Vitellogenin is Glycosylated in the Fat Body of the Stick Insect Carausius morosus and Not Further Modified Upon Transfer to the Ovarian Follicle

Micron ◽  
1998 ◽  
Vol 29 (6) ◽  
pp. 451-460 ◽  
Author(s):  
F Giorgi ◽  
A Cecchettini ◽  
A Falleni ◽  
M Masetti ◽  
V Gremigni
1972 ◽  
Vol 56 (1) ◽  
pp. 129-137
Author(s):  
J. E. TREHERNE

1. The effects of variation in the sodium concentration of the bathing media on axonal function has been measured in de-sheathed connectives in the presence of the overlying neural fat-body sheath. 2. The response to solutions of the same sodium concentration as the haemolymph (15 mM/1) was found to be essentially similar to that recorded in de-sheathed connectives in the absence of the fat-body sheath, there being a rapid decline in amplitude of the recorded action potentials in both preparations. 3. On the basis of these observations it is concluded that the neural fat-body sheath is unlikely to be involved in the regulation of the extra-neuronal sodium level.


1980 ◽  
Vol 46 (1) ◽  
pp. 1-16
Author(s):  
F. Giorgi ◽  
F. Macchi

Vitellogenesis in the stick insect Carausius morosus (Br.) has been studied with the goal of identifying vitellogenin in various tissues. Following exposure to in vivo to radioactive amino acids, oocytes in the medium size range are labelled with a minimum delay of 6 h after the time of injection. Incorporation of radioactivity under these conditions is shown to depend upon accumulation of proteins rather than on a differential rate of protein synthesis in succeeding stages of oogenesis. By immunochemical analyses, it is shown that at least two antigens are common to both haemolymph and ovary and that one of these is also present in the fat body. Both antigens are labelled during exposure to radioactive amino acids. When analysed by the SDS polyacrylamide gel electrophoresis, extracts from both haemolymph and ovary appear to share a number of protein fractions which range in molecular weight from 40 000 to 200 000 Daltons. The labelling pattern exhibited by these fractions is clearly indicative of a protein transfer from the fat body to the oocyte. Fat body cultured in vivo for up to 4 h releases a major macromolecular complex in the external medium. The latter has been identified as vitellogenin by both immuno-precipitation assay and SDS polyacrylamide gel electrophoresis. The protein which is synthesized and secreted under these conditions results from the processing of a protein complex of higher molecular weight.


1995 ◽  
Vol 167 (1) ◽  
pp. 379-387 ◽  
Author(s):  
Franco Giorgi ◽  
Antonella Cecchettini ◽  
Maria Teresa Locci ◽  
Massimo Masetti ◽  
James T. Bradley

1959 ◽  
Vol 197 (2) ◽  
pp. 360-366 ◽  
Author(s):  
Herbert C. Dessauer ◽  
Wade Fox

The first stage of follicle development was due chiefly to hydration; during the second (deutoplasmic) stage 60 mg of solid were taken up with each 100 mg increase in follicle weight. Plasma calcium and protein P rose near end of hydration stage, remained elevated during deutoplasmic stage, reached extreme levels (max. Ca = 90 mm/l.; protein P = 86 mm/l.) near ovulation, and generally fell to anestrous levels while eggs were in early cleavage. Calcium increased in proportion to protein bound P of both plasma and follicles. During deutoplasmic stage a phospho-lipoprotein, of similar gross composition to yolk protein, appeared in plasma. Liver weight increased during hydration stage, remained elevated throughout deutoplasmic stage and decreased near ovulation. Fat body weight increased with onset of estrus, reached maximum during hydration stage and progressively decreased during deutoplasmic stage. Plasma and liver changes characteristic of estrus were reproduced in fasted male snakes with estradiol injections.


Chromosoma ◽  
1980 ◽  
Vol 79 (1) ◽  
pp. 105-114 ◽  
Author(s):  
Laas P. Pijnacker ◽  
Margriet A. Ferwerda

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