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Lipids in Insect Oocytes: From the Storage Pathways to Their Multiple Functions

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Oocytes

Part of the book series: Results and Problems in Cell Differentiation ((RESULTS,volume 63))

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Abstract

In insect physiology, the mechanisms involved in the buildup and regulation of yolk proteins in developing oocytes have been thoroughly researched during the last three decades. Comparatively, the study of lipid metabolism in oocytes had received less attention. The importance of this issue lies in the fact that lipids make up to 40% of the dry weight of an insect egg, being the most important supply of energy for the developing embryo. Since the oocyte has a very limited capacity to synthesize lipids de novo, most of the lipids in the mature eggs arise from the circulation. The main lipid carriers in the insect circulatory system are the lipoproteins lipophorin and vitellogenin. In some species, the endocytosis of lipophorin and vitellogenin may account for about 10% of the lipids present in mature eggs. Thus, most of the lipids are transferred by a lipophorin-mediated pathway, in which the lipoprotein unloads its lipid cargo at the surface of oocytes without internalization. This chapter recapitulates the current status on lipid storage and its utilization in insect oocytes and discusses the participation of key factors including lipoproteins, transfer proteins, lipolytic enzymes, and dynamic organelles such as lipid droplets. The new findings in the field of lipophorin receptors are presented in the context of lipid accumulation during egg maturation, and the roles of lipids beyond energy source are summarized from the perspective of oogenesis and embryogenesis. Finally, prospective and fruitful areas of future research are suggested.

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Abbreviations

α-ATPase:

α subunit of the F1FO adenosine triphosphate synthase complex

apoA-I:

apolipoprotein A-I

apoLp-I:

apolipophorin I

apoLp-II:

apolipophorin II

ATPase:

F1FO adenosine triphosphate synthase

β-ATPase:

β subunit of the F1FO adenosine triphosphate synthase complex

bHLH-PAS:

basic helix-loop-helix Per/Arnt/Sim

CaM:

calmodulin

COX:

cyclooxygenases

DAG:

diacylglycerol

DGAT:

acyl-CoA:diacylglycerol O-acyltransferase

EcR:

ecdysone receptor

FAs:

fatty acids

FFAs:

free fatty acids

GPAT:

glycerol-3-phosphate acyltransferase

HCs:

hydrocarbons

HDL:

high-density lipoproteins

HDLp:

high-density lipophorin

IDL:

intermediate-density lipoproteins

IP2 :

phosphatidylinositol 4,5-biphosphate

IP3 :

inositol 1,4,5-trisphosphate

JH:

juvenile hormones

LA:

LDLR class A ligand-binding domain

LDL:

low-density lipoproteins

LDLp:

low-density lipophorin

LDLR:

low-density lipoprotein receptor

LOX:

lipoxygenases

LPL:

lipoprotein lipase

LpR:

lipophorin receptor

LSD-1:

lipid storage droplet 1

LSD-2:

lipid storage droplet 2

LTP:

lipid transfer particle

MAG:

monoacylglycerol

Met:

Methoprene-tolerant

mVg:

microvitellogenin

PGs:

prostaglandins

PLC:

phospholipase C

PLs:

phospholipids

SCRB15:

scavenger receptor class B member 15

SREBP:

sterol regulatory element-binding protein

TAG:

triacylglycerol

TOR:

target of rapamycin

USP:

ultraspiracle

VgR:

vitellogenin receptor

VHDLp:

very high-density lipophorin

VLDL:

very low-density lipoproteins

YPPs:

yolk protein precursors

YPs:

yolk polypeptides

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Acknowledgments

Authors thank Dr. B. P. Settembrini and Dr. E. R. Rubiolo for helpful suggestions and critical reading. Unpublished scanning electron micrographs were obtained in collaboration with Dr. B. P. Settembrini.

Funding

Work in the L.E.C. laboratory is supported by grants from SECyT-UNC, FONCyT (PICT 2013-0626), and CONICET (PIP 0159).

Authors’ Contribution

L.L.F., J.L., and L.E.C. wrote the chapter and approved the final version. The authors declare that there is no conflict of interest in regard to the contents of this chapter.

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  1. Instituto do Cerebro (InsCer). Pontifícia Universidade Católica do Rio Grande do Sul, Porto Alegre, RS, Brazil

    Leonardo L. Fruttero

  2. Departamento de Bioquímica Clínica, Centro de Investigaciones en Bioquímica Clínica e Inmunología (CIBICI-CONICET), Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Córdoba, CP 5000, Argentina

    Jimena Leyria & Lilián E. Canavoso

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  1. Leonardo L. Fruttero
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Correspondence to Lilián E. Canavoso .

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  1. Department of Surgery, The Houston Methodist Hospital, Houston, Texas, USA

    Malgorzata Kloc

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Fruttero, L.L., Leyria, J., Canavoso, L.E. (2017). Lipids in Insect Oocytes: From the Storage Pathways to Their Multiple Functions. In: Kloc, M. (eds) Oocytes. Results and Problems in Cell Differentiation, vol 63. Springer, Cham. https://doi.org/10.1007/978-3-319-60855-6_18

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