Recently, additional nomenclature has been introduced to designate specific lipophorin subspecies that differ in lipid and/or apoprotein content.
The concentration of lipophorin subspecies (HDLp and LDLp) changes can be considered to reflect the physiological state of the organism with respect to lipid metabolism.
[4] Furin is a member of the proprotein convertase family of subtilisin like serine endoproteases that is mainly active in the trans-Golgi network.
The core of a lipophorin particle typically consists of nonpolar lipids, such as diacylglycerols and hydrocarbons, surrounded by a layer of phospholipids, cholesterol, and apolipoproteins.
At the N-terminus of apoLp-I, followed by the amino acid sequence RQKR, similar to the other apolipophorin precursors known to date, in locust apoLp-II/I (3359 aa residues).
LDLp is derived from HDLp during periods of high lipid transport demand, such as flight or vitellogenesis, as it becomes enriched with diacylglycerol.
Lipophorin is the main carrier of different lipids, such as diacylglycerol (DAG), hydrocarbons, phospholipids, and sterols, into insect hemolymph (blood).
Lipophorin is also necessary for cholesterol transport and performs functions similar to HDL in humans, such as membrane synthesis and hormone production.
During vitellogenesis, lipophorin transports lipids like diacylglycerol (DAG) from the fat body to the ovaries, where they are used for yolk formation in developing oocytes.
Acting as a reusable shuttle, it interacts with ovarian receptors to deliver lipids essential for vitellogenin synthesis and lipid-rich yolk deposition.