Isolation and Characterization of Rhamnose-binding Lectins from Eggs of Steelhead Trout (Oncorhynchus mykiss) Homologous to Low Density Lipoprotein Receptor Superfamily

Tateno, Hiroaki; Saneyoshi, Ayako; Ogawa, Tomoya; Muramoto, Koji; Kamiya, Hisao; Saneyoshi, Mineo

doi:10.1074/jbc.273.30.19190

Cited by 115 publications

(74 citation statements)

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“…The peptide (200 M) was incubated with proteinases for 30 min at 37°C in PBS. Each digest was separated by reversed-phase HPLC on a Wakosil 5C4-200 column (5 mm, 4.6 ϫ 250 mm) (WAKO, Osaka, Japan) using a linear gradient from 0 to 30% acetonitrile in 0.1% trifluoroacetic acid, and the amino acid sequences of peptide fragments were analyzed by a gas phase protein sequencer (PSQ-1; Shimadzu, Kyoto, Japan) and a matrix-assisted laser desorption ionization time of flight mass spectrometry (Kompact MALDI I; Shimadzu), according to a previously described procedure (38).…”

Section: Analysis Of Peptide Cleavagementioning

confidence: 99%

Activation of Human Oral Epithelial Cells by Neutrophil Proteinase 3 Through Protease-Activated Receptor-2

Uehara¹,

Sugawara²,

Muramoto

et al. 2002

The Journal of Immunology

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Proteinase 3 (PR3), a 29-kDa serine proteinase secreted from activated neutrophils, also exists in a membrane-bound form, and is suggested to actively contribute to inflammatory processes. The present study focused on the mechanism by which PR3 activates human oral epithelial cells. PR3 activated the epithelial cells in culture to produce IL-8 and monocyte chemoattractant protein-1 and to express ICAM-1 in a dose- and time-dependent manner. Incubation of the epithelial cells for 24 h with PR3 resulted in a significant increase in the adhesion to neutrophils, which was reduced to baseline levels in the presence of anti-ICAM-1 mAb. Activation of the epithelial cells by PR3 was inhibited by serine proteinase inhibitors and serum. The epithelial cells strongly express protease-activated receptor (PAR)-1 and PAR-2 mRNA and weakly express PAR-3 mRNA. The expression of PAR-2 on the cell surface was promoted by PR3, and inhibited by cytochalasin B, but not by cycloheximide. PR3 cleaved the peptide corresponding to the N terminus of PAR-2 with exposure of its tethered ligand. Treatment with trypsin, an agonist for PAR-2, and a synthetic PAR-2 agonist peptide induced intracellular Ca2+ mobilization, and rendered cells refractory to subsequent stimulation with PR3 and vice versa. The production of cytokine induced by PR3 and the PAR-2 agonist peptide was completely abolished by a phospholipase C inhibitor. These findings suggest that neutrophil PR3 activates oral epithelial cells through G protein-coupled PAR-2 and actively participates in the process of inflammation such as periodontitis.

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Section: Analysis Of Peptide Cleavagementioning

confidence: 99%

Activation of Human Oral Epithelial Cells by Neutrophil Proteinase 3 Through Protease-Activated Receptor-2

Uehara¹,

Sugawara²,

Muramoto

et al. 2002

The Journal of Immunology

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“…It is possible that a rhamnose-specific lectin could be involved in clavosine binding and uptake by a particular cell type or in an intracellular targeting mechanism. Rhamnose-specific lectins have been predominantly identified in fish eggs (35)(36)(37). Perhaps the clavosines discourage predation of marine sponges and/or associated microorganism(s) that produce the compounds; species of fish with rhamnose-specific lectins could be harmed if the clavosines were ingested.…”

Section: Examination Of Existing Calyculin a Binding Models-a Recent mentioning

confidence: 99%

Inhibition of Protein Phosphatase-1 by Clavosines A and B

McCready¹,

Islam²,

Schmitz³

et al. 2000

Journal of Biological Chemistry

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Site-directed mutagenesis was used to investigate the mechanism of interaction between the catalytic subunit of human protein phosphatase-1 (PP-1c␥) and members of the calyculin family of toxins. Clavosines A and B are related to calyculins but are glycosylated with a trimethoxy rhamnose group. We provide experimental evidence implicating Tyr-134 as an important residue in PP-1c␥ that mediates interactions with the calyculins. Mutation of Tyr-134 to Phe, to prevent hydrogen bond formation, resulted in a slight increase in sensitivity of PP-1c␥ to clavosines A and B and calyculin A. In contrast, a Y134A mutant was 10-fold less sensitive to inhibition by all three inhibitors. The greatest effect on inhibition was found by substituting an Asp for Tyr-134 in the phosphatase. Clavosine B inhibited PP-1c␥ Y134D with a 310-fold decrease in potency. Clavosine A and calyculin A were also markedly poorer inhibitors of this mutant. These results suggest that a hydrogen bond between Tyr-134 and the calyculins is unlikely to be essential for inhibitor binding to the phosphatase. Serine/threonine protein phosphatases are highly conserved enzymes, which have been isolated from numerous eukaryotic and prokaryotic organisms (1, 2). Eukaryotic protein phosphatases are inhibited by a structurally diverse array of natural product toxins. These include the polyether okadaic acid from marine dinoflagellates, cyclic peptide microcystins and nodularins from cyanobacteria, and the spiroketal calyculins isolated from marine sponges (3).The first member of the calyculin family of phosphatase inhibitors was identified in 1986 (4). Calyculin A was originally purified from a hydrophobic extract of the marine sponge Discodermia calyx. It was found to be cytotoxic toward P388 and L1210 leukemia cells and to be a strong inhibitor of starfish egg development (4, 5). It was subsequently characterized as a powerful inhibitor of the catalytic subunits of type 1 and 2A protein phosphatases, PP-1c 1 and PP-2Ac, two of the four major eukaryotic serine/threonine protein phosphatases (6). Calyculin A was also shown to have tumor-promoting activity as potent as that of okadaic acid (7). Many additional calyculins (8 -13), and the structurally related calyculinamides (11,14), have since been identified.Recently we reported the isolation of two novel glycosylated members of the calyculin family, clavosines A and B from the marine sponge Myriastra clavosa (15). Clavosines A and B are potent inhibitors of mammalian PP-1c and PP-2Ac and were found to be more cytotoxic overall than the calyculins and the calyculinamides (14, 15) in the National Cancer Institute (NCI) screening panel of tumor cell lines (16). The polyfunctional structure of clavosines A and B and calyculin A is depicted in linear diagrams (Fig. 1a) and space filling models (Fig. 1b). The clavosines (Fig. 1) have many structural features in common with the calyculins but differ markedly from them in having a methyl group at C-32 and an unusual trimethoxy rhamnose group at position C-21. Like the...

