In molecular biology, apovitellenin-1 is a family of proteins found in birds. As part of the avian reproductive effort, large quantities of triglyceride-rich very-low-density lipoprotein (VLDL) particles are transported by receptor-mediated endocytosis into the female germ cells, apovitellenin-1 is a protein component of this VLDL. Although the oocytes are surrounded by a layer of granulosa cells harbouring high levels of active lipoprotein lipase, non-lipolysed VLDL is transported into the yolk. This is because the VLDL particles are protected from lipolysis by apovitellenin-1a, which acts as a potent dimeric lipoprotein lipase inhibitor.[1] Apo-VLDL-II is produced in the liver and secreted into the blood stream when induced by estrogen production in female birds.

Apo-VLDL-II
Identifiers
SymbolApo-VLDL-II
PfamPF05418
InterProIPR008404
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

References

edit
  1. ^ MacLachlan I, Steyrer E, Hermetter A, Nimpf J, Schneider WJ (July 1996). "Molecular characterization of quail apolipoprotein very-low-density lipoprotein II: disulphide-bond-mediated dimerization is not essential for inhibition of lipoprotein lipase". Biochem. J. 317 (2): 599–604. doi:10.1042/bj3170599. PMC 1217528. PMID 8713091.
This article incorporates text from the public domain Pfam and InterPro: IPR008404