Correlation of yolk phosphatase expression with the programmed proteolysis of vitellin in <i>Blattella germanica</i> during embryonic development

Purcell, John P.; Quinn, Theresa; Kunkel, Joseph G.; Nordin, John H.

doi:10.1002/arch.940090307

Cited by 36 publications

(34 citation statements)

References 22 publications

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“…Unique limit peptides in vitro were M r 88,000, 70,000, and 50,000 -53,000. Processing of the M r 50,000 subunit in vitro was obscured by other products of that approximate size, but this subunit is processed beginning at day 5 (16,18). Addition of fresh enzyme to the in vitro incubation did not alter the product distribution.…”

Section: Resultsmentioning

confidence: 92%

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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: 92%

“…These assays identified both cathepsin L-and B-like activities (17), the former constituting more than 85% of the total. The finding that the yolk of certain B. germanica translocation heterozygotes with defective embryo development and Vt processing lack yolk protease activity also implicates them (9,18).…”

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confidence: 95%

A Cysteine Protease That Processes Insect Vitellin

Liu¹,

McCarron²,

Nordin

1996

Journal of Biological Chemistry

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“…Endocytic activities during insect oogenesis involve the incorporation of the lipophosphoglycoprotein vitellogenin (Oliveira et al, 1986;Raikhel and Dadhialla, 1992;Valle, 1993;Sappington and Raikhel, 1998). Once inside the oocyte the vitellogenin, now referred to as vitellin (VT), is stored in organelles known as yolk granules (YGs) (Kunkel and Nordin, 1985;Purcell et al, 1988;Machado et al, 1998). After oviposition, the YGs fill almost the entire volume of the fresh egg and can vary significantly in size and density.…”

Section: Introductionmentioning

confidence: 99%

“…(Fagotto, 1991;Nordin et al, 1991;Mallya et al, 1992;Fagotto, 1995) and proton pyrophosphatases (H + -PPases) (Motta et al, 2004). In insects, several hydrolytic enzymes found in YGs such as cathepsins (Takahashi et al, 1996;Cho et al, 1999;Ribolla et al, 2001), acid phosphatases (Nussenzveig et al, 1992;Ribolla et al, 1993;Fialho et al, 2002;Fialho et al, 2005) and glycosidases (Purcell et al, 1988) were shown to be activated by low pH. Acidification of YGs, therefore, results in activation of hydrolases and degradation of VT.…”

Section: Introductionmentioning

confidence: 99%

Calcium-regulated fusion of yolk granules is important for yolk degradation during early embryogenesis of Rhodnius prolixusStahl

Ramos

Miranda

Souza

et al. 2007

Journal of Experimental Biology

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SUMMARY This study examined the process of membrane fusion of yolk granules (YGs)during early embryogenesis of Rhodnius prolixus. We show that eggs collected at days 0 and 3 after oviposition contain different populations of YGs, for example day-3 eggs are enriched in large YGs (LYGs). Day-3 eggs also contain the highest free [Ca2+] during early embryogenesis of this insect. In vitro incubations of day-0 YGs with [Ca2+]similar to those found in day-3 eggs resulted in the formation of LYGs, as observed in vivo. Fractionation of LYGs and small YGs (SYGs) and their subsequent incubation with the fluorescent membrane marker PKH67 showed a calcium-dependent transference of fluorescence from SYGs to LYGs, possibly as the result of membrane fusion. Acid phosphatase and H+-PPase activities were remarkably increased in day-3 LYGs and in calcium-treated day-0 LYGs. Both fractions were found to contain vitellins as major components, and incubation of YGs with calcium induced yolk proteolysis in vitro. Altogether, our results suggest that calcium-induced membrane fusion events take part in yolk degradation, leading to the assembly of the yolk mobilization machinery.

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“…This type of yolk mobilization has been reported for tick Ornithodoros moubata development (Fagotto, 1991), sea urchin Strongylocentrotus purpuratus (Mallya et al,1992), and the African clawed frog, X. laevis (Lemanski and Aldoroty, 1974;Fagotto and Maxfield, 1994). In insects, the presence of acid hydrolases, such as proteinases (Yamamoto and Takahashi, 1993), glycosidase (Purcell et al, 1988), and acid phosphatases (Ribolla et al, 1993;Fialho et al, 2002), has also been described.…”

Section: Introductionmentioning

confidence: 96%

Characterization of a tyrosine phosphatase activity in the oogenesis ofPeriplaneta americana

Oliveira

Machado

2006

Arch. Insect Biochem. Physiol.

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In this work, phosphatase activity was characterized in the ovary and the haemolymph of Periplaneta americana. The optimum pH for these activities was 4.0, and a temperature of 44 degrees C was ideal for the maximal enzyme activity. The phosphatase activities were inhibited by NaF, sodium tartrate, Pi, sodium orthovanadate, and ammonium molybdate. The ovarian phosphatase activity at pH 4.0 was almost exclusive against phosphotyrosine, with little or no effect on the residues of phosphoserine or phosphothreonine. These results indicate that this phosphatase activity is due to the presence of an acid tyrosine phosphatase. The phosphatase activities of acid extracts from P. americana ovaries (OEX) and an acid extract from P. americana haemolymph (HEX) were analyzed in non-denaturant gel electrophoresis using an analog substrate beta-naphtyl phosphate. The gel revealed two bands with phosphatase activity in the ovary and one band in the haemolymph; these bands were excised and submitted to a 10% SDS-PAGE showing a single 70-kDa polypeptide in both samples. Histochemistry of the ovary with alpha-naphtyl phosphate for localization of acid phosphatase activity showed mainly labeling associated to the oocyte peripheral vesicles, basal lamina, and between follicle cells. Electron microscopy analysis showed that acid phosphatase was localized in small peripheral vesicles in the oocyte, but not inside yolk granules. The possible role of this phosphatase during oogenesis and embryogenesis is also discussed in this article.

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Correlation of yolk phosphatase expression with the programmed proteolysis of vitellin in Blattella germanica during embryonic development

Cited by 36 publications

References 22 publications

A Cysteine Protease That Processes Insect Vitellin

A Cysteine Protease That Processes Insect Vitellin

Calcium-regulated fusion of yolk granules is important for yolk degradation during early embryogenesis of Rhodnius prolixusStahl

Characterization of a tyrosine phosphatase activity in the oogenesis ofPeriplaneta americana

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