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Y Doi - One of the best experts on this subject based on the ideXlab platform.
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characterization of progressive changes in zpc of the Vitelline Membrane of quail oocyte following oviductal transport
Molecular Reproduction and Development, 2000Co-Authors: S Kido, Y Doi, Jianzhi Pan, Tomohiro Sasanami, Shizuka Nakajima, Makoto MoriAbstract:The inner layer of the Vitelline Membrane of avian oocyte is equivalent to the zona pellucida of mammalian oocytes or to the Vitelline envelope of amphibian oocytes. One of the two major glycoproteins in the inner layer of quail Vitelline Membrane, formerly called 33-kDa glycoprotein, is homologous to mammalian ZPC, one of the components of zona pellucida. Quail ZPC is found to have different mobilities on SDS-polyacrylamide gel electrophoresis depending on whether it is obtained from the preovulatory follicle or from the laid eggs. In order to characterize the progressive changes in the molecular size of quail ZPC during the oviductal transport, the inner layer isolated from the follicle was incubated in vivo in various regions of the oviduct and subjected to Western blot analysis with anti-quail ZPC antiserum. The quail ZPC of the inner layer incubated in infundibulum reduced its apparent molecular weight, exhibiting the same electrophoretic mobility as that of laid eggs. The similar reduction in molecular weight was observed after the in vitro incubation of the inner layer with the extracts of infundibulum. From the comparison of the N-terminal amino acid sequences, it was found that the first 26 residues of the quail ZPC in follicular oocytes are missing from the ZPC of laid eggs. In addition, lectin blot analysis suggested the modification of oligosaccharide chains during the oviductal transport. These results represent the first description in the avian oviduct of the presence of protease, which is similar to oviductin, a trypsin-like protease involved in the hydrolysis of a major component of the Vitelline envelope of amphibian oocytes. Mol. Reprod. Dev. 55:175–181, 2000. © 2000 Wiley-Liss, Inc.
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characterization of Vitelline Membrane outer layer protein i vmo i amino acid sequence and structural stability
Journal of Biochemistry, 1995Co-Authors: S Kido, Fimi Kim, Y Doi, Emi Morishita, Hiroshi Narita, Shigenori Kanaya, Tadayashu Ohkubo, Ken Nishikawa, Toru Yao, Tatsuo OoiAbstract:Vitelline Membrane outer layer protein I (VMO-I) tightly bound to ovomucin fibrils of hen's egg yolk Membrane was characterized in terms of its amino acid sequence and structural stability. The deduced sequence of VMO-I using the conventional sequencing method is: RTREYTSVITVPNGGHWGKWGIRQFCHSGYANGFALKVEPSQFGRDDTALNGIRLRCLD- GSVIESLVGKWGTWTSFLVCPTGYLVSFSLRSEKSQGGGDDTAANNIQFRCSDEAVLVGD- DLSWGRFGPWSKRCKICGLQTKVESPQGLRDDTALNNVRFFCCK. Thus, VMO-I is composed of 163 amino acid residues with a calculated molecular weight of 17,979. The sequence confirms the cDNA sequence of VMO-I we recently determined and does not show any significant similarity to proteins compiled in the NBRF database. Two of the four disulfide bonds found in VMO-I were estimated to lie between Cys26 and Cys57 and between Cys79 and Cys110. The sequence analyses show that VMO-I contains three 53-residue internal repeats that contain distinctive regions of turns flanked by beta-sheets consistent with the recent finding that the molecule contains a new beta-fold motif, the beta-prism. The molecular characteristics of VMO-I in solution were examined by CD spectroscopy in the far and near ultraviolet regions, NMR spectroscopy, and high sensitive differential scanning calorimetry (DSC). CD spectra in the far UV region at room temperature were similar to that assigned to a random coil, while in the near UV region, small positive peaks were observed. The ellipticity in both regions decreased on raising the temperature. Proton NMR experiments showed the native structure unfolds to unordered conformations at 70 degrees C.(ABSTRACT TRUNCATED AT 250 WORDS)
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cloning and sequencing of hen magnum cdnas encoding Vitelline Membrane outer layer protein i vmo i
Gene, 1994Co-Authors: Atsuko Uyeda, S Kido, Y Doi, Chikako Inuzuka, Masakazu KikuchiAbstract:Abstract Two cDNAs encoding hen Vitelline Membrane outer layer protein I (VMO-I), which is classified as a new type of multi-β-sheet assembly, were cloned and sequenced. Northern blot analysis using vmo-I cDNA as a probe showed the presence of three mRNA species. Strikingly, expression of these mRNAs was restricted to a specific region of the hen oviduct, the area joining the infundibulum to the magnum.
