Apovitellenin-1
| Apo-VLDL-II | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Apo-VLDL-II | ||||||||
| Pfam | PF05418 | ||||||||
| InterPro | IPR008404 | ||||||||
| |||||||||
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
[edit ]- ^ 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.