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Advances in Bioscience and Biotechnology 2018年第1期9卷 52-62页

作者： Kakeru Fujimori Hideto Fukushima masahiro matsumiya Department of Marine Science and Resources College of Bioresource Sciences Nihon University Fujisawa Japan

Chitin deacetylase (CDA;EC 3. 5. 1. 41) catalyzes the deacetylation of chitin. In this study, we successfully cloned and sequenced a chitin deacetylase gene from the red snow crab Chionoecetes japonicas. By using reverse transcription-polymerase chain reaction (RT-PCR) and 5' and 3' rapid amplification of cDNA ends, we obtained a 2141-bp amplicon containing a chitin deacetylase gene (CjCDA) from the epidermis of C. japonicas. The amplicon contains a 1575-bp open reading frame that is predicted to encode a 525-amino acid protein. The structure predicted from the deduced amino acid sequence included an N-terminal signal peptide, chitin-binding domain (CBD), low-density lipoprotein receptor class A domain (LDL-A), and catalytic domain. Comparative analysis of the deduced amino acid sequence of CjCDA revealed the highest homology (74%) to gastrolith protein 59 of Cherax quadricarinatus. We used RT-PCR to evaluate the expression of CjCDA in various tissues of C. japonicas, and we observed that CjCDA was expressed only in the epidermis. A phylogenetic analysis, using the amino acid sequences of CjCDA and other known chitin deacetylases, showed that CjCDA belonged to a group of crustacean chitin deacetylases. To our knowledge, this is the first study reporting the cDNA cloning of a chitin deacetylase from a crab.

关键词： Chitin Deacetylase Molecular Cloning Chionoecetes japonicas Phylogenetic Analysis Expression Analysis

Distribution of Chitinolytic Enzymes in the Organs and cDNA Cloning of Chitinase Isozymes from the Stomach of Two Species of Fish, Chub Mackerel (Scomber japonicus) and Silver Croaker (Pennahia argentata)

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Open Journal of Marine Science 2015年第4期5卷 398-411页

作者： Hiromi Kakizaki Mana Ikeda Hideto Fukushima masahiro matsumiya College of Bioresource Sciences Nihon University Fujisawa Japan

Chitinolytic activities were measured in two fish species having different feeding habits, chub mackerel (Scomber japonicus) and silver croaker (Pennahia argentata). Chitinase (an endo-type chitinolytic enzyme) activity was measured using pNP-(GlcNAc)n (n = 2, 3) as substrates;its level was significantly high in the stomachs of both species, as well as in the gills, intestine, pyloric appendage, testis, and liver of chub mackerel and in the spleen, kidney, pyloric appendage, ovaries, heart, and liver of silver croaker. β-N-Acetylhexosaminidase (an exo-type chitinolytic enzyme) activity was measured using pNP-(GlcNAc) as a substrate;it was detected at high levels in many parts apart from the digestive tracts of both species. The optimum pH for chitinase activity was 3.0 - 5.0 in the stomachs of both species, 4.0 in the liver of chub mackerel, and 4.0 and 8.0 in the kidney of silver croaker. Full-length cDNAs encoding two chitinase isozymes were obtained from the stomachs of the two fish species: SjChi-1 (1604 bp) and SjChi-2 (1512 bp) from chub mackerel and PaChi-1 (1630 bp) and PaChi-2 (1606 bp) from silver croaker. Expression analysis of these genes in the organs of the two species revealed strong expression of SjChi-1 in the stomach of chub mackerel and that of PaChi-1 andPaChi-2 in the stomach of silver croaker. The difference in the expression pattern of these genes is likely attributed to the difference in the feeding habits of the two fish species. Our results suggested the presence of novel chitinases in the two species.

关键词： Chitinolytic Enzyme Chitinase β-N-Acetylhexosaminidase Distribution Phylogenetic Tree Analysis

Distribution of Chitinolytic Enzymes in the Organs and cDNA Cloning of Chitinase Isozymes from the Liver of Golden Cuttlefish Sepia esculenta

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Advances in Bioscience and Biotechnology 2017年第10期8卷 361-377页

作者： Ryo Nishino Hiromi Kakizaki Hideto Fukushima masahiro matsumiya Department of Marine Science and Resources College of Bioresource Sciences Nihon University Fujisawa Kanagawa Japan

