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BOR - Papers in Press, published online ahead of print February 21, 2007.
Biol Reprod 2007, 10.1095/biolreprod.106.059766
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biolreprod.106.059766v1
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Submitted December 23, 2006
Returned for revision January 26, 2007
Accepted February 20, 2007

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Vertebrate Yolk Complexes and the Functional Implications of Phosvitins and Other Subdomains in Vitellogenins

Roderick Nigel Finn *

* To whom correspondence should be addressed. E-mail: nigel.finn{at}bio.uib.no.

Abstract
In non-placental or non-trophotenic vertebrates early development depends on the maternal provision of egg yolk that is mainly derived from large multi-domain vitellogenin (Vtg) precursors. To reveal the molecular nature of protein pools found in vertebrate oocytes, published data for the N-termini of yolk proteins are mapped to the deduced primary structures of their parent Vtgs. Available evidence shows that the primary cleavage sites of Vtgs are conserved, but the cleavage products exist as multi-domain variants in the yolk protein pool. The serine-rich phosvitin (Pv) domains are linearly related to the Mr of the lipovitellin heavy chain. The 3-dimensional location of Pv is mapped to the outer edges of the Vtg monomer where it is proposed to form amphipathic structures that loop up over the lipid pocket. In this locus it is proposed that Pv stabilises nascent Vtg while it receives its lipid cargo, and thus facilitates the hepatic loading and locking of lipid within the Vtg (A-sheet)-(N-sheet)-(LvL) cavity, and enhances its solubility following secretion to the circulating plasma. The C-terminal regions of Vtgs are homologous to human von Willebrand factor type D domains (Vwfd), a conserved cysteine rich molecule with homologous regions prevalent in Vtgs, lipophorins, mucins, integrins, and zonadhesins. Unlike human Vwfd, lower vertebrate Vwfds do not contain "RGD" motifs associated with extracellular matrix binding. Its function in Vtg is unknown, but the lubricant properties associated with mucins, and the cell adhesion properties associated with integrins and zonadhesins implicate Vwfd in the origin of hemostatic platelet aggregation. Similarly, the proteolytic inhibitory properties associated with the binding of factor VIII in humans, suggests that Vwfd may stabilize Vtg during passage in the systemic circulation.

Key words: Gamete Biology • Developmental biology • Gametogenesis • Oocyte development





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