Vitellogenesis in the stable fly, stomoxys calcitrans

Chen, A.C.; Kim, H.R.; Mayer, Richard T.; Norman, James O’Higgins

doi:10.1016/0305-0491(87)90261-6

Cited by 13 publications

(10 citation statements)

References 31 publications

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“…Insect yolk proteins are generally referred to as vitellin (Vn) or egg-specific protein (ESP). Vg is the protein which is synthesized by fat body, released into the hemolymph, and then taken up by the growing ovary to become Vn (Engelmann, 1979;Kunkel and Nordin, 1985), whereas ESP is synthesized by the ovary itself (Irie and Yamashita, 1983;Chen et al, 1987).…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of yolk protein‐2 from the fall webworm,Hyphantria cuneadrury

Lee

Kim

1995

Arch Insect Biochem Physiol

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Yolk proteins (YPl, YP2, and YP3) of the fall webworm, Hyphantria cunea, are of relatively low molecular weight. Yolk protein-2 (YP2) was purified from gel slices and by KBr density gradient ultracentrifugation followed by ion exchange chromatography. YP2 i s composed of one subunit with a molecular weight of 35.5 kDa. YP2 contains neutral lipids (diacylglycerol and triacylglycerol) and phospholipids (phosphatidylcholine and phosphatidylethanolamine). The neutral lipids are largely composed of lauric acid and palrnitoleic acid. YP2 contains relatively large amounts of glutamic acid and aspartic acid but small amounts of tyrosine, phenylalanine, and methionine. YP2 is a vitellin (Vn) synthesized by the fat body. Vitellogenin-2 (Vg2), the precursor of YP2, is present in very small amounts in the hemolymph. Lipophorin and storage protein also are found in the ovary of H. cunea, and these proteins do not immunologically cross-react with YP2. YP2 is detected in first instar larvae but completely disappears during the second instar, indicating that YP2 is intensively utilized during postembryonic development. Anti-YP2 antibodies cross-react with ovarial extracts of Bornbyx mori but not with those of insects from other orders such as Cletus schrnidti (Hemiptera), Lucilia illustris (Diptera), Anechura japonica (Dermaptera), Periplaneta americana (Dictyoptera), and Ducetia japonica (Orthoptera). o 1995 WiIey-Liss, Inc.

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Section: Discussionmentioning

confidence: 99%

Purification and characterization of yolk protein‐2 from the fall webworm,Hyphantria cuneadrury

Lee

Kim

1995

Arch Insect Biochem Physiol

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“…Three subunits have been reported for C. erythrocephala, Lucilia cuprina, M. domestica, Protophormia terrae-novae, and N. bullata (see Zou et al, 1988). However, four subunits have been reported for P. regina (Zou et al, 1988), five for M. domestica (Bianchi et al, 1985), and six for S. calcitrans (Chen et al, 1987). We believe the YP number, as determined by protein analysis, should be considered tentative until their corresponding genes or mRNAs are identified and characterized.…”

Section: Biosynthesis Of Vitellogeninmentioning

confidence: 96%

“…However, in species such as D. melanogaster and M. domestica, the ovarian follicle cells also produce a significant amount of Vg (Brennan and Mahowald, 1982;Agui et al, 1985). In an even more extreme case, Vg synthesis occurs solely in the ovarian tissues of the stable fly, Stomoxys calcitrans (Chen et al, 1987). Yolk protein of this group of flies may also have different numbers of subunits.…”

Section: Biosynthesis Of Vitellogeninmentioning

confidence: 99%

Juvenile hormone regulation of reproduction in the cyclorrhaphous diptera with emphasis on oogenesis

Yin

Stoffolano

1997

Arch. Insect Biochem. Physiol.

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“…In addition to the reduction in yolk protein genes, the tissue specificity of tsetse yolk protein genes differs from that of most brachyceran flies such as Drosophila , in which yolk proteins are produced by both the fat body and ovarian follicle cells (20, 46, 64, 67, 142). In tsetse, yolk protein is synthesized only by the follicle cells of the developing oocyte (6, 58, 62), as in Stomoxys calcitrans (29, 60). The Drosophila yolk protein gene ( yp2 ) is expressed in a follicle-cell-specific manner (48), suggesting that follicle-specific expression for yp2 orthologs likely occurs in most brachyceran flies.…”

Section: Oogenesis and Ovulation In Tsetsementioning

confidence: 99%

Adenotrophic Viviparity in Tsetse Flies: Potential for Population Control and as an Insect Model for Lactation

Benoit

Attardo

Baumann

et al. 2015

Annu. Rev. Entomol.

107

102

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Tsetse flies (Glossina spp.), vectors of African trypanosomes, are distinguished by their specialized reproductive biology, defined by adenotrophic viviparity (maternal nourishment of progeny by glandular secretions followed by live birth). This trait has evolved infrequently among insects and requires unique reproductive mechanisms. A key event in Glossina reproduction involves the transition between periods of lactation and nonlactation (dry periods). Increased lipolysis, nutrient transfer to the milk gland, and milk-specific protein production characterize lactation, which terminates at the birth of the progeny and is followed by a period of involution. The dry stage coincides with embryogenesis of the progeny, during which lipid reserves accumulate in preparation for the next round of lactation. The obligate bacterial symbiont Wigglesworthia glossinidia is critical to tsetse reproduction and likely provides B vitamins required for metabolic processes underlying lactation and/or progeny development. Here we describe findings that utilized transcriptomics, physiological assays, and RNA interference–based functional analysis to understand different components of adenotrophic viviparity in tsetse flies.

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Vitellogenesis in the stable fly, stomoxys calcitrans

Cited by 13 publications

References 31 publications

Purification and characterization of yolk protein‐2 from the fall webworm,Hyphantria cuneadrury

Purification and characterization of yolk protein‐2 from the fall webworm,Hyphantria cuneadrury

Juvenile hormone regulation of reproduction in the cyclorrhaphous diptera with emphasis on oogenesis

Adenotrophic Viviparity in Tsetse Flies: Potential for Population Control and as an Insect Model for Lactation

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