Title of article :
Vitellogenesis in the hematophagous Dipetalogaster maxima (Hemiptera: Reduviidae), a vector of Chagas’ disease
Author/Authors :
Aguirre، نويسنده , , Silvina A. and Frede، نويسنده , , Silvia and Rubiolo، نويسنده , , Edilberto R. and Canavoso، نويسنده , , Liliلn E.، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2008
Pages :
10
From page :
393
To page :
402
Abstract :
Oocyte extracts of anautogenous Dipetalogaster maxima were chromatographed on an ion-exchange column in order to purify vitellin (Vt), the main insect yolk protein precursor. Purified Vt (Mr ∼443 kDa) was composed of four subunits with approximate molecular weights of 174, 170, 50, and 44 kDa. Polyclonal anti-Vt antibody, which cross-reacted equally with fat body extracts and hemolymph vitellogenin (Vg), was used to measure the kinetics of Vg expression in the fat body and the levels in hemolymph. In addition, morphological and immunohistochemical changes that took place in the ovary during vitellogenesis were analyzed. The study was performed between 2 and 8 days post-ecdysis and between 2 and 25 days post-blood feeding. During the post-ecdysis period, D. maxima showed decreased synthesis of Vg and concomitantly, low levels of Vg in hemolymph (4.5×10−3 μg/μl at day 4). After a blood meal, Vg synthesis in the fat body and its levels in hemolymph increased significantly, reaching an average of 19.5 μg/μl at day 20. The biochemical changes observed in the fat body and hemolymph were consistent with the histological and immunohistochemical finds. These studies showed noticeable remodeling of tissue after blood feeding.
Keywords :
Blood meal , Hematophagous vector , Vitellogenesis , Oocyte , Vitellin
Journal title :
Journal of Insect Physiology
Serial Year :
2008
Journal title :
Journal of Insect Physiology
Record number :
1414797
Link To Document :
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