The distribution of chitinolytic enzymes in eight organs of the golden cuttlefish Sepia esculenta was determined. Chitinase activity (activity of endo-type chitinolytic enzyme) was measured using pNP-(GlcNAc)n (n = 2, 3) as substrates, with high activity detected in the liver, posterior salivary gland, and stomach. β-N-acetylhexosaminidase (Hex) activity (activity of exo-type chitinolytic enzyme) was determined using pNP-(GlcNAc) as a substrate, and high activity was observed in six organs, including the liver, branchial heart, posterior salivary gland, and stomach. In addition, two chitin-binding proteins (CBP-A, CBP-B) were isolated from the liver using a chitin affinity column. Two full-length cDNAs (SeChi-1: 1484 bp;SeChi-2: 1748 bp) encoding chitinases were obtained from the liver of S. esculenta. SeChi-1 contained a 1377-bp open reading frame (ORF) encoding 459 amino acids, and SeChi-2 contained a 1656-bp ORF encoding 552 amino acids. Domain structures predicted from the deduced amino acid sequences of SeChi-1 and SeChi-2 (SeChi-1, SeChi-2) contained signal peptides, a GH Family 18 catalytic domain, one chitin binding domain (CBD) in SeChi-1, and two CBDs in SeChi-2. Proteome analysis revealed that 125 peptide residues of CBP-A were present in SeChi-1, and 116 peptide residues of CBP-B were present in SeChi-2. Organ expression analysis revealed that SeChi-1 and SeChi-2 were expressed only in the liver of S. esculenta. Phylogenetic analysis of SeChi-1, SeChi-2, and GH family 18 chitinases revealed that SeChi-2 belongs to a group of previously reported squid chitinases, while SeChi-1 does not belong to any previously reported group of mollusk chitinases.

关键词： Chitinolytic Enzyme Chitinase Distribution cDNA Cloning Golden Cuttlefish Sepia esculenta

Molecular Cloning of a Chitinase Gene from the Ovotestis of Kuroda’s Sea Hare Aplysia kurodai

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Advances in Bioscience and Biotechnology 2016年第1期7卷 38-46页

作者： Gaku Matsunaga Syuuji Karasuda Ryo Nishino Hideto Fukushima masahiro matsumiya Department of Marine Science and Resources College of Bioresource Sciences Nihon University Kanagawa Japan

In this study, we report that we successfully cloned and sequenced a chitinase gene from the ovotestis of Kuroda’s sea hare Aplysia kurodai. By using reverse transcription-polymerase chain reaction (RT-PCR) and a system for the 5’ and 3’ rapid amplification of cDNA ends, we obtained a 1352 bp chitinase gene (AkChi) from the ovotestis of A. kurodai. AkChi contains a 1263 bp open reading frame that encodes 421 amino acids. The domain structure predicted from the deduced amino acid sequence was an N-terminal signal peptide and a catalytic domain of glycoside hydrolase (GH) family 18 chitinase. A comparative analysis of the deduced amino acid sequences of AkChi with those of the acidic mammalian chitinase of the California sea hare Aplysia californica revealed the highest homology at 83%. The purified chitinase from the ovotestis was digested by trypsin, and 119 residues of digested peptides were consistent with the deduced amino acid sequence of AkChi. We used RT-PCR to evaluate the expression of AkChi in various tissues of A. kurodai, and we observed that AkChi was expressed only in the ovotestis. A phylogenetic tree analysis, performed using the amino acid sequences of AkChi and known GH family 18 chitinases, showed that AkChi was separated from the molluscan chitinases with a chitin binding domain. To our knowledge, this is the first study demonstrating the cDNA cloning of an ovotestis chitinase from a sea hare.

关键词： Chitinase Molecular Cloning Kuroda’s Sea Hare Aplysia kurodai Mollusc Ovotestis Phylogenetic Tree Analysis

cDNA Cloning of Paramyosin from Several Kinds of Squid Mantle Muscle

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Advances in Bioscience and Biotechnology 2018年第1期9卷 11-25页

作者： Takayuki Kajita Yoshiko Takeda Saki Yoshida Koki Yamada masahiro matsumiya Hideto Fukushima Department of Marine Science and Resources College of Bioresource Science Fujisawa Japan

