Book•
Progress in vitellogenesis
01 Jan 2002-
TL;DR: Biosynthesis of Insect Yolk Protein Precursors and Regulation of Yolk protein Genes in Higher Diptera: Mary Bownes Juvenile Hormone and Vitellogenin Gene Expression: Xavier Belles
Abstract: Biosynthesis of Insect Yolk Protein Precursors: M. Takeda and A.S. Raikhel The Cell Biology of Insect Yolk Protein Precursors Yolk and the Secretory Pathway: A.S. Raikhel et al. Regulation of Yolk Protein Genes by Ecdysone: A.S. Raikhel et al. Regulation of Yolk Protein Genes in Higher Diptera: Mary Bownes Juvenile Hormone and Vitellogenin Gene Expression: Xavier Belles Regulation of Tissue-specificity of Yolk Protein Gene Expression: David Martin and A.S. Raikhel Receptor-mediated Endocytosis and Internalization Pathways of Yolk Proteins in Insects Oocytes: E. Snigievskaya and A.S. Raikhel Yolk Protein Receptors in Invertebrate Oocytes: A.S. Raikhel et al. Lipid Accumulation in Oocytes: Rick van Antwerpen et al. Non-Vitellin Yolk Proteins: H. Masuda and Pedro Oliviera Yolk Degrading Proteases: S. Takhashi and Y. Yamamoto Biochemical and Ultrastructural Aspects of Vitellin Utilization during Embryogenesis: Franco Giorgi and Jack Nordin
Citations
More filters
TL;DR: Phylogenetic analysis using 31 Vg sequences from 25 insect species reflects, in general, the current phylogenies of insects, suggesting that Vgs are still phylogenetically bound, although a divergence exists among them.
375 citations
TL;DR: The expression studies clearly demonstrate that insect VgRs are ovary-bound receptors of the LDLR family as compared to LpRs, which are transcribed in a wide range of tissues including ovary, fat body, midgut, brain, testis, Malpighian tubules, and muscles.
206 citations
TL;DR: Although Insect oocytes can readily synthesize TAG from free fatty acids (FFAs) and glycerol, however, de novo synthesis of FAs by the oocyte is marginal and FAs have to be imported from the fat body or the diet.
180 citations
TL;DR: The structural and phylogenetic data presented indicate that the major egg yolk precursor protein of decapod crustaceans is surprisingly closely related to insect apoLp-II/I and vertebrate apoB and should be known as apolipocrustacein (apoCr) rather than Vtg.
Abstract: In animals, the biogenesis of some lipoprotein classes requires members of the ancient large lipid transfer protein (LLTP) superfamily, including the cytosolic large subunit of microsomal triglyceride transfer protein (MTP), vertebrate apolipoprotein B (apoB), vitellogenin (Vtg), and insect apolipophorin II/I precursor (apoLp-II/I). In most oviparous species, Vtg, a large glycolipoprotein, is the main egg yolk precursor protein. This report clarifies the phylogenetic relationships of LLTP superfamily members and classifies them into three families and their related subfamilies. This means that the generic term Vtg is no longer a functional term, but is rather based on phylogenetic/structural criteria. In addition, we determined that the main egg yolk precursor protein of decapod crustaceans show an overall greater sequence similarity with apoLp-II/I than other LLTP, including Vtgs. This close association is supported by the phylogenetic analysis, i.e. neighbor-joining, maximum likelihood and Bayesian inference methods, of conserved sequence motifs and the presence of three common conserved domains: an N-terminal large lipid transfer module marker for LLTP, a DUF1081 domain of unknown function in their central region exclusively shared with apoLp-II/I and apoB, and a von Willebrand-factor type D domain at their C-terminal end. Additionally, they share a conserved functional subtilisin-like endoprotease cleavage site with apoLp-II/I, in a similar location. The structural and phylogenetic data presented indicate that the major egg yolk precursor protein of decapod crustaceans is surprisingly closely related to insect apoLp-II/I and vertebrate apoB and should be known as apolipocrustacein (apoCr) rather than Vtg. These LLTP may arise from an ancient duplication event leading to paralogs of Vtg sequences. The presence of LLTP homologs in one genome may facilitate redundancy, e.g. involvement in lipid metabolism and as egg yolk precursor protein, and neofunctionalization and subfunctionalization, e.g. involvement in clotting cascade and immune response, of extracellular LLTP members. These protein-coding nuclear genes may be used to resolve phylogenetic relationships among the major arthropod groups, especially the Pancrustacea-major splits.
111 citations
TL;DR: Peptide mass fingerprints of the vitelline polypeptides suggest that the predicted endoprotease cleavage site at amino acids 725-728 does indeed undergo cleavage and may serve as a model to study alternate regulation of gene expression during these two processes.
96 citations