Effects on properties of a thiol protease from <i>Xenopus</i> embryos of changes in substrate and assay conditions.

Miyata, Shogo

doi:10.1006/cbir.1995.1076

Cited by 8 publications

(1 citation statement)

References 9 publications

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“…We found Mn-CL2 mRNA signals were stronger in stages II and III which is well distributed in the nucleus and around yolk. cathepsin L was reported to be distributed around the cytoplasm and yolk granules in Xenopus ( 34 ) which was consistent with the results of this study. All the results indicated that as the lysosome protein, Mn-CL2 was produced in hepatopancreas and played a key role in ovarian maturation.…”

Section: Discussionsupporting

confidence: 93%

Molecular Characterization of a Novel Cathepsin L in Macrobrachium nipponense and Its Function in Ovary Maturation

et al. 2022

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Cathepsin L genes, which belonged to cysteine proteases, were a series of multifunctional protease and played important roles in a lot of pathological and physiological processes. In this study, we analyzed the characteristics a cathepsin L (named Mn-CL2) in the female oriental river prawn, Macrobrachium nipponense which was involved in ovary maturation. The Mn-CL2 was1,582 bp in length, including a 978 bp open reading frame that encoded 326 amino acids. The Mn-CL2 was classified into the cathepsin L group by phylogenetic analysis. Real-time PCR (qPCR) analysis indicated that Mn-CL2 was highly expressed in the hepatopancreas and ovaries of female prawns. During the different ovarian stages, Mn-CL2 expression in the hepatopancreas and ovaries peaked before ovarian maturation. In situ hybridization studies revealed that Mn-CL2 was localized in the oocyte of the ovary. Injection of Mn-CL2 dsRNA significantly reduced the expression of vitellogenin. Changes in the gonad somatic index also confirmed the inhibitory effects of Mn-CL2 dsRNA on ovary maturation. These results suggest that Mn-CL2 has a key role in promoting ovary maturation.

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Section: Discussionsupporting

confidence: 93%

Molecular Characterization of a Novel Cathepsin L in Macrobrachium nipponense and Its Function in Ovary Maturation

et al. 2022

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Degradation of M r 25,000 Protein by Cathepsin L-like Protease in Xenopus laevis Oocytes

2014

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A phosphorylated protein with a molecular mass of 25,000 (pp25) is involved in Xenopus laevis vitellogenin B1 and partially overlaps with phosvitin and lipovitellin 2. The protease responsible for pp25 degradation was studied in vitro since this occurs during embryogenesis. Initially, a protease thought to be a contaminant of the purified pp25 preparation was analyzed and an antipain-sensitive protease presumed to be involved. When commercially available proteases were examined, pp25 was not degraded by calpain I or 20S proteasome, but it was degraded by cathepsin L in vitro. A survey of the protease responsible for pp25 degradation in the cytoplasm of Xenopus oocytes found partially purified pp25 was degraded in partly antipain-sensitive manner. These results suggest that an antipain-sensitive protease or cathepsin L (or a related protease) is a candidate for pp25 degradation.

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Expression and functional analysis of cathepsin L1 in ovarian development of the oriental river prawn, Macrobrachium nipponense

Zhu¹,

Fu²,

Qiao³

et al. 2021

Aquaculture Reports

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Effects on properties of a thiol protease from Xenopus embryos of changes in substrate and assay conditions.

Cited by 8 publications

References 9 publications

Molecular Characterization of a Novel Cathepsin L in Macrobrachium nipponense and Its Function in Ovary Maturation

Molecular Characterization of a Novel Cathepsin L in Macrobrachium nipponense and Its Function in Ovary Maturation

Degradation of M r 25,000 Protein by Cathepsin L-like Protease in Xenopus laevis Oocytes

Expression and functional analysis of cathepsin L1 in ovarian development of the oriental river prawn, Macrobrachium nipponense

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