Biochemical and Immunological Studies on Larval Serum Protein 1, the Major Haemolymph Protein of <i>Drosophila melanogaster</i> Third‐Instar Larvae

Wolfe, Jonathan; Akam, Michael; Roberts, David

doi:10.1111/j.1432-1033.1977.tb11782.x

Cited by 67 publications

(23 citation statements)

References 23 publications

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“…Gel purified subunits were eluted from the gel slices, oxidised, and digested with trypsin for 5 h at 37 "C. The resulting peptides were analysed on silica gel thin-layer plates using electrophoresis at pH 3.5 in the first dimension and chromatography with butanol/acetic acid/water/pyridine (15: 3 : 12: 10). The peptides were detected by autoradiography after exposure for one week [26-291 from the methionine content of LSP-1 and LSP-2 [8]. These results together suggest that the observed methionine-containing peptides are specific products of tryptic digestion.…”

Section: Two-dimensional Pep Tide Mappingmentioning

confidence: 84%

“…LSP-1 is a heterohexamer composed of the apparently random association of three different subunits, designated a (83000 M J , b (80000 M,) and y (77000 M,), whereas LSP-2 is a homohexamer with one 80000-M, subunit [8,9]. LSP-2 is glycosylated, and the p and y subunits of LSP-1 are phosphorylated (Brock and Roberts, unpublished results).…”

mentioning

confidence: 99%

“…LSP-1 and LSP-2 have similar amino acid compositions [lo]. The a, fJ and y subunits of LSP-1 share common antigenic sites as well as each possessing unique sites, but antisera prepared against LSP-1 subunits do not cross-react with LSP-2 and vice versa [8].…”

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confidence: 99%

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Comparison of the Larval Serum Proteins of Drosophila melanogaster

Brock

Roberts

1980

European Journal of Biochemistry

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Immunological data, amino acid composition, and coordinate control during development suggest that the a, fJ and y subunits of the major protein of Dvosophilu larval serum (LSP-1) are coded for by genes which evolved by replications of an ancestral gene followed by mutation. In order to test this hypothesis, and to study the relationship of these genes with that coding for the second major larval serum protein (LSP-2), we compared the one and two-dimensional peptide maps of all four larval serum protein subunits. One-dimensional maps generated by three different proteases showed many similarities among these proteins. Two-dimensional peptide mapping of the methionine-containing tryptic peptides showed that half of these peptides are common to all four larval serum protein subunits, and that about two-thirds are common to the three LSP-1 subunits. These observations show that the LSP-1 subunits are more closely related to each other than any is to LSP-2, and supported the initial suggestion that the proteins are homologous. Because the genes for the LSP-1 subunits are each located on a different chromosome, the LSP-1 subunits are a suitable system for investigating the evolution and dispersal of related genes, and trans control in eu karyo tes.The larval serum proteins (LSP) of Dvosophilu melunogustev make up 70% of the late third-instar larval haemolymph protein [l], and are synthesized exclusively by the fat body (Sato and Roberts, unpublished results). These proteins are amenable to genetic and biochemical analysis, and are being studied in order to understand the control of their synthesis.

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Section: Two-dimensional Pep Tide Mappingmentioning

confidence: 84%

mentioning

confidence: 99%

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Comparison of the Larval Serum Proteins of Drosophila melanogaster

Brock

Roberts

1980

European Journal of Biochemistry

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“…Diferentes tipos celulares podem ocorrer, porém, os mais comuns são os trofócitos (ou adipócitos) e enócitos, funcionalmente diversificados e capazes de armazenar glicogênio, lipídeos e proteínas. (KILBY, 1963;LOCKE e COLLINS, 1966e 1968BUTTERWORTH et al, 1965;PRICE, 1973;WIGGLESWORTH, 1974;WOLFE et al, 1977;DEAN et. al., 1985;KEELEY, 1985;CHAPMAN, 1991;CRUZ-LANDIM e CONTE, 1992;CONTE, 1994;HAUNERLAND e SHIRK, 1995;CRUZ-LANDIM, 2004;ROMA, 2007;MARTINS, 2008;CRUZ-LANDIM, 2009).…”