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crystal structure of Vitelline Membrane outer layer protein i vmo i a folding motif with homologous greek key structures related by an internal three fold symmetry
The EMBO Journal, 1994Co-Authors: Toshiyuki Shimizu, S Kido, Y Doi, D G Vassylyev, Kosuke MorikawaAbstract:The crystal structure of Vitelline Membrane outer layer protein I (VMO-I), which is isolated from the Vitelline Membrane outer layer of hen's eggs, has been determined by the multiple isomorphous replacement method and refined to an R-factor of 18.8% at 2.2 A resolution. The main chain folds into an unusual structure that consists of three beta-sheets forming Greek key motifs, which are related by an internal pseudo three-fold symmetry. The internal portion surrounded by these three beta-sheets is filled with hydrophobic side chains. This conformational feature coincides with three internal repeats in the sequence. Although a similar fold exists in the second domain of delta-endotoxin, there are significant structural differences between the two proteins, with the three-fold symmetry being most regular in VMO-I.
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crystallization and preliminary crystallographic data of Vitelline Membrane outer layer protein i vmo i
Journal of Molecular Biology, 1994Co-Authors: Toshiyuki Shimizu, S Kido, Kosuke Morikawa, Y DoiAbstract:The Vitelline Membrane outer layer protein I (VMO-I), which is isolated from the Vitelline Membrane outer layer of hen's eggs, has been crystallized from an acetate buffer solution by the hanging-drop method. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell dimensions a = 62.42 A, b = 110.52 A, c = 44.15 A. There are two molecules (M(r) = 18,000) per asymmetric unit. The crystals diffract to at least 2.2 A Bragg spacings.
S Kido - One of the best experts on this subject based on the ideXlab platform.
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characterization of progressive changes in zpc of the Vitelline Membrane of quail oocyte following oviductal transport
Molecular Reproduction and Development, 2000Co-Authors: S Kido, Y Doi, Jianzhi Pan, Tomohiro Sasanami, Shizuka Nakajima, Makoto MoriAbstract:The inner layer of the Vitelline Membrane of avian oocyte is equivalent to the zona pellucida of mammalian oocytes or to the Vitelline envelope of amphibian oocytes. One of the two major glycoproteins in the inner layer of quail Vitelline Membrane, formerly called 33-kDa glycoprotein, is homologous to mammalian ZPC, one of the components of zona pellucida. Quail ZPC is found to have different mobilities on SDS-polyacrylamide gel electrophoresis depending on whether it is obtained from the preovulatory follicle or from the laid eggs. In order to characterize the progressive changes in the molecular size of quail ZPC during the oviductal transport, the inner layer isolated from the follicle was incubated in vivo in various regions of the oviduct and subjected to Western blot analysis with anti-quail ZPC antiserum. The quail ZPC of the inner layer incubated in infundibulum reduced its apparent molecular weight, exhibiting the same electrophoretic mobility as that of laid eggs. The similar reduction in molecular weight was observed after the in vitro incubation of the inner layer with the extracts of infundibulum. From the comparison of the N-terminal amino acid sequences, it was found that the first 26 residues of the quail ZPC in follicular oocytes are missing from the ZPC of laid eggs. In addition, lectin blot analysis suggested the modification of oligosaccharide chains during the oviductal transport. These results represent the first description in the avian oviduct of the presence of protease, which is similar to oviductin, a trypsin-like protease involved in the hydrolysis of a major component of the Vitelline envelope of amphibian oocytes. Mol. Reprod. Dev. 55:175–181, 2000. © 2000 Wiley-Liss, Inc.