Paramyosin is a rod-shaped muscle protein found exclusively in invertebrates, with α-helices coiled around each other to form a coiled-coil structure. Marine organisms in which the primary structure of paramyosin has been determined are mollusks, including abalone (Haliotis discus), mussels (Mytilus galloprovincialis), octopus (Octopus bimaculoides), and oyster (Crassostrea gigas). In contrast, the primary structure of squid paramyosin, which is of particular interest, has yet to be reported. In the present study, cDNA cloning of paramyosins from four squid species, the neon flying squid (Ommastrephes bartramii), the Humboldt squid (Dosidicus gigas), the golden cuttlefish (Sepia esculenta), and the clawed armhook squid (Gonatus onyx), was performed to determine the following: the 2605-bp O. bartramii paramyosin gene containing a 2574-bp open reading frame (ORF), the 2691-bp D. gigas paramyosin gene containing a 2640-bp ORF, the 2631-bp S. esculenta paramyosin gene containing a 2574 ORF, and the 2609-bp G. onyx paramyosin gene containing a 2574-bp ORF. The primary structure of the four squid paramyosins was found to contain heptad repeats and an ACD (assembly competence domain), which are characteristic of a coiled coil. A phylogenetic analysis was performed with paramyosin sequences from species including the four squid species examined in this study, the results of which indicated that the four squid paramyosins form a group independent from the paramyosins of other species, to which octopus paramyosins are closest.

关键词： Paramyosin Squid cDNA Cloning Mantle Muscle Phylogenetic Analysis

Distribution of Chitinolytic Enzyme in the Organs and Molecular Cloning of a Novel Chitinase Gene from the Kidney of Marbled Rockfish Sebastiscus marmoratus

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Advances in Bioscience and Biotechnology 2018年第1期9卷 36-51页

作者： Miku Watanabe Hiromi Kakizaki Taro Tsukamoto Miku Fujiwara Hideto Fukushima Mitsuhiro Ueda masahiro matsumiya Department of Marine Science and Resources College of Bioresource Sciences Nihon University Kanagawa Japan Department of Applied Biological Chemistry College of Agriculture Osaka Prefecture University Osaka Japan

Actinopterygii express two types of chitinase (acidic fish chitinase-1 (AFCase-1) and acidic fish chitinase-2 (AFCase-2)) that are active at acidic pHs and involved in digestion in the stomach. We proposed the existence of a new fish chitinase that has a non-digestive function. In this study, we used Sebastiscus marmoratus, for which characteristics and cDNA cloning of chitinase isozymes (SmChi-1, SmChi-2) in the stomach have been reported. Initially, we examined the distribution of chitinase and β-N-acetylhexosaminidase (Hex) in the body and then we tried to clone novel chitinase cDNA from the kidney. Chitinase and Hex activities were measured using pNP-(GlcNAc)n, (n = 2, 3) and pNP-GlcNAc as substrates, respectively. Total RNA was extracted from the kidney. RT-PCR was performed to obtain chitinase cDNA fragments using reverse transcriptase with an oligo dT primer. The RACE method was used to obtain sequences of the upstream and downstream regions of cDNA. The full-length chitinase cDNA was determined using PrimeSTAR®?Max DNA polymerase with proofreading activity. High chitinase activity was observed in the stomach, as previously reported. In addition, relatively high activity was observed in the liver, spleen, kidney, and heart. In contrast, Hex activity was detected in all organs. This result is consistent with the report that Hex is related to body-wide metabolism. Full-length cDNA (SmChi-3) of the novel chitinase was obtained from the kidney, which contained 1440 bp open reading frames. The domain structure of SmChi-3 was assumed to be similar to those of SmChi-1 and SmChi-2. SmChi-1 and SmChi-2 have a serine and glycine-rich linker region, which is characteristic of AMCase. In contrast, SmChi-3 contained no apparent sequence in the linker region. Phylogenetic analysis revealed the existence of a new chitinase group, which was named fish chitinase-3 (FCase-3) and differed from AFCase-1 and AFCase-2.

