Ocular tissues are highly dependent on lipid turnover and metabolism,
which requires an uptake mechanism for fatty acids from lipoproteins.
We studied the activity and expression of lipoprotein lipase (LPL), wh
ich catalyzes the hydrolysis of plasma triglycerides, in different ocu
lar regions. Human and bovine eyes were dissected and various speciali
zed anatomical areas were assayed for LPL activity, mRNA, and immunore
activity. Variable levels of LPL activity were detected in all structu
res in human and bovine eyes. LPL activity was much higher in vascular
ized structures, such as ciliary body, iris, and retina than in avascu
lar eye structures, such as vitreous body, lens, and cornea. In both h
uman and bovine eyes, ciliary body contained the highest LPL lipolytic
activity. LPL mRNA was detected by reverse transcription followed by
polymerase chain reaction (RT-PCR) in all regions of human eyes. By RT
-PCR analysts It was shown that bovine eyes contained high levels of L
PL mRNA in ciliary body and iris, lower levels were found in retina, o
ptic nerve, and lens, whereas no LPL mRNA could be found in bovine cor
nea. RT-PCR data, obtained in bovine eyes, agree with the results obta
ined by Northern blot experiments, confirming the high levels of LPL m
RNA in iris and ciliary body. Immunofluorescence experiments performed
on human eye samples indicated that the LPL protein is mostly distrib
uted on the choroides, the choriocapillaris, and on the vessels of cil
iary body, iris, optic nerve, and retina. The present study demonstrat
es that active LPL protein is synthesized, secreted, and located among
microvessels in several specialized regions of the eye, and suggests
that LPL could be involved in the uptake of fatty acids by the ocular
tissues.-Casaroli-Marano, R. P., J. Peinado-Onsurbe, M. Reina, B. Stae
ls, J. Auwerx, and S. Vilaro. Lipoprotein lipase in highly vascularize
d structures of the eye.