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characterization of Vitelline Membrane outer layer protein i vmo i amino acid sequence and structural stability
Journal of Biochemistry, 1995Co-Authors: S Kido, Fimi Kim, Y Doi, Emi Morishita, Hiroshi Narita, Shigenori Kanaya, Tadayashu Ohkubo, Ken Nishikawa, Toru Yao, Tatsuo OoiAbstract:Vitelline Membrane outer layer protein I (VMO-I) tightly bound to ovomucin fibrils of hen's egg yolk Membrane was characterized in terms of its amino acid sequence and structural stability. The deduced sequence of VMO-I using the conventional sequencing method is: RTREYTSVITVPNGGHWGKWGIRQFCHSGYANGFALKVEPSQFGRDDTALNGIRLRCLD- GSVIESLVGKWGTWTSFLVCPTGYLVSFSLRSEKSQGGGDDTAANNIQFRCSDEAVLVGD- DLSWGRFGPWSKRCKICGLQTKVESPQGLRDDTALNNVRFFCCK. Thus, VMO-I is composed of 163 amino acid residues with a calculated molecular weight of 17,979. The sequence confirms the cDNA sequence of VMO-I we recently determined and does not show any significant similarity to proteins compiled in the NBRF database. Two of the four disulfide bonds found in VMO-I were estimated to lie between Cys26 and Cys57 and between Cys79 and Cys110. The sequence analyses show that VMO-I contains three 53-residue internal repeats that contain distinctive regions of turns flanked by beta-sheets consistent with the recent finding that the molecule contains a new beta-fold motif, the beta-prism. The molecular characteristics of VMO-I in solution were examined by CD spectroscopy in the far and near ultraviolet regions, NMR spectroscopy, and high sensitive differential scanning calorimetry (DSC). CD spectra in the far UV region at room temperature were similar to that assigned to a random coil, while in the near UV region, small positive peaks were observed. The ellipticity in both regions decreased on raising the temperature. Proton NMR experiments showed the native structure unfolds to unordered conformations at 70 degrees C.(ABSTRACT TRUNCATED AT 250 WORDS)
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cloning and sequencing of hen magnum cdnas encoding Vitelline Membrane outer layer protein i vmo i
Gene, 1994Co-Authors: Atsuko Uyeda, S Kido, Y Doi, Chikako Inuzuka, Masakazu KikuchiAbstract:Abstract Two cDNAs encoding hen Vitelline Membrane outer layer protein I (VMO-I), which is classified as a new type of multi-β-sheet assembly, were cloned and sequenced. Northern blot analysis using vmo-I cDNA as a probe showed the presence of three mRNA species. Strikingly, expression of these mRNAs was restricted to a specific region of the hen oviduct, the area joining the infundibulum to the magnum.
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crystal structure of Vitelline Membrane outer layer protein i vmo i a folding motif with homologous greek key structures related by an internal three fold symmetry
The EMBO Journal, 1994Co-Authors: Toshiyuki Shimizu, S Kido, Y Doi, D G Vassylyev, Kosuke MorikawaAbstract:The crystal structure of Vitelline Membrane outer layer protein I (VMO-I), which is isolated from the Vitelline Membrane outer layer of hen's eggs, has been determined by the multiple isomorphous replacement method and refined to an R-factor of 18.8% at 2.2 A resolution. The main chain folds into an unusual structure that consists of three beta-sheets forming Greek key motifs, which are related by an internal pseudo three-fold symmetry. The internal portion surrounded by these three beta-sheets is filled with hydrophobic side chains. This conformational feature coincides with three internal repeats in the sequence. Although a similar fold exists in the second domain of delta-endotoxin, there are significant structural differences between the two proteins, with the three-fold symmetry being most regular in VMO-I.
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crystallization and preliminary crystallographic data of Vitelline Membrane outer layer protein i vmo i
Journal of Molecular Biology, 1994Co-Authors: Toshiyuki Shimizu, S Kido, Kosuke Morikawa, Y DoiAbstract:The Vitelline Membrane outer layer protein I (VMO-I), which is isolated from the Vitelline Membrane outer layer of hen's eggs, has been crystallized from an acetate buffer solution by the hanging-drop method. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell dimensions a = 62.42 A, b = 110.52 A, c = 44.15 A. There are two molecules (M(r) = 18,000) per asymmetric unit. The crystals diffract to at least 2.2 A Bragg spacings.
Giuseppe Gargiulo - One of the best experts on this subject based on the ideXlab platform.
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control of Vitelline Membrane gene expression during d melanogaster oogenesis
2008Co-Authors: Giuseppe GargiuloAbstract:The formation of extracellular structures is a complex process that requires time-coordinate synthesis, cleavage and transport of various proteins, and finally, cross-linking mediated by particular functional domains. Exactly how the precise features of such biological structures are constructed remains a fascinating problem. We approach this question by studying the eggshell assembly in Drosophila melanogaster. Although much is known about the induction and refinement of the signaling pathways involved in the formation of the anterior eggshell structures, little is known about the regulation and the function of the genes encoding eggshell structural proteins. This review will summarize the knowledge on Vitelline Membrane gene expression, focusing on our results on the expression pattern and the regulatory elements controlling transcription of a member of this gene family, the VM32E gene. Compared with the other Vitelline Membrane genes, this gene shows a peculiar expression pattern that suggests interesting perspectives of VM32E protein function in eggshell assembly.