Section: Introductionunclassified

Morfo-histologia do corpo gorduroso perivisceral em adultos de Hedypathes betulinus (Klug, 1825) (Coleoptera, Cerambycidae)

2011

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ResumoNos insetos, o corpo gorduroso pode ser considerado um centro de metabolismo intermediário e também o local de síntese de alguns componentes da hemolinfa. Com objetivo de obter maiores informações sobre essa estrutura, foi realizado um estudo para a sua caracterização morfológica em adultos de Hedypathes betulinus Klug. Os resultados mostram que a estrutura ocorre em duas porções, a primeira, aderida ao trato digestivo e a segunda, associada ao tegumento, denominando-se, corpo gorduroso perivisceral e parietal, respectivamente. Histologicamente o corpo gorduroso apresenta dois tipos celulares, os trofócitos e os enócitos. Os trofócitos apresentam na área citoplasmática, vacúolos, núcleos esféricos, cromatina granular com variações na condensação, e em alguns casos, foram observados núcleos deslocados para a periferia celular. A presença de nucléolos múltiplos em algumas células sugere alta atividade nuclear. Os enócitos foram observados associados aos trofócitos, com núcleos centrais de formato esférico e cromatina de aspecto granular dispersa; os nucléolos apresentaram-se proeminentes em número variável e diferem dos trofócitos pela ausência de vacúolos, citoplasma granular, formato e tamanho das células.

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“…The first group, represented by the prototypical Calliphorin of Calliphora vicina (Munn and Greville, 1969) and the D. melanogaster larval serum protein 1 (LSP-1) (Wolfe et al, 1977), is expressed exclusively during the larval stage and its major function appears to be to supply amino acids for the synthesis of adult tissues during metamorphosis (Levenbook and Bauer, 1984; Telfer and Kunkel, 1991). The second group, represented by the prototype D.…”

Section: Introductionmentioning

confidence: 99%

Primary characterization and basal promoter activity of two hexamerin genes of Musca domestica

Moreira

Capurro

Walter

et al. 2004

Journal of Insect Science

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Hexamerins are high molecular-weight proteins found in the hemolymph of insects and have been proposed to function as storage proteins. In previous studies, two Musca domestica hexamerins, designated Hex-L and Hex-F were characterized. Hex-L is synthesized exclusively by the larval fat bodies, is secreted into the hemolymph and likely provides a source of amino acids and energy during metamorphosis. Hex-F synthesis is induced by a proteinaceous meal and occurs only in the adult insect fat bodies. Hex-F also is secreted into the hemolymph and it has been suggested that in females it may be an amino acid reservoir to be used during the final stages of egg formation. Genomic clones containing full-length copies of the genes MdHexL1 and MdHexF1, encoding subunits of the larval and the adult female hexamerin, respectively, were isolated. Complete nucleotide sequences, including the 5′-end untranscribed regions, were determined and analyzed for each of the genes. Comparisons of the conceptual translation products of the cloned genes indicated that MdHexL1 and MdHexF1 are related to the larval serum proteins (LSP) 1 and 2 of Calliphora vicina and Drosophila melanogaster. DNA fragments containing the putative promoters of the two hexamerin genes were compared and cloned into a plasmid vector so as to drive the expression of the GFP reporter gene. The constructs were assayed in vitro in transfected S2 Drosophila melanogaster cells demonstrating that the cloned M. domestica DNA fragments exhibit promoter activity.Abbreviation:Hex L, Hex FLarval and female hexamerins respectivelyLSPLarval serum proteinMdHexL1, MdHexF1hexamerins of Musca domestica

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Biochemical and Immunological Studies on Larval Serum Protein 1, the Major Haemolymph Protein of Drosophila melanogaster Third‐Instar Larvae

Cited by 67 publications

References 23 publications

Comparison of the Larval Serum Proteins of Drosophila melanogaster

Comparison of the Larval Serum Proteins of Drosophila melanogaster

Morfo-histologia do corpo gorduroso perivisceral em adultos de Hedypathes betulinus (Klug, 1825) (Coleoptera, Cerambycidae)

Primary characterization and basal promoter activity of two hexamerin genes of Musca domestica

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