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“…35,38,[40][41][42] Three RBLs, named STL1, STL2, and STL3, were isolated from eggs of steelhead trout (Oncorhynchus mykiss) 41,42 and three RBLs, CSL1, CSL2, and CSL3, with a high degree of sequence identity with O. mykiss were isolated from chum salmon (Oncorhynchus keta) 43 (Table 18.1). Only one RBL (SAL) and two RBLs (WCL1 and WCL3) were isolated from catfish (Silurus asotus) and whitespotted charr (Salvelinus leucomaenis) eggs, respectively 44,45 (Table 18.1).…”

Section: Rbls In Fish: Biochemical and Molecular Featuresmentioning

confidence: 99%

Evolution and Immune Function of Fish Lectins

Cammarata¹,

Parisi²,

Vasta³

2016

Lessons in Immunity

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Any queries or remarks that have arisen during the processing of your manuscript are listed below and are highlighted by flags in the proof. (AU indicates author queries; ED indicates editor queries; and TS/TY indicates typesetter queries.) Please check your proof carefully and answer all AU queries. Mark all corrections and query answers at the appropriate place in the proof using on-screen annotation in the PDF file. For a written tutorial on how to annotate PDFs, click http://www.elsevier.com/__data/assets/ pdf_file/0007/98953/Annotating-PDFs-Adobe-Reader-9-X-or-XI.pdf. A video tutorial is also available at http://www.screencast. com/t/9OIDFhihgE9a. Alternatively, you may compile them in a separate list and tick off below to indicate that you have answered the query. Please return your input as instructed by the project manager. Location in articleQuery / remark AU1, page 244 Please provide the expansion for genus names "S. purpuratus" and "C. intestinalis" in the sentence "In contrast, the N…". ■ AU4, page 250 Please check the term "conCL-s" mentioned in the sentence "In the latter, conCL-s…". ■ AU5, page 243The citation 'Ogawa et al.,25 ' in the legend of To protect the rights of the author(s) and publisher we inform you that this PDF is an uncorrected proof for internal business use only by the author(s), editor(s), reviewer(s), Elsevier and typesetter TNQ Books and Journals Pvt Ltd. It is not allowed to publish this proof online or in print. This proof copy is the copyright property of the publisher and is confidential until formal publication. 10018-BALLARIN-9780128032527Chapter 18 Evolution and Immune Function of Fish LectinsMatteo Cammarata, Maria G. Parisi University of Palermo, Palermo, Italy Gerardo R. Vasta University of Maryland School of Medicine, Baltimore, MD, United States c0018 INTRODUCTIONThe term "lectin" is commonly used to encompass a wide variety of carbohydrate-binding proteins, widely distributed in viruses, prokaryotes, and eukaryotes. 1 The first invertebrate lectins were described in the early 1900s in the snail Helix pomatia, 2 the horseshoe crab Limulus polyphemus, 3 and the lobster Homarus americanus. 3 Among the vertebrates, Watkins and Morgan 4 first described an l-fucose-specific lectin in the European eel Anguilla anguilla, which led to the discovery of the carbohydrate nature of the H blood substance. Animal lectins are grouped in various molecular families, differing in carbohydrate recognition domain (CRD) structure and organization. 1,[5][6][7] Based on their CRD sequence motifs and cation requirements, animal lectins can be categorized in several families, such as C-type lectins (CTLs), galectins (formerly S-type lectins), rhamnose-binding lectins (RBLs), F-type lectins (FTLs), X-type lectins (XTLs), I-type lectins, P-type lectins, and pentraxins. 1,[5][6][7] Lectins are involved in a variety of key biological processes ranging from development to immune responses. 1,[7][8][9][10][11] The roles of lectin-carbohydrate interactions in self/non-self recognition in early dev...

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Isolation and Characterization of Rhamnose-binding Lectins from Eggs of Steelhead Trout (Oncorhynchus mykiss) Homologous to Low Density Lipoprotein Receptor Superfamily

Cited by 115 publications

References 50 publications

Activation of Human Oral Epithelial Cells by Neutrophil Proteinase 3 Through Protease-Activated Receptor-2

Activation of Human Oral Epithelial Cells by Neutrophil Proteinase 3 Through Protease-Activated Receptor-2

Inhibition of Protein Phosphatase-1 by Clavosines A and B

Evolution and Immune Function of Fish Lectins

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