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

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.

References

  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
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