Expression of Cysteine Proteases in Extraembryonic Tissues during Mouse Embryogenesis

Sol‐Church, Katia; Shipley, Jonathan; Beckman, David A.; Mason, Robert W.

doi:10.1006/abbi.1999.1520

Cited by 18 publications

(11 citation statements)

References 17 publications

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“…Support for this hypothesis was found in previous reports where cysteine proteases have been shown to be involved in yolk degradation during invertebrate embryonic development (33)(34)(35). In vertebrate models the expression of active cathepsin L was significantly higher in visceral yolk sac than in placenta (36). This was consistent with a higher proteolytic activity needed in the yolk sac for the production of amino acids for protein synthesis.…”

Section: Figsupporting

confidence: 78%

Cathepsin L Is Essential for Embryogenesis and Development ofCaenorhabditis elegans

Hashmi¹,

Britton²,

Liu³

et al. 2002

Journal of Biological Chemistry

111

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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.Cysteine proteases of the papain superfamily have long been recognized for their role in intracellular and extracellular protein degradation in a range of cellular processes (1). Within the papain family, the cathepsins can be subdivided into more than 10 subfamilies on the basis of their primary sequence and enzymatic activity (2). The family includes cathepsin B, C, L, and Z, all of which contain an essential cysteine residue in their active site but differ in tissue distribution and in some enzymatic properties, such as substrate specificity and pH stability. Cathepsin B-like cysteine protease genes occur as a large multigene family in a wide range of parasitic and free-living nematodes. Several cathepsin B genes were reported to be expressed in Caenorhabditis elegans, some of which were restricted to the intestines of larval and adult transgenic worms (3-5). Interestingly, the structurally similar Hemonchus contortus (3-5) and Schistosoma mansoni (6) cathepsin B homologues were also expressed in the gut and were suggested to be potentially involved in feeding (5, 7), such as nutrient digestion. Heterologous transformation of C. elegans with an H. contortus cathepsin B gene promoter has demonstrated also conservation of the mechanisms controlling its spatial expression in free-living and parasitic nematodes (8), and therefore both enzymes were hypothesized to be not only structurally similar, but also...

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Section: Figsupporting

confidence: 78%

Cathepsin L Is Essential for Embryogenesis and Development ofCaenorhabditis elegans

Hashmi¹,

Britton²,

Liu³

et al. 2002

Journal of Biological Chemistry

111

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“…The authors stipulated that fish egg cathepsin L could be responsible for yolk reserve mobilization for nutrient supply after fertilization until first feeding. Similar studies have been performed on other vertebrates [20][21][22], in which cathepsin L is highly expressed in the visceral yolk sac of embryos. Regarding pelagic egg-spawning marine fish, however, the expression profile and proteolytic roles of embryonic cathepsin L are so far unknown.…”

Section: Resultssupporting

confidence: 74%

Differential Expression of Ovarian Cathepsins B, D and L during Oocyte Growth in Scad

Aranishi¹

2000

Journal of Reproduction and Development

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Abstract. In pelagic egg-spawning marine fish, sequential processing of a hepatically derived vitellogenin occurs concomitant with oocyte growth within the follicles. This process consists of yolk formation during early oocyte growth and yolk degradation during late oocyte growth. Since ovarian cathepsins B, D and L have been suspected of being involved in both events, the present study determines their different expression during oocyte growth in round scad Decapterus maruadsi. By adopting specific substrates and inhibitors in newly established assays, the activities of scad ovarian cathepsins B, D and L had been assessed as CA074-sensitive Z-Arg-Arg-MCA hydrolysis, pepstatinsensitive MOCAc-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys(Dnp)-Arg-NH 2 hydrolysis and Z-PhePhe-CHN 2 -sensitive Z-Phe-Arg-MCA hydrolysis, respectively. All ovarian cathepsins were expressed at the highest level in early growing oocytes. With oocyte growth, the expression of cathepsin L decreased significantly, while that of cathepsins B and D showed only marginal variation. The results indicate that highly expressed ovarian cathepsins B and D play roles in yolk degradation during late oocyte growth in scad.

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“…The majority of studies on mRNA expression of the PECS have focused on elevated expression in term placenta [10][11][12][13]36] with little information of expression in TGs. Reexamination of earlier in situ hybridization data does reveal the location of cathepsin P mRNA in a sub-population of cells on the apical surface of mouse ectoplacental cone, even though expression is higher later in gestation in the labyrinthine layer of the mature placenta [11,12].…”

Section: Discussionmentioning

confidence: 99%

Expression of Cathepsin P mRNA, Protein and Activity in the Rat Choriocarcinoma Cell Line, Rcho-1, During Giant Cell Transformation

Hassanein

Korant

et al. 2007

Placenta

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Lysosomal proteases perform critical functions in protein turnover and are essential for normal growth and development. Cathepsin P is a member of a newly discovered family of lysosomal cysteine proteases uniquely expressed in rodent placenta (PECs), and is closely related to human cathepsin L. Using the rat choriocarcinoma cell line model, Rcho-1, mRNA for the PECs cathepsins P, M, Q, R, 1, 2 was found to increase in expression during differentiation into a trophoblast giant cell phenotype. By contrast, expression of cathepsin L was not regulated. A specific enzyme assay was developed to show that activity of cathepsin P mirrored mRNA expression during differentiation. Cathepsin P protein co-localizes with cathepsin B, indicating that the enzyme probably functions in the endosomal-lysosomal compartment. This study demonstrates that the PEC genes produce functional proteases that can perform specific placental roles that are probably performed by broader specificity proteases in human placenta.

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Expression of Cysteine Proteases in Extraembryonic Tissues during Mouse Embryogenesis

Cited by 18 publications

References 17 publications

Cathepsin L Is Essential for Embryogenesis and Development ofCaenorhabditis elegans

Cathepsin L Is Essential for Embryogenesis and Development ofCaenorhabditis elegans

Differential Expression of Ovarian Cathepsins B, D and L during Oocyte Growth in Scad

Expression of Cathepsin P mRNA, Protein and Activity in the Rat Choriocarcinoma Cell Line, Rcho-1, During Giant Cell Transformation

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