Vitellogenesis in Oncopeltus fasciatus: PLC/IP(3), DAG/PK-C pathway triggered by CaM.

Abstract:

:In Oncopeltus fasciatus, evidence shown here indicates it is calmodulin (CaM) that activates phospholipase-C (PLC), beginning a signalling pathway necessary for endocytic uptake of yolk precursor molecules. Epithelial cell-produced CaM, transported to oocytes via gap junctions, has been shown to be required for receptor-mediated endocytic uptake of vitellogenins (Vgs, the protein precursors of yolk). To determine if CaM was directly or indirectly stimulating the phospholipase-C (PLC) signalling cascade and thus controlling Vg endocytosis we used a series of molecules known to inactivate various elements of the pathway. W-7 prevents CaM from interacting with other molecules. Neomycin isolates PIP(2) from PLC. U-73122 directly inactivates PLC. 2-APB blocks IP(3) receptors which would otherwise cause release of Ca(2+). Verapamil and CdCl(2) block Ca(2+) release channels. Staurosporin and calphostin are inhibitors of PK-C. 1-Hexadecyl-2-acetyl glycerol (HAG) binds to diacylglycerol (DAG). Through the use of these antagonists we show here that: (1) the activation of phospholipase-C in this system requires CaM. (2) Stimulated phospholipase-C converts PIP(2) into IP(3) and DAG. (3) IP(3) causes increase in cytosolic Ca(2+). (4) DAG and Ca(2+) each stimulate phosphokinase-C, resulting in endocytosis of Vgs.

journal_name

J Insect Physiol

authors

Brown PT,Herbert P,Woodruff RI

doi

10.1016/j.jinsphys.2010.04.006

subject

Has Abstract

pub_date

2010-09-01 00:00:00

pages

1300-5

issue

9

eissn

0022-1910

issn

1879-1611

pii

S0022-1910(10)00122-8

journal_volume

56

pub_type

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