Cuticular proteins: The neglected component
- 1 December 1987
- journal article
- research article
- Published by Wiley in Archives of Insect Biochemistry and Physiology
- Vol. 6 (4) , 203-215
- https://doi.org/10.1002/arch.940060402
Abstract
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 is 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.Keywords
This publication has 41 references indexed in Scilit:
- Ecdysone regulation of cuticle protein gene expression inDrosophilaArchives of Insect Biochemistry and Physiology, 1986
- The paradigm of stage-specific gene sets in insect metamorphosis: Time for revision!Archives of Insect Biochemistry and Physiology, 1986
- The pupal cuticle of Drosophila: differential ultrastructural immunolocalization of cuticle proteins.The Journal of cell biology, 1986
- Gene within a gene: Nested Drosophila genes encode unrelated proteins on opposite DNA strandsCell, 1986
- Rapid and Sensitive Protein Similarity SearchesScience, 1985
- CartilageScientific American, 1984
- Cuticle protein genes of Drosophila: Structure, organization and evolution of four clustered genesCell, 1982
- Secondary structure predictions for silkmoth chorion proteinsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- Biochemistry of Insect CuticleAnnual Review of Entomology, 1979
- A study of the physical and chemical properties of the insect cuticleProceedings of the Royal Society of London. B. Biological Sciences, 1940