Post-translational modifications of the cuticular proteins of Hyalophora cecropia from different anatomical regions and metamorphic stages

Cox, Diana L.; Willis, Judith H.

doi:10.1016/0020-1790(87)90007-2

Cited by 33 publications

(11 citation statements)

References 48 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Some soluble cuticular proteins are conjugated to GlcNAc [25]. Chitin itself is in part covalently bound with proteins in the cuticle [26-291 and can be regarded as an aminoglycoprotein [30].…”

Section: Discussionmentioning

confidence: 99%

“…Ten microliters were used for measurement of radioactivity in a liquid scintillation counter, and 50 pl was eluted on a HPLC gel filtration column according to the procedure described above. Fractions were collected every minute for 25 min, and radioactivity in each fraction was measured. Aliquots (10 1.…”

Section: Effect Of 20e Treatment On Gicnac Processing By Imaginal Dismentioning

confidence: 99%

See 1 more Smart Citation

Ecdysteroid‐stimulated synthesis and secretion of an N‐acetyl‐D‐glucosamine‐rich glycopeptide in a lepidopterna cell line derived from imaginal discs

Porcheron

Morinière

Coudouel

et al. 1991

Arch Insect Biochem Physiol

View full text Add to dashboard Cite

Hormone-regulated processing of N-acetyl-D-glucosamine was studied in an insect cell line derived from imaginal wing discs of the Indian meal moth, Plodia interpunctella (Hübner). The cell line, IAL-PID2, responded to treatment with 20-hydroxyecdysone with increased incorporation of GlcNAc into glycoproteins. Cycloheximide and tunicamycin counteracted the action of the hormone. In particular, treatment with 20-hydroxyecdysone resulted in the secretion of a 5,000 dalton N-acetyl-D-glucosamine-rich glycopeptide by the IAL-PID2 cells. Accumulation of this peptide was prevented by the use of teflubenzuron, a potent chitin synthesis inhibitor. A glycopeptide of similar molecular weight was observed in imaginal discs of P. interpunctella treated with 20-hydroxyecdysone in vitro, under conditions that induce chitin synthesis. Although the function of the 5,000 dalton glycopeptide is not known, we believe that the PID2 cell line is a promising model for molecular analysis of ecdysteroid-regulated processing of aminosugars by epidermal cells during insect development.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Effect Of 20e Treatment On Gicnac Processing By Imaginal Dismentioning

confidence: 99%

Ecdysteroid‐stimulated synthesis and secretion of an N‐acetyl‐D‐glucosamine‐rich glycopeptide in a lepidopterna cell line derived from imaginal discs

Porcheron

Morinière

Coudouel

et al. 1991

Arch Insect Biochem Physiol

View full text Add to dashboard Cite

show abstract

“…The details have been published [22], and the end result is that we failed to find any evidence for mammalian-type glycosaminoglycans in Cecropia cuticle. Since we completed this work, studies have been published showing glycosaminoglycans in various other insect preparations [25,26].…”

Section: Introductionmentioning

confidence: 90%

Cuticular proteins: The neglected component

Willis

1987

Arch Insect Biochem Physiol

Self Cite

View full text Add to dashboard Cite

This paper emphasizes the importance of the protein component of cuticles.Correlation of electrophoretic charge distribution of individual cuticular proteins and physical properties of the cuticles from which they were extracted, as well as interpopulation and interspecies conservation of electrophoretic patterns, are used to argue that individual proteins play precise roles in the cuticle. Glycosylation of cuticular proteins is described, but no function for these modifications is yet known. Analogy is drawn to analyses of chorion proteins and the case i s made that analysis of amino acid sequence data is likely to provide insights into how cuticular proteins and chitin interact to construct the diverse types of cuticles.

show abstract

“…The proteins resemble the exocuticular proteins in the lack of sulphur-containing amino acids and a relatively high content of proline. The main differences are low isoelectric points (PI 4 -6) and high contents of hydrophilic amino acids in endocuticular proteins.The presence of glycosylated proteins in soft larval lepidopteran cuticle has been described [4], but the specific glycosylation sites and the detailed structures of the glycosyl residues have not been reported. We have now determined the complete structure of a glycosylated endocuticular protein, Correspondence to P.…”

mentioning

confidence: 99%

“…The presence of glycosylated proteins in soft larval lepidopteran cuticle has been described [4], but the specific glycosylation sites and the detailed structures of the glycosyl residues have not been reported. We have now determined the complete structure of a glycosylated endocuticular protein, Correspondence to P. Roepstorff Ahhreviutions.…”

mentioning

confidence: 99%

Determination of the covalent structure of an N‐ and C‐terminally blocked glycoprotein from endocuticle of Locusta migratoria

Talbo¹,

Højrup²,

Rahbek-Nielsen³

et al. 1991

European Journal of Biochemistry

View full text Add to dashboard Cite

The complete structure of a protein isolated from endocuticle of sexually mature locusts, Locusta migratoria, has been determined by a combination of automatic Edman degradation and plasma desorption mass spectrometry. The protein is extensively post-translationally modified. The N-terminal is 5-oxoproline (pyroglutamic acid) and the C-terminal proline residue is amidated. Furthermore, the protein is glycosylated by a single N-acetylgalactosamine residue at one, two or three threonines. The N-terminal sequence was obtained by analysing the N-acetylated N,O-permethylated derivative using plasma desorption mass spectrometry. The position and type of carbohydrate were determined by combining an HPLC-based carbohydrate analysis with the peak pattern of the phenylthiohydantoin derivative in automatic sequencing and with mass information on peptides.The protein has pronounced similarity to cuticular proteins from larvae of diptera and lepidoptera, but only slight resemblance to the previously sequenced locust exocuticular proteins. This indicates a similarity between soft larval cuticles and locust endocuticle, a similarity which may extend to their mechanical properties.Locust cuticle consists of a relatively soft endocuticle, which contains mainly acidic proteins, and a harder exocuticle, containing more basic proteins [l]. The proteins in the exocuticle of the migratory locust Locusta migratoria can only be extracted immediately after ecdysis, before cuticular sclerotization is initiated. Several of the exocuticular proteins have been purified and a few have been sequenced using a combination of "' Cf plasma desorption mass spectrometry and Edman degradation [2, 31. The extractable, endocuticular proteins from mature locust abdominal cuticle have been characterised using gel electrophoresis and amino acid analysis [l]. The proteins resemble the exocuticular proteins in the lack of sulphur-containing amino acids and a relatively high content of proline. The main differences are low isoelectric points (PI 4 -6) and high contents of hydrophilic amino acids in endocuticular proteins.The presence of glycosylated proteins in soft larval lepidopteran cuticle has been described [4], but the specific glycosylation sites and the detailed structures of the glycosyl residues have not been reported. We have now determined the complete structure of a glycosylated endocuticular protein, Correspondence to P.

show abstract

Post-translational modifications of the cuticular proteins of Hyalophora cecropia from different anatomical regions and metamorphic stages

Cited by 33 publications

References 48 publications

Ecdysteroid‐stimulated synthesis and secretion of an N‐acetyl‐D‐glucosamine‐rich glycopeptide in a lepidopterna cell line derived from imaginal discs

Ecdysteroid‐stimulated synthesis and secretion of an N‐acetyl‐D‐glucosamine‐rich glycopeptide in a lepidopterna cell line derived from imaginal discs

Cuticular proteins: The neglected component

Determination of the covalent structure of an N‐ and C‐terminally blocked glycoprotein from endocuticle of Locusta migratoria

Contact Info

Product

Resources

About