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Drosophila Vitelline Membrane cross-linking requires the fs(1)Nasrat, fs(1)polehole and chorion genes activities
Development Genes and Evolution, 2001Co-Authors: Filippo M. Cernilogar, Francesco Fabbri, Davide Andrenacci, Carlo Taddei, Giuseppe GargiuloAbstract:During the final step of Drosophila Vitelline Membrane formation, the structural proteins composing this layer become cross-linked by covalent bonds. In the present report, we analyzed the Vitelline Membrane cross-linking in mutants having defects either in this layer or in the chorionic layers. In the fs(1)Nasrat and fs(1)polehole mutant alleles conferring defects in Vitelline Membrane formation, disruption of Vitelline Membrane cross-linking was observed, indicating the involvement of these two genes in the process. On the contrary, in the fs(1)Nasrat and fs(1)polehole alleles showing defects only at the termini of the embryo the Vitelline Membrane is properly formed, confirming a multifunctional activity of their gene products. Altered Vitelline Membrane cross-linking was also detected in a mutant of the chorion protein gene Cp36 and in the chorion amplification mutant fs(1)K1214 , suggesting a role of the structural components of chorion layers in the process of Vitelline Membrane hardening.
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regulatory elements in the promoter of the Vitelline Membrane gene vm32e of drosophila melanogaster direct gene expression in distinct domains of the follicular epithelium
Molecular Genetics and Genomics, 1997Co-Authors: Valeria Cavaliere, Davide Andrenacci, Stefania Spano, L Cortesi, Giuseppe GargiuloAbstract:The Drosophila Vitelline Membrane protein gene VM32E is expressed according to a precise temporal and spatial program in the follicle cells. Results from germ line transformation experiments using different fragments of the −465/−39 VM32E region fused to the hsp/lacZ reporter gene revealed that the region −348/−39 is sufficient to confer the wild-type expression pattern. Within this segment, distinct cis-regulatory elements control VM32E expression in ventral and dorsal follicle cells. The region between −135/−113 is essential for expression of the VM32E gene in the ventral columnar follicle cells. Expression in the dorsal domain requires the two regions −348/−254 and −118/−39. Furthermore, the region −253/−119 appears to contain a negative element that represses gene activity in anterior centripetal cells. We suggest that the expression of the VM32E gene throughout the follicular epithelium is controlled by specific cis-regulatory elements acting in distinct spatial domains and following a precise developmental program.
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cellular specificity of expression and regulation of drosophila Vitelline Membrane protein 32e gene in the follicular epithelium identification of cis acting elements
Mechanisms of Development, 1991Co-Authors: Giuseppe Gargiulo, Carla Malva, Silvia Gigliotti, Franco GrazianiAbstract:Abstract In this paper we analyze the expression in follicular cells and regulation of the Vitelline Membrane protein gene we identified in region 32E of the second chromosome of D. melanogaster (VMP32E). We report germ line transformation results obtained with different kinds of gene fusion leading to the identification of a follicular cell subpopulation involved in the expression of the VMP32E. We have characterized two 5′ non-transcribed regions (-465/-249;-135/-39) where the cis -acting transcriptional regulatory sequences, directing tissue and temporal specificity, are contained. The region between -465 and -249, which appears to control transcriptional high efficiency, does not behave as an enhancer as it is incapable of conferring any expression to a reporter gene. The region between -135 and -39 can confer temporal specificity of expression of the VMP32E gene, albeit at a very low level. Most interestingly, sequence similarities to ecdysone response elements raise the possibility of hormonal control also for VMP gene expression.
Toshiyuki Shimizu - One of the best experts on this subject based on the ideXlab platform.
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crystal structure of vmo i Vitelline Membrane outer layer protein i isolated from the Vitelline Membrane of hen s eggs
Nihon Kessho Gakkaishi, 1996Co-Authors: Toshiyuki ShimizuAbstract:The crystal structure of Vitelline Membrane outer layer protein I (VMO-I), which was isolated from the outer layer of the Vitelline Membrane of hen's eggs, has been determined by X-ray analysis. VMO-I is composed of three homologous structures, each containing a β-sheet forming Greek key motif, which are in accordance with the three repeats in the sequence. These three homologous structures are related by a pseudo three-fold symmetry. This new folding motif, recently designated as the β-prism, has also been observed in the second domain of δ-endotoxin. Thus, VMO-I and δ-endotoxin constitute a new family with a novel folding motif. The VMO-I molecule has a groove-like cavity. This region contains invariant acidic residues in the three repeats. VMO-I is assumed to be an oligosaccharide binding protein like lysozyme, although details of its catalytic function remain to be solved. A docking model of an oligosaccharide to VMO-I has been constructed. This model shows that the cavity has a sufficient space to bind roughly pentamer saccharides. The structural features strongly suggest that the negatively-charged cavity in the top region of the protein may be involved in an unknown catalytic reaction.
