, divided into 6 subgroups (I to VI) that correlate with the functionally significant C-terminal domain structure (Möhrlen et al 2003). The subgroup V enzymes (NAS-33 to NAS-38) have been identified to be essential for the correct development of C. elegans, in that worms mutant in nas-34 display a delayed hatching phenotype (Hishida et al 1996), those mutant in nas-35 (a.k.a. dpy-31) have a dumpy appearance, indicating a specific role in the proper formation of the cuticle (Novelli et al 2004), and worms lacking nas-36 and nas-37, but particularly nas-37, show defects in the shedding of the cuticle, indicating a specific role for these enzymes in cuticle ecdysis (Davis et al 2004;Suzuki et al 2004).…”

mentioning

confidence: 99%

The astacin metalloprotease moulting enzyme NAS-36 is required for normal cuticle ecdysis in free-living and parasitic nematodes

et al. 2010

View full text Add to dashboard Cite

S U M M A R YNematodes represent one of the most abundant and species-rich groups of animals on the planet, with parasitic species causing chronic, debilitating infections in both livestock and humans worldwide. The prevalence and success of the nematodes is a direct consequence of the exceptionally protective properties of their cuticle. The synthesis of this cuticle is a complex multi-step process, which is repeated 4 times from hatchling to adult and has been investigated in detail in the freeliving nematode, Caenorhabditis elegans. This process is known as moulting and involves numerous enzymes in the synthesis and degradation of the collagenous matrix. The nas-36 and nas-37 genes in C. elegans encode functionally conserved enzymes of the astacin metalloprotease family which, when mutated, result in a phenotype associated with the late-stage moulting defects, namely the inability to remove the preceding cuticle. Extensive genome searches in the gastrointestinal nematode of sheep, Haemonchus contortus, and in the filarial nematode of humans, Brugia malayi, identified NAS-36 but not NAS-37 homologues †. Significantly, the nas-36 gene from B. malayi could successfully complement the moult defects associated with C. elegans nas-36, nas-37 and nas-36/nas-37 double mutants, suggesting a conserved function for NAS-36 between these diverse nematode species. This conservation between species was further indicated when the recombinant enzymes demonstrated a similar range of inhibitable metalloprotease activities.

show abstract

hch-1, a gene required for normal hatching and normal migration of a neuroblast in C. elegans, encodes a protein related to TOLLOID and BMP-1.

Cited by 59 publications

References 60 publications

Cloning and characterization of a cDNA coding for Astacus embryonic astacin, a member of the astacin family of metalloproteases from the crayfish Astacus astacus

Cloning and characterization of a cDNA coding for Astacus embryonic astacin, a member of the astacin family of metalloproteases from the crayfish Astacus astacus

A conserved metalloprotease mediates ecdysis inCaenorhabditis elegans

The astacin metalloprotease moulting enzyme NAS-36 is required for normal cuticle ecdysis in free-living and parasitic nematodes

Contact Info

Product

Resources

About