Binding of riboflavin to lipophorin and a hexameric protein in the hemolymph of Heliothis virescens

Miller, Stephen G.; Silhacek, Donald L.

doi:10.1016/0965-1748(92)90034-c

Cited by 15 publications

(8 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Previous research in both flies (Levenbook & Baur 1984) and moths (Huebers et al. 1988; Miller & Silhacek 1992; Wu & Tischler 1995) has shown that amino acids, iron, and riboflavin from LSPs are used to synthesize adult tissues, with nearly 50% of radiolabelled LSP amino acids incorporated in flight muscle proteins (Levenbook & Baur 1984). Positive effects of protein mobilization on both oogenesis and flight performance provides a mechanistic hypothesis for the absence of a trade‐off between dispersal and fecundity in this species (Hanski et al.…”

Section: Discussionmentioning

confidence: 99%

Functional genomics of life history variation in a butterfly metapopulation

et al. 2011

View full text Add to dashboard Cite

In fragmented landscapes, small populations frequently go extinct and new ones are established with poorly understood consequences for genetic diversity and evolution of life history traits. Here, we apply functional genomic tools to an ecological model system, the well-studied metapopulation of the Glanville fritillary butterfly. We investigate how dispersal and colonization select upon existing genetic variation affecting life history traits by comparing common-garden reared 2-day adult females from new populations with those from established older populations. New-population females had higher expression of abdomen genes involved in egg provisioning and thorax genes involved in the maintenance of flight muscle proteins. Physiological studies confirmed that new-population butterflies have accelerated egg maturation, apparently regulated by higher juvenile hormone titer and angiotensin converting enzyme mRNA, as well as enhanced flight metabolism. Gene expression varied between allelic forms of two metabolic genes (Pgi and Sdhd), which themselves were associated with differences in flight metabolic rate, population age and population growth rate. These results identify likely molecular mechanisms underpinning life history variation that is maintained by extinction-colonization dynamics in metapopulations.

show abstract

Section: Discussionmentioning

confidence: 99%

Functional genomics of life history variation in a butterfly metapopulation

et al. 2011

View full text Add to dashboard Cite

show abstract

“…Thus, failure to produce RbH during the last larval instar might not seriously diminish the amino acid reserves available for adult developoment. Since the riboflavin-storing function of this protein can be served by lipophorin (Miller and Silhacek, 1992;Magee et al, 1994), its only known ligand-binding function is also replaceable. The question then becomes not so much how other species get along without RbH, but how its persistence can be accounted for in those species that still produce it.…”

Section: Fig 4 Comparison Of Arh As a Storage Site For [mentioning

confidence: 99%

Equivalence of riboflavin-binding hexamerin and arylphorin as reserves for adult development in two saturniid moths

Pan

Telfer

1999

Arch. Insect Biochem. Physiol.

View full text Add to dashboard Cite

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. Arch. Insect Biochem. Physiol. 42:138–146, 1999. © 1999 Wiley‐Liss, Inc.

show abstract

mentioning

confidence: 99%

“…The hexamerin superfamily includes insect hemolymph proteins as well as hemocyanins of crustaceans, chelicerates and myriapods [1]. In contrast to the established function of hemocyanins as copper-binding oxygen carriers [2], the insect hexamerins perform several functions, such as amino acid reservoirs (storage proteins) for non-feeding developmental stages [3Ϫ7], as a major yolk protein [8,9], and as binding proteins for riboflavin [10,11] and juvenile hormone (JH) [12].Insect hexamerins so far sequenced have been classified into the following five groups primarily based on amino acid sequence alignment [13,14]: (a) lepidopteran methionine-rich hexamerins; (b) lepidopteran aromatic-amino-acid-rich arylphorins ; (c) lepidopteran JH-suppressible hexamerins; (d) dipteran arylphorins; (e) coleopteran and dictyopteran JH-suppressible arylphorins. Our present understanding of insect hexamerins, thus, is mainly from the studies on higher endopterygote insect orders.…”

mentioning

confidence: 99%

Two hexameric cyanoprotein subunits from an insect, Riptortus clavatus

Miura

Shinoda

Yura

et al. 1998

European Journal of Biochemistry

View full text Add to dashboard Cite

Hemolymph of a hemipteran insect, Riptortus clavatus, contains four distinct hexameric proteins (cyanoproteins) composed of two distinct subunits, CPA and CPβ, which show profiles of abundance depending on developmental stage, diapause status controlled by juvenile hormone, and sex. We have isolated cDNA clones encoding the two subunits and determined the complete sequences. The nucleotide sequences predict polypeptides of 693 and 691 residues for CPA and CPβ, respectively, including identical 16-residue signal peptides. The deduced amino acid sequences of both CPA and CPβ have significant similarity to other hemocyanin-related proteins, indicating that the cyanoproteins represent hexamerins. Phylogenetic analyses show that the cyanoprotein subunits can be grouped together with other hexamerins from exopterygote insects. Developmental Northern-blot analyses suggest that the expression of the cyanoproteins is regulated at the level of transcript abundance. In addition, the expression of the CPA subunit in female adults has been shown to be enhanced by juvenile hormone (JH) while the expression of the CPβ subunit is suppressed by the same hormone. To our knowledge, the CPA subunit of R. clavatus is the first case of a JH-enhanceable hexamerin whose sequence has been determined.Keywords : insect; hexamerin; juvenile hormone regulation; molecular phylogeny.The hexamerins are arthropod hexameric or multi-hexameric serum proteins composed of identical or distinct subunits with molecular masses of around 80 kDa. The hexamerin superfamily includes insect hemolymph proteins as well as hemocyanins of crustaceans, chelicerates and myriapods [1]. In contrast to the established function of hemocyanins as copper-binding oxygen carriers [2], the insect hexamerins perform several functions, such as amino acid reservoirs (storage proteins) for non-feeding developmental stages [3Ϫ7], as a major yolk protein [8,9], and as binding proteins for riboflavin [10,11] and juvenile hormone (JH) [12].Insect hexamerins so far sequenced have been classified into the following five groups primarily based on amino acid sequence alignment [13,14]: (a) lepidopteran methionine-rich hexamerins; (b) lepidopteran aromatic-amino-acid-rich arylphorins ; (c) lepidopteran JH-suppressible hexamerins; (d) dipteran arylphorins; (e) coleopteran and dictyopteran JH-suppressible arylphorins. Our present understanding of insect hexamerins, thus, is mainly from the studies on higher endopterygote insect orders. Recently, several research groups have reported the cDNA cloning of proenzymes of insect and crustacean pheCorrespondence to K. Miura, Department of Medical Zoology, School of Medicine, Mie University, 2-174 Edobashi, Tsu City, Japan 514Fax: ϩ81 59 231 5215. E-mail: k-miura@doc.medic.mie-u.ac.jp Abbreviations. CP, cyanoprotein; JH, juvenile hormone; JHA, juvenile hormone analog.Note. The nucleotide sequence data of CPA and CPβ reported in this paper appear in the GSDB, DDBJ, EMBL and NCBI nucleotide sequence databases with the accession numbers D87272 an...

show abstract

Binding of riboflavin to lipophorin and a hexameric protein in the hemolymph of Heliothis virescens

Cited by 15 publications

References 34 publications

Functional genomics of life history variation in a butterfly metapopulation

Functional genomics of life history variation in a butterfly metapopulation

Equivalence of riboflavin-binding hexamerin and arylphorin as reserves for adult development in two saturniid moths

Two hexameric cyanoprotein subunits from an insect, Riptortus clavatus

Contact Info

Product

Resources

About