Analysis of the cuticular proteins of Hyalophora cecropia with two dimensional electrophoresis

Cox, Diana L.; Willis, Judith H.

doi:10.1016/0020-1790(87)90006-0

Cited by 64 publications

(14 citation statements)

References 22 publications

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“…No charge trains of spots, which often reveal the presence of glycosylated proteins, were observed on two-dimensional gels. This is consistent with previous observations that adult cuticular proteins of Tenebrio do not bind to a vdriety of lectins (Lemoine et al, 1990), and with the low amounts of glycosylation found in hard cuticles of Hyulophoru (COX and Willis, 1987) and Surcophugu (Kimura et al, 1976) The high percentage of glycine residues observed in ACP-20 (upto 60% in the N-and C-terminal glycine rich regions) reflects the over-representation of glycine in some hard cuticle proteins (Apple and Fristrom, 1991;Bouhin et al, unpublished results) as well as in other structural proteins such as in egg cliorion (Regier and Kafatos, 1985), intermediate filaments (Steinert et al, 1985), or plant cell wall (Condit and Meagher, 1986;Lei and Wu, 1991). Secondary structure predictions made using two methods (Garnier et al, 1978;Chou and Fasman, 1978) show that the glycine-rich regions of ACP-20 are constituted of short /3-strands interrupted by coiled or turn regions.…”

Section: Discussionsupporting

confidence: 81%

cDNA cloning and deduced amino acid sequence of a major, glycine‐rich cuticular protein from the coleopteran Tenebrio molitor

Charles

Bouhin

Quennedey

et al. 1992

European Journal of Biochemistry

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In Coleoptera, the elytra (forewings), with a very hard and thick cuticle, protect the membranous and delicate hindwings against mechanical stress. We have isolated and characterized a cDNA encoding a major cuticle protein in Tenebrio molitor, named ACP‐20. The deduced amino acid sequence is roughly tripartite, with two terminal glycine‐rich domains and a central region showing pronounced similarities with some other hard cuticle proteins. Northern blot and in situ hybridization analyses reveal that ACP‐20 gene expression is developmentally regulated since transcript accumulation occurs only in epidermal regions synthesizing hard cuticle and is restricted to the period of preecdysial adult cuticle deposition. Moreover, application of a juvenile hormone analogue prevents the appearance of the transcript, indicating that juvenile hormone, a key molecule involved in the control of insect metamorphosis, negatively regulates the expression of the ACP‐20 gene.

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Section: Discussionsupporting

confidence: 81%

cDNA cloning and deduced amino acid sequence of a major, glycine‐rich cuticular protein from the coleopteran Tenebrio molitor

Charles

Bouhin

Quennedey

et al. 1992

European Journal of Biochemistry

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“…The existence of terminal GalNAc residues on insect proteins from several different species has been demonstrated previously using N-acetylgalactosamine specific lectins [ 1,2,9,11]. Thus, the inability to add terminal sialic acid to 0-linked structures may be a general characteristic among insect cells, as has been reported for N-linked structures.…”

Section: Discussionmentioning

confidence: 75%

Structure of O‐glycosidically linked oligosaccharides synthesized by the insect cell line Sf9

Thomsen

Post

Elhammer

1990

J of Cellular Biochemistry

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The O-glycosidically linked oligosaccharides on the pseudorabies virus (PRV) glycoprotein gp50 synthesized by three different cell lines were studied. The intact membrane protein (gp50) was expressed in Vero cells and in the insect cell line Sf9. In addition, a truncated, secreted form lacking the transmembrane and cytoplasmic domains (gp50T), was expressed in CHO and Sf9 cells. The protein, both in intact and truncated form, synthesized by the two mammalian cells contained only the disaccharide Gal beta 1-3GalNAc, either unsubstituted or substituted with one or two sialic acid residues. By contrast, the major O-linked structure on gp50 and gp50T synthesized by Sf9 cells was the monosaccharide GalNAc. The Sf9 cells also linked lower amounts of Gal beta 1-3GalNAc to gp50 (12%) and gp50T (26%). None of the structures synthesized by Sf9 cells contained sialic acid. Measurements of the two relevant glycosyltransferases revealed that while all three cell lines contain comparable levels of UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase activity, there is a greater variation in the levels of UDP-Gal:N-acetylgalactosamine, beta 1-3 galactosyltransferase, with the Sf9 cells containing the lowest level.

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“…The size of band (33 kDa) was larger than that of estimated by deduced amino acid sequences (29 kDa). The result may depend on the reason that Cox and Willis (1987) reported, where urea concentration and buffer strength affected the mobility of cuticular proteins in SDS gel.…”

Section: Specific Expression Of Bmgrp2mentioning

confidence: 67%

Glycine-rich protein genes, which encode a major component of the cuticle, have different developmental profiles from other cuticle protein genes in Bombyx mori

Zhong

Mita

Shimada

et al. 2006

Insect Biochemistry and Molecular Biology

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Analysis of the cuticular proteins of Hyalophora cecropia with two dimensional electrophoresis

Cited by 64 publications

References 22 publications

cDNA cloning and deduced amino acid sequence of a major, glycine‐rich cuticular protein from the coleopteran Tenebrio molitor

cDNA cloning and deduced amino acid sequence of a major, glycine‐rich cuticular protein from the coleopteran Tenebrio molitor

Structure of O‐glycosidically linked oligosaccharides synthesized by the insect cell line Sf9

Glycine-rich protein genes, which encode a major component of the cuticle, have different developmental profiles from other cuticle protein genes in Bombyx mori

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