The secretory pathway of vitellogenin in the fat body of the stick insect bacillus rossius: An ultrastructural and immunocytochemical study

Mazzini, Massimo; Burrini, A. G.; Giorgi, Franco

doi:10.1016/0040-8166(89)90011-6

Cited by 13 publications

(2 citation statements)

References 33 publications

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“…This observation is in agreement with numerous biochemical studies (reviewed in Kunkel and Nordin 1985;Kanost et al 1990;Raikhel and Dhadialla 1992). Visualization of Vg in the fat body trophocytes has been previously performed for several insects by means of immunocytochemical techniques for fluorescent light microscopy (Tanaka and Yokizaki 1974) and electron microscopy (Couble et al 1979;Thomsen et al 1980;Mazzini et al 1989) and is particularly detailed for A. aegypti (Raikhel and Lea 1983;Raikhel 1986a, b;1987).…”

Section: Discussionmentioning

confidence: 99%

Secretory and internalization pathways of mosquito yolk protein precursors

Snigirevskaya

Hays

Raikhel

1997

Cell and Tissue Research

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The vitellogenic female fat body of the mosquito Aedes aegypti produces three yolk protein precursors that are deposited in the yolk bodies of developing oocytes: vitellogenin, vitellogenic carboxypeptidase (VCP), and 44-kDa protein (44KP). We have used gold immunocytochemistry to investigate the pathways of their secretion in fat body trophocytes and their internalization by oocytes. In fat body trophocytes, all three yolk protein precursors are co-localized in the Golgi complex and secretory granules, indicating that they proceed simultaneously through the secretory pathway. The lysosomal system plays an important role in the termination of vitellogenesis in mosquito trophocytes, by degrading biosynthetic organelles and secretory granules. At this time, VCP and 44KP are found together with vitellogenin in trophocyte autophagolysosomes, suggesting that all three yolk protein precusors are redirected from the secretory to the lysosomal degradative pathway. Localization of VCP and 44KP in developing mosquito oocytes clearly shows that the internalization of these yolk protein precursors by oocytes occurs via the same endocytotic route as vitellogenin: all three yolk protein precursors are found on the oocyte microvillus membrane, in coated vesicles, and early endosomes. They are observed intermixed with one another in the late endosomes or in transitional yolk bodies. In mature yolk bodies, however, 44KP and VCP are segregated from vitellin, the crystallized storage form of vitellogenin; 44KP and VCP reside in the non-crystalline cortex, surrounding the vitellin core in nature yolk bodies.

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Section: Discussionmentioning

confidence: 99%

Secretory and internalization pathways of mosquito yolk protein precursors

Snigirevskaya

Hays

Raikhel

1997

Cell and Tissue Research

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“…Las Vg de insectos generalmente se secretan a la HL como dímeros de 400-600 kDa (Tufail & Takeda, 2008), todas se encuentran glicosiladas y en su mayoría altamente fosforiladas (Tufail et al, 2005;Giorgi et al, 1998;Takahashi, 1987). En este grupo, las Vg son sintetizadas en los ribosomas asociados al retículo endoplasmático, transferidas al aparato de Golgi y eventualmente empaquetadas en gránulos secretorios que emergen de la red trans-Golgi (Giorgi et al, 1998;Snigirevskaya et al, 1997;Mazzini et al, 1989;Giorgi et al, 1989). A lo largo de la ruta secretoria, la Vg es modificada postraduccionalmente por glicosilación (Giorgi et al, 1998;Osir et al, 1986;Kunkel et al, 1980), fosforilación (della Cioppa & Engelmann, 1987;Takahashi, 1987;Brennan & Mahowald, 1982) y sulfatación (Dhadialla & Raikhel, 1990;Bauerle & Huttner, 1985).…”

Section: I72 Lipoproteínas Circulantes Ligadas Al Sexo (Vitelogeniunclassified

Bioquímica y fisiología de lipoproteínas en arácnidos

Laino¹

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La especie Polybetes pythagoricus es representante de un género de arañas exclusivamente sudamericano, perteneciente al Suborden Araneomorpha, Familia Sparassidae, abundante en regiones tropicales y subtropicales. Por tratarse de una especie de fácil obtención, manipulación y mantenimiento, fue elegida como modelo de estudio para este trabajo de tesis. En el presente estudio, se buscó ampliar el conocimiento a nivel estructural de la lipoproteína hemolinfática de muy alta densidad (VHDL) de dicha araña, se analizaron aspectos bioquímicos y fisiológicos estudiando el rol de las lipoproteínas de esta especie en la dinámica de la circulación de lípidos, y el transporte de éstos lípidos, desde y hacia los tejidos; y por último se estudió la presencia y estructura de dos lipovitelinas de huevos.

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The basic organization of the Plathelminthes

Ehlers

1995

Biology of Turbellaria and Some Related Flatworms

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The secretory pathway of vitellogenin in the fat body of the stick insect bacillus rossius: An ultrastructural and immunocytochemical study

Cited by 13 publications

References 33 publications

Secretory and internalization pathways of mosquito yolk protein precursors

Secretory and internalization pathways of mosquito yolk protein precursors

Bioquímica y fisiología de lipoproteínas en arácnidos

The basic organization of the Plathelminthes

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