Insect Cuticular Chitin Contributes to Form and Function

Author(s): Subbaratnam Muthukrishnan*, Seulgi Mun, Mi Y. Noh, Erika R. Geisbrecht, Yasuyuki Arakane*

Journal Name: Current Pharmaceutical Design

Volume 26 , Issue 29 , 2020

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Chitin contributes to the rigidity of the insect cuticle and serves as an attachment matrix for other cuticular proteins. Deficiency of chitin results in abnormal embryos, cuticular structural defects and growth arrest. When chitin is not turned over during molting, the developing insect is trapped inside the old cuticle. Partial deacetylation of cuticular chitin is also required for proper laminar organization of the cuticle and vertical pore canals, molting, and locomotion. Thus, chitin and its modifications strongly influence the structure of the exoskeleton as well as the physiological functions of the insect.

Internal tendons and specialized epithelial cells called “tendon cells” that arise from the outer layer of epidermal cells provide attachment sites at both ends of adult limb muscles. Membrane processes emanating from both tendon and muscle cells interdigitate extensively to strengthen the attachment of muscles to the extracellular matrix (ECM). Protein ligands that bind to membrane-bound integrin complexes further enhance the adhesion between muscles and tendons. Tendon cells contain F-actin fiber arrays that contribute to their rigidity. In the cytoplasm of muscle cells, proteins such as talin and other proteins provide attachment sites for cytoskeletal actin, thereby increasing integrin binding and activation to mechanically couple the ECM with actin in muscle cells. Mutations in integrins and their ligands, as well as depletion of chitin deacetylases, result in defective locomotion and muscle detachment from the ECM. Thus, chitin in the cuticle and chitin deacetylases strongly influence the shape and functions of the exoskeleton as well as locomotion of insects.

Keywords: Chitin, cuticle, insects, deacetylation, molting, locomotion, muscle attachment.

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Article Details

Year: 2020
Page: [3530 - 3545]
Pages: 16
DOI: 10.2174/1381612826666200523175409
Price: $65

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