Involvement of tyrosine residues, N-terminal amino acids, and β-alanine in insect cuticular sclerotization
Involvement of tyrosine residues, N-terminal amino acids, and β-alanine in insect cuticular sclerotization
复制标题
DOI：
10.1016/j.ibmb.2007.05.002
复制
发表时间：
2007-09-01
影响因子：
3.8
通讯作者：
Andersen, Svend Olav
中科院分区：
文献类型：
--
作者：
Andersen, Svend Olav
在昆虫表皮硬化过程中，酰基多巴胺、N-乙酰多巴胺（NADA）和N-β-丙氨酰多巴胺（NBAD）被氧化结合到表皮基质中，从而通过在表皮基质中的蛋白质之间形成交联和通过形成填充表皮中分子间空间的聚合物来硬化和稳定材料。从蝗虫，Schistocerca gregaria，和甲虫，黄粉虫，硬化角质层在稀盐酸中水解，并从水解产物中分离出一些成分，推测角质层交联的降解产物。在两种组分中，3，4-二羟基苯乙酮的侧链分别与甘氨酸和β-丙氨酸的氨基连接，而在第三种组分中，侧链与酪氨酸的酚基连接。这三种化合物，甘氨酸-二羟基苯乙酮、β-丙氨酸-二羟基苯乙酮和O-酪氨酸-二羟基苯乙酮，以及先前报道的化合物赖氨酸-二羟基苯乙酮[Andersen，S.O.，Roepstorff，P.，2007.蝗虫，Schistocerea gregaria和甲虫，黄粉虫表皮硬化的方面。昆虫生物化学分子37，223-234]，被认为是表皮交联的降解产物，其中氨基酸残基与酰基多巴胺侧链的α-和β-位置形成连接。(c)2007爱思唯尔有限公司版权所有。
During sclerotization of insect cuticle the acyldopamines, N-acetyldopamine (NADA) and N-beta-alanyldopamine (NBAD), are oxidatively incorporated into the cuticular matrix, thereby hardening and stabilizing the material by forming crosslinks between the proteins in the cuticular matrix and by forming polymers filling the intermolecular spaces in the cuticle. Sclerotized cuticle from the locust, Schistocerca gregaria, and the beetle, Tenebrio molitor, was hydrolyzed in dilute hydrochloric acid, and from the hydrolysates some components presumably degradation products of cuticular crosslinks were isolated. In two of the components, the sidechain of 3,4dihydroxyacetophenone was linked to the amino groups of glycine and beta-alanine, respectively, and in the third component to the phenolic group of tyrosine. These three compounds, glycino-dihydroxyacetophenone, beta-alanino-dihydroxyacetophenone, and O-tyrosino-dihydroxyacetophenone, as well as the previously reported compound, lysino-dihydroxyacetophenone [Andersen, S.O., Roepstorff, P., 2007. Aspects of cuticular sclerotization in the locust, Schistocerea gregaria, and the beetle, Tenebrio molitor. Insect Biochem. Mol. Biol. 37, 223-234], are suggested to be degradation products of cuticular crosslinks, in which amino acid residues formed linkages to both the alpha- and beta-positions of the sidechain of acyldopamines. (c) 2007 Elsevier Ltd. All rights reserved.