Purification and characterization of cathepsin L from the white muscle of chum salmon, Oncorhynchus keta

Yamashita, Michiaki; Konagaya, Shiro

doi:10.1016/0305-0491(90)90371-y

Cited by 67 publications

(35 citation statements)

References 26 publications

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“…Purified protease had the same relative susceptibility to inhibitors as the crude extract (Table I). TLCK and TPCK, inhibitors of trypsin and chymotrypsin-like serine proteases respectively (31), also inhibit some cysteine proteases (32). Protease-free Vt-When Vt is prepared by ion exchange chromatography of day 0 yolk (33), it retains some acid-activable protease, which made it unsuitable for in vitro enzyme action pattern studies (described below).…”

Section: Resultsmentioning

confidence: 99%

A Cysteine Protease That Processes Insect Vitellin

Liu¹,

McCarron²,

Nordin

1996

Journal of Biological Chemistry

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A cysteine protease that initiates degradation of vitellin (Vt) in the orthopteran Blattella germanica, and its proprotease precursor, were purified from yolk and partially characterized. The protease, purified 300-fold, contains three peptides of M r 27,000, 29,000, and 31,000. A comparison of the purified enzyme's action pattern on Vt in vivo and in vitro confirmed its role in Vt processing. Protease-deficient yolk (day 0 postovulation) contained peptides of M r 35,500, 37,000, 39,000, and 41,000, which were absent from yolk with protease activity. These were replaced by three peptides of approximately M r 29,000, at days 2-3, the same time in development that protease expression and acidification of yolk granules occur (Nordin, J. H., Beaudoin, E. L., and Liu, X. (1991) Arch. Insect Biochem. Physiol. 18, 177-192). Acidification of purified proprotease converted it to three peptides of approximately M r 29,000 with cysteine protease activity. This conversion also required participation of a cysteine protease. Activated proprotease had the same pH activity profile, susceptibility to inhibitors, and cathepsin classification (L) as the protease. These results indicate that the Vt-processing protease is derived from a proprotease, which is activated in vivo by a developmentally regulated decrease in intragranular pH.

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Section: Resultsmentioning

confidence: 99%

A Cysteine Protease That Processes Insect Vitellin

Liu¹,

McCarron²,

Nordin

1996

Journal of Biological Chemistry

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“…The MW of 30-kDa and 58-kDa proteinases were 27,000 and 58,000, respectively, using Sephadex G-75 (data not shown). The 30-kDa proteinase was similar to salmon cathepsin L. 16 ) Since the SDS only bound to the protein domain on the glycoprotein, which consequently decreased the mobility on SD8-PAGE, the MW of glycoprotein is usually estimated· too high.26) Since the 30-kDa proteinase is a glycoprotein, the MW estimated by SD8-PAGE was greater than that bySephadex G-75. The data obtained in this study suggested that both purified proteinases were monomers.…”

Section: Molecular Weightmentioning

confidence: 99%

Purification and Characterization of Proteinases Identified as Cathepsins L and L-like (58 kDa) Proteinase from Mackerel (Scomber australasicus)

Lee

Chen

Jiang

1993

Bioscience, Biotechnology, and Biochemistry

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“…In order to detect ovarian cathepsin D in these reports, its activity was routinely assayed with hemoglobin as a substrate. Since hemoglobin is lysed preferentially by fish cathepsin L [18], it is impossible to assess the activity of ovarian cathepsin D in the hemoglobin assay without interference of coexistent cathepsin L. Similar problems had arisen when mammalian cathepsin D in cell lysates was assayed, and a novel fluorometric substrate was recently constructed to assess the activity of cathepsin D specifically [13]. This study adopted it in assessing that of scad ovarian cathepsin D to exclude interference of coexistent proteases including cathepsin L.…”

Section: Resultsmentioning

confidence: 99%

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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Purification and characterization of cathepsin L from the white muscle of chum salmon, Oncorhynchus keta

Cited by 67 publications

References 26 publications

A Cysteine Protease That Processes Insect Vitellin

A Cysteine Protease That Processes Insect Vitellin

Purification and Characterization of Proteinases Identified as Cathepsins L and L-like (58 kDa) Proteinase from Mackerel (Scomber australasicus)

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

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