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crystal structure of Vitelline Membrane outer layer protein i vmo i a folding motif with homologous greek key structures related by an internal three fold symmetry
The EMBO Journal, 1994Co-Authors: Toshiyuki Shimizu, S Kido, Y Doi, D G Vassylyev, Kosuke MorikawaAbstract:The crystal structure of Vitelline Membrane outer layer protein I (VMO-I), which is isolated from the Vitelline Membrane outer layer of hen's eggs, has been determined by the multiple isomorphous replacement method and refined to an R-factor of 18.8% at 2.2 A resolution. The main chain folds into an unusual structure that consists of three beta-sheets forming Greek key motifs, which are related by an internal pseudo three-fold symmetry. The internal portion surrounded by these three beta-sheets is filled with hydrophobic side chains. This conformational feature coincides with three internal repeats in the sequence. Although a similar fold exists in the second domain of delta-endotoxin, there are significant structural differences between the two proteins, with the three-fold symmetry being most regular in VMO-I.
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crystallization and preliminary crystallographic data of Vitelline Membrane outer layer protein i vmo i
Journal of Molecular Biology, 1994Co-Authors: Toshiyuki Shimizu, S Kido, Kosuke Morikawa, Y DoiAbstract:The Vitelline Membrane outer layer protein I (VMO-I), which is isolated from the Vitelline Membrane outer layer of hen's eggs, has been crystallized from an acetate buffer solution by the hanging-drop method. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell dimensions a = 62.42 A, b = 110.52 A, c = 44.15 A. There are two molecules (M(r) = 18,000) per asymmetric unit. The crystals diffract to at least 2.2 A Bragg spacings.
Yaqi Meng - One of the best experts on this subject based on the ideXlab platform.
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Comparative N-Glycoproteomic Analysis Provides Novel Insights into the Deterioration Mechanisms in Chicken Egg Vitelline Membrane during High-Temperature Storage.
Journal of agricultural and food chemistry, 2021Co-Authors: Yu Zhou, Ning Qiu, Yoshinori Mine, Russell Keast, Yaqi MengAbstract:The weakening of chicken egg Vitelline Membrane (CEVM) is one of the most important factors influencing egg quality during high-temperature storage. Therefore, a comparative N-glycoproteomic analysis of CEVM after 10 days of storage at 30 °C was performed to explore the roles of protein N-glycosylation in Membrane deterioration. In total, 399 N-glycosites corresponding to 198 proteins were identified, of which 46 N-glycosites from 30 proteins were significantly altered. Gene ontology analysis revealed that these differentially N-glycosylated proteins (DGPs) were involved in antibacterial activity, glycosaminoglycan binding, lipid binding, and aminopeptidase activity. Removal of the N-glycans in Mucin-5B may result in a loss of CEVM's mechanical properties. The N-glycosites enriched in the apolipoprotein B β2 domain in CEVM were significantly changed, which may contribute to lipid composition modifications during storage. Moreover, N-glycosites in several metalloproteases were located within the functional domain or active site region, indicating that the decreased N-glycosylation levels may affect their structural stability, specific substrate binding, or enzyme activity. These findings provide novel insights into the roles of protein N-glycosylation during Membrane weakening.
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quantitative comparative proteomic analysis of chicken egg Vitelline Membrane proteins during high temperature storage
Journal of Agricultural and Food Chemistry, 2020Co-Authors: Yu Zhou, Ning Qiu, Yoshinori Mine, Russell Keast, Yaqi Meng, Chunxia ZhuAbstract:To explore the thermally induced alterations in chicken egg Vitelline Membrane (CEVM) protein abundances, a comparative proteomic analysis of CEVM after 10 days of storage at 30 °C was performed. Altogether, 981 proteins were identified, of which 124 protein abundances were decreased and 79 were increased. Bioinformatic analysis suggested that the altered proteins were related to structure (n = 10), mechanical properties (n = 13), chaperone (n = 15), antibacterial (n = 12), and antioxidant (n = 3). Alterations in abundances of structural proteins, possibly resulting from the disintegration of these complexes, were observed in this study, suggesting a loss in fibrous structure. Several proteins involved in mechanical strength (n = 10), elasticity (n = 3), and chaperone were decreased in abundances, which indicated that deficits in these proteins might affect the CEVM mechanical properties. These findings will extend our understanding of CEVM deterioration during high-temperature storage from a proteomic perspective.