关键词： Chitinolytic Enzyme Chitinase Sebastiscus marmoratus Distribution cDNA Cloning

Chondrichthyes Chitinase: Molecular Cloning, Distribution, and Phylogenetic Analysis

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Open Journal of Marine Science 2018年第1期8卷 136-151页

作者： Miku Watanabe Hiromi Kakizaki Momo Kanai Satoshi Kawashima Kaneyuki Hamaguchi Hiroki Mizuno Tsubasa Ueno Chiaki Yasukawa Ryuji Agata Mana Ikeda Hideto Fukushima Mitsuhiro Ueda masahiro matsumiya College of Bioresource Sciences Nihon University Fujisawa Japan Laboratory of Biocycle Engineering Department of Applied Biological Chemistry Osaka Prefecture University Sakai Japan

We have previously reported the presence of three types of chitinase (acidic fish chitinase-1: AFCase-1, acidic fish chitinase-2: AFCase-2, fish chitinase-3: FCase-3) in Actinopterygii. In the present research, we report the identification of the novel chitinase genes HjChi (ORF: 1380 bp) and DkChi (ORF: 1440 bp) from the stomach of Chondrichthyes, Japanese bullhead shark (Heterodontus japonicas) and Kwangtung skate (Dipturus kwangtungensis), respectively. Organ-specific expression analysis identified the stomach-specific expression of HjChi, whereas DkChi was expressed widely in all organs. Chitinase activity was measured using pNP-(GlcNAc)n (n = 2, 3) as a substrate and β-N-acetylhexosaminidase (Hex) activity was measured using pNPGlcNAc. Relatively high values of chitinase activity were observed in the stomach, spleen, and gonads of the Japanese bullhead shark, H. japonicas , compared with that observed in the stomach of the Kwangtung skate D. kwangtungensis . However, Hex activity was detected throughout the body of both species. The optimal pH of chitinase in both the Japanese bullhead shark, H. japonicas, and the Kwangtung skate, D. kwangtungensis, were 3.5 - 5.5 and 3.5 - 4.0, respectively, and 4.0 for Hex in both species. Phylogenetic analysis revealed that Chondrichthyes chitinase forms a unique group (Chondrichthyes chitinase). These results suggested that the possibility of the formation of chitinase groups for each class in the phylogenetic analysis based on the observation of class-specific chitinase.

关键词： Chitinase Distribution Chondrichthyes cDNA Cloning Phylogenetic Analysis

Laser ion source for heavy ion inertial fusion

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Matter and Radiation at Extremes 2018年第2期3卷 61-66页

作者： masahiro Okamura Collider-Accelerator Department Brookhaven National LaboratoryBuilding 930UptonNY 11973USA

The proposed heavy ion inertial fusion(HIF)scenarios require ampere class low charge state ion beams of heavy *** laser ion source(LIS)is recognized as one of the promising candidates of ion beam providers,since it can deliver high brightness heavy ion beams to *** design of LIS for the HIF depends on the accelerator structure and accelerator complex following the *** this article,we discuss the specifications and design of an appropriate LIS assuming two major types of the accelerators:radio frequency(RF)high quality factor cavity type and non-resonant induction core *** believe that a properly designed LIS would satisfy the requirements of both types,while some issues need to be verified experimentally.

关键词： Inertial fusion Accelerator Ion source Laser ablation Heavy ion source

On a Relation between the Universal Teichmu¨ller Space and the Grunsky Operator

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Acta Mathematica Sinica,English Series 2014年第4期30卷 591-600页

作者： masahiro YANAGISHITA Departments in Fundamental Science and Engineering Waseda University

Being a Strebel point gives a sufficient condition for that the extremal Beltrami coefficient is uniquely determined in a Teichmiiller equivalence class. We consider how Strebel points are characterized. In this paper, we will give a new characterization of Strebel points in a certain subset of the universal Teichmfiller space by a property of the Grunsky operator.

关键词： Quasiconformal mappings Strebel points Grunsky inequalities

An Inverse Problem for Maxwell's Equations in Anisotropic Media

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Chinese Annals of Mathematics,Series B 2007年第1期28卷 35-54页

作者： masahiro YAMAMOTO Graduate School of Mathematical Sciences The University of Tokyo 3-8-1 Komaba Meguro Tokyo 153Japan

The authors consider Maxwell＇s equations for an isomagnetic anisotropic and inhomogeneous medium in two dimensions, and discuss an inverse problem of determining the permittivity tensor （ε1,ε2,ε2,ε3 ） and the permeability μ in the constitutive relations from a finite number of lateral boundary measurements. Applying a Carleman estimate, the authors prove an estimate of the Lipschitz type for stability, provided that ε1,ε2,ε3,μ satisfy some a priori conditions.

关键词： Anisotropic media Inverse problem Maxwell's equations Carleman estimate Lipschitz stability