Pan M L, Telfer W H
Department of Ecology and Evolutionary Biology, University of Tennessee, Knoxville, TN 37996-1610, USA.
Arch Insect Biochem Physiol. 1999 Oct;42(2):138-46. doi: 10.1002/(SICI)1520-6327(199910)42:2<138::AID-ARCH4>3.0.CO;2-1.
The riboflavin-binding hexamerin (RbH) and arylphorin (ArH) were compared as storage reservoirs for adult development in Hyalophora cecropia. The two hexamerins were metabolically labeled with [3H]leucine and [35S]methionine, isolated by column chromatography, and separately injected into pupae whose diapause had been terminated by chilling. By the time of eclosion at least 98% of both hexamerins had been cleared from the hemolymph. Every reproductive and somatic tissue tested contained trichloroacetic acid-precipitable label; consistent differences between the two hexamerins were not detected in the distribution of their label to these tissues. While incorporation of intact hexamerins was not ruled out, hydrolysis and reincorporation of the liberated amino acids were indicated by label in vitellogenin and lipophorin, and by differences in 35S/3H ratios, which ranged from over 1.0 in chorions to 0.4 in wings, as compared with 0.75 in the injected hexamerins. Injection of [35S,3H]RbH from H. cecropia into A. luna, a species in the same subfamily whose pupae lack this hexamerin, resulted in a pattern of isotope incorporation similar to that yielded by RbH in the donor species. In neither species was there indication of a developing adult tissue that distinguished between RbH and ArH as precursor reservoirs for morphogenesis. This equivalence helps explain how many species of Lepidoptera are able to complete metamorphosis and reproduce without expressing an RbH gene. Evidence is also presented that ArH stored in the fat body protein granules during pupation may be utilized differently from that remaining in pupal hemolymph.
在天蚕中,对核黄素结合六聚体蛋白(RbH)和芳基蛋白(ArH)作为成虫发育的储存库进行了比较。用[³H]亮氨酸和[³⁵S]甲硫氨酸对这两种六聚体蛋白进行代谢标记,通过柱层析分离,然后分别注射到经低温处理已终止滞育的蛹中。到羽化时,两种六聚体蛋白至少98%已从血淋巴中清除。所测试的每个生殖和体细胞组织都含有三氯乙酸沉淀性标记;在这两种六聚体蛋白向这些组织的标记分布中未检测到一致的差异。虽然不排除完整六聚体蛋白的掺入,但卵黄原蛋白和脂磷蛋白中的标记以及³⁵S/³H比值的差异表明,释放的氨基酸发生了水解和再掺入,与注射的六聚体蛋白中的0.75相比,该比值在卵壳中超过1.0,在翅膀中为0.4。将来自天蚕的[³⁵S,³H]RbH注射到同一亚科的月神蛾中,该种蛹缺乏这种六聚体蛋白,其同位素掺入模式与供体物种中RbH产生的模式相似。在这两个物种中,均未发现发育中的成虫组织能区分RbH和ArH作为形态发生的前体储存库。这种等效性有助于解释为什么许多鳞翅目物种能够在不表达RbH基因的情况下完成变态和繁殖。还提供了证据表明,化蛹期间储存在脂肪体蛋白颗粒中的ArH与蛹血淋巴中剩余的ArH利用方式可能不同。