Butterfly wings, a new site of porphyrin synthesis and cleavage: Studies on the expression of the lipocalin bilin-binding protein in Pieris brassicae

Sehringer, Bernd; Kayser, Hartmut

doi:10.1016/j.ibmb.2006.03.005

Cited by 5 publications

(8 citation statements)

References 22 publications

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“…Their identity was confirmed by MS and oxidative degradation . Biliverdin IXγ was also isolated from the wings of the butterfly P. brassicae . Commercial biliverdin IXα hydrochloride was used a reference.…”

Section: Methodsmentioning

confidence: 99%

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Structure of a novel farnesylated bilin from an insect – formation by α‐cleavage of heme A of mitochondrial cytochrome c oxidases?

2014

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Biliproteins are present in almost all forms of life, and many of them play vital roles in photobiology. The bilin ligand of a recently characterized 500‐kDa biliprotein from an insect has been isolated and its structure elucidated with chemical and spectroscopic techniques (UV–visible, IR, MS, NMR, and CD). This blue pigment, named CV‐bilin, represents a unique high molecular mass derivative of biliverdin IXα, with an unusual 10E‐configuration and a molecular mass of 852 Da, corresponding to C48H60N4O10. The high mass of this open‐chain tetrapyrrole results from the presence of an epoxi‐dihydroxyethylfarnesyl substituent at C‐18 and a hydroxymethyl substituent at C‐13. This substitution pattern exactly reflects that of heme A of mitochondrial cytochrome c oxidases with a hydroxyethylfarnesyl chain and a formyl group at corresponding positions of the cyclic tetrapyrrole. As no other natural product is known to show these structural features (heme O, the precursor of heme A, has a methyl group at C‐13), this bilin is presumed to be derived from heme A by cleavage of the α‐methine bridge and oxidative modifications at C‐13 and the hydroxyethylfarnesyl chain. Possibly, a bilin structurally related to this insect bilin is also produced in other organisms as a result of mitochondrial turnover or degradation. As CV‐bilin in complex with a specific protein is accumulated at the end of larval life, stored in the pupa, and finally transferred to the oocytes, a possible role of the free or protein‐bound pigment in egg or embryonic development is discussed.

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Section: Methodsmentioning

confidence: 99%

“…The bilin was isolated with Method 1, and an aliquot was methylated. [ 14 C]5‐ALA‐labeled biliverdin IXγ was prepared from developing wings of P. brassicae . 14 C‐labeled products of microchemical degradation on TLC plates were detected by autoradiography with a Fuji‐Film FLA3000 Phospho Imager (Fuji Photo Film Co., Tokyo, Japan).…”

Section: Methodsmentioning

confidence: 99%

Structure of a novel farnesylated bilin from an insect – formation by α‐cleavage of heme A of mitochondrial cytochrome c oxidases?

2014

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“…Lepidopteran Lipocalins like Bilin binding protein from Pieris brasssicae and Samia cynthia or Insecticyanin from Manduca sexta are expressed in epidermis, and some of them have been demonstrated to play roles in cuticle coloration (Riddiford et al, 1990;Saito, 1998;Sehringer and Kayser, 2006) and prevention of oxidative damage (Schmidt and Skerra, 1994). Brain Lipocalins have been identified both in Diptera and Lepidoptera.…”

Section: Introductionmentioning

confidence: 99%

Grasshopper Lazarillo, a GPI-anchored Lipocalin, increases Drosophila longevity and stress resistance, and functionally replaces its secreted homolog NLaz

Ruiz

Wicker-Thomas

Sánchez

et al. 2012

Insect Biochemistry and Molecular Biology

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“…BBP is also a member of the lipocalin family, extracellular proteins sharing several molecular ligand properties: the binding of small, principally lipophilic molecules such as retinol []. They have been categorized mainly as transport proteins, but it is obvious that members of the lipocalin family carry out a wide variety of different functions such as retinol transport, invertebrate cryptic coloration, olfaction, and pheromone transport [].…”

Section: Introductionmentioning

confidence: 99%

“…Biliproteins belonging to this family have been widely found in various insect orders and these proteins have been purified and characterized from their hemolymph in number of species []. Blue biliproteins can be classified into three groups according to the molecular weight of subunits.…”

Section: Introductionmentioning

confidence: 99%

Mass spectrometrical analysis of bilin‐binding protein from the wing of Hebomoia glaucippe (Linnaeus, 1758) (Lepidoptera: Pieridae)

et al. 2012

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Bilin-binding protein (BBP) is a member of the lipocalin superfamily and a pigment protein in Lepidoptera. It is binding to a series of lipidic compounds but its functions remain to be elucidated. Working on wing proteins in Hebomoia glaucippe, we observed this protein on gels and decided to characterize BBP. A gel-based mass spectrometrical method using two-dimensional gel electrophoresis followed by in-gel digestion of protein spots followed by nano-LC-ESI-MS/MS (ion trap, HCT) identification and characterization of proteins was applied. An antibody was generated against the protein and immunoblotting in the butterfly and mouse brain was carried out. Two spots were identified from the butterfly wing as BBP (P09464) with high sequence coverage. Nitrotyrosination (Y163; as aminotyrosine) was observed and nitration was verified using immunoblotting. Additional posttranslational modifications (PTMs) as hypusine, carboxylation, kynurenine, aminoadipic acid, were proposed. The presence of BBP-immunoreactive protein was also observed in mouse brain. The characterization of BBP showed high sequence similarity with mouse apolipoprotein D and the findings suggest a tentative function of BBP comparable to apolipoproteins. The role of the PTMs remains elusive but nitration, in analogy to nitration effects reported in literature, proposes a role for mechanoelastic proteins and protein-protein interactions.

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Butterfly wings, a new site of porphyrin synthesis and cleavage: Studies on the expression of the lipocalin bilin-binding protein in Pieris brassicae

Cited by 5 publications

References 22 publications

Structure of a novel farnesylated bilin from an insect – formation by α‐cleavage of heme A of mitochondrial cytochrome c oxidases?

Structure of a novel farnesylated bilin from an insect – formation by α‐cleavage of heme A of mitochondrial cytochrome c oxidases?

Grasshopper Lazarillo, a GPI-anchored Lipocalin, increases Drosophila longevity and stress resistance, and functionally replaces its secreted homolog NLaz

Mass spectrometrical analysis of bilin‐binding protein from the wing of Hebomoia glaucippe (Linnaeus, 1758) (Lepidoptera: Pieridae)

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