Involvement of tyrosine residues, N-terminal amino acids, and β-alanine in insect cuticular sclerotization

Andersen, Svend Olav

doi:10.1016/j.ibmb.2007.05.002

Cited by 25 publications

(22 citation statements)

References 11 publications

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“…Mild acid hydrolysis of cuticles from various insect species have yielded adducts containing amino acid residues linked to the a-position of 3,4-dihydroxyacetophenone (Andersen and Roepstorff, 2007;Andersen, 2007). The amino acids include lysine, linked via its 3-amino group (XXVI), glycine and b-alanine, linked via their amino groups (XXVII and XXVIII), and tyrosine, linked via its phenolic group (XXIX).…”

Section: Adduct Formation During In Vivo Sclerotizationmentioning

confidence: 99%

“…As the adducts contain an amino acid linked to the a-position and a keto-group in the b-position, it was suggested that they were produced by hydrolytic degradation of NADA-derived cuticular crosslinks having both sidechain positions involved in linkage to proteins. A possible way for producing the degradation products from such crosslinks has been suggested (Andersen and Roepstorff, 2007;Andersen, 2007).…”

Section: Adduct Formation During In Vivo Sclerotizationmentioning

confidence: 99%

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Insect cuticular sclerotization: A review

Andersen

2010

Insect Biochemistry and Molecular Biology

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426

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Section: Adduct Formation During In Vivo Sclerotizationmentioning

confidence: 99%

Section: Adduct Formation During In Vivo Sclerotizationmentioning

confidence: 99%

Insect cuticular sclerotization: A review

Andersen

2010

Insect Biochemistry and Molecular Biology

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490

426

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“…The 3,4-dihydroxyacetophenone adducts which contain an amino acid residue linked to the a-position were suggested to be degradation products of the crosslinks formed when oxidized dehydro-NADA reacted with cuticular proteins (Andersen and Roepstorff, 2007;Andersen, 2007).…”

Section: Discussionmentioning

confidence: 99%

“…Both types of quinones may react with nucleophilic groups (such as histidine) present in the cuticular proteins to give ring-substituted adducts (7) and sidechain-substituted adducts (8), respectively. The NADA p-quinone methide (3) can also be rearranged to dehydro-NADA (4), which after oxidation to quinones (5 and 6) may react with available catechols to give dihydroxyphenyl-dihydrobenzodioxine derivatives (9) or with two nucleophilic groups (HX and HY), which are thereby crosslinked (10) (Modified from Andersen, 2007).…”

Section: Methodsmentioning

confidence: 99%

“…3) which, respectively, contain glycine, b-alanine, lysine, and tyrosine residues linked to the a-position of 3,4-dihydroxyacetophenone, were obtained from adult cuticles of S. gregaria and T. molitor, and it was argued that they were degradation products of crosslinks where both the a-and the b-position of NADA were involved in linkages to the proteins (Andersen, 2007). The results reported by Kramer et al (2001) showed that insect cuticles differ significantly in the yields of various catecholic hydrolysis products, indicating that they differ both in degree of sclerotization and in the quinones involved in the reactions.…”

Section: Introductionmentioning

confidence: 99%

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Quantitative determination of catecholic degradation products from insect sclerotized cuticles

Andersen

2008

Insect Biochemistry and Molecular Biology

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Variation among arthropod taxa in the amino acid content of exoskeleton and digestible tissue

Reeves

Herzog

Barnes

et al. 2023

Ecology and Evolution

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Arthropod consumption provides amino acids to invertebrates and vertebrates alike, but not all amino acids in arthropods may be digestible as some are bound in the exoskeleton. Consumers may not be able to digest exoskeleton in significant amounts or avoid it entirely (e.g., extraoral digestion). Hence, measures that do not separate digestible amino acids from those in exoskeleton may not accurately represent the amino acids available to consumers. Additionally, arthropods are taxonomically diverse, and it remains unclear if taxonomic differences also reflect differences in amino acid availability. Thus, we tested: (1) if there were consistent differences in the content and balance of amino acids between the digestible tissue and exoskeleton of arthropods and (2) if arthropod Orders differ in amino acid content and balance. We measured the amino acid content (mg/100 mg dry mass) and balance (mg/100 mg protein) of whole bodies and exoskeleton of a variety of arthropods using acid hydrolysis.Overall, there was higher amino acid content in digestible tissue. There were also significant differences in the amino acid balance of proteins in digestible tissue and exoskeleton. Amino acid content and balance also varied among Orders; digestible tissues of Hemiptera contained more of some essential amino acids than other Orders. These results demonstrate that arthropod taxa vary in amino acid content, which could have implications for prey choice by insectivores. In addition, exoskeleton and digestible tissue content differ in arthropods, which means that whole body amino acid content of an arthropod is not necessarily a predictor of amino acid intake of a predator that feeds on that arthropod.

show abstract

Involvement of tyrosine residues, N-terminal amino acids, and β-alanine in insect cuticular sclerotization

Cited by 25 publications

References 11 publications

Insect cuticular sclerotization: A review

Insect cuticular sclerotization: A review

Quantitative determination of catecholic degradation products from insect sclerotized cuticles

Variation among arthropod taxa in the amino acid content of exoskeleton and digestible tissue

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