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Book ; Online: Recent Advances in Thrombosis and Hemostasis 2008

Tanaka, Kenzo / Davie, Earl W. / Ikeda, Yasuo / Iwanaga, Sadaaki / Saito, Hidehiko / Sueishi, Katsuo

2008

Author's details	edited by Kenzo Tanaka, Earl W. Davie, Yasuo Ikeda, Sadaaki Iwanaga, Hidehiko Saito, Katsuo Sueishi
Keywords	Cytology ; Hematology ; Internal medicine ; Medicine
Language	English
Publisher	Springer Japan
Publishing place	Tokyo
Document type	Book ; Online
HBZ-ID	TT050387888
ISBN	978-4-431-78846-1 ; 978-4-431-78847-8 ; 4-431-78846-8 ; 4-431-78847-6
DOI	10.1007/978-4-431-78847-8
Database	ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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Article: Biochemical principle of Limulus test for detecting bacterial endotoxins.

Iwanaga, Sadaaki

Proceedings of the Japan Academy. Series B, Physical and biological sciences

2013 Volume 83, Issue 4, Page(s) 110–119

Abstract: A hemocyte lysate from horseshoe crab (Limulus) produced a gel, when exposed to Gram-negative bacterial endotoxins, lipopolysaccharides (LPS). This gelation reaction of the lysate, so-called Limulus test, has been widely employed as a simple and very ... ...

Abstract	A hemocyte lysate from horseshoe crab (Limulus) produced a gel, when exposed to Gram-negative bacterial endotoxins, lipopolysaccharides (LPS). This gelation reaction of the lysate, so-called Limulus test, has been widely employed as a simple and very sensitive assay method for endotoxins. Recent biochemical studies on the principle of Limulus test indicate that the hemocytes contain several serine protease zymogens, which constitute a coagulation cascade triggered by endotoxins, and that there is a (1,3)-β-D-glucan-mediated coagulation pathway which also results in the formation of gel. Up to now, six protein components, designated coagulogen, proclotting enzyme, factor B, factor C, and factor G, all of which are closely associated with the endotoxin-mediated coagulation pathway, have been purified and biochemically characterized. The molecular structures of these proteins have also been elucidated. Moreover, the reconstitution experiments using the isolated clotting factors, factor C, factor B, proclotting enzyme and coagulogen in the presence of endotoxin, leads to the formation of coagulin gel. Here, I will focus on the biochemical principle of Limulus test for detecting bacterial endotoxins, and its activation and regulation mechanism on the LPS-mediated coagulation cascade.
Language	English
Publishing date	2013-09-09
Publishing country	Japan
Document type	Journal Article ; Review
ZDB-ID	161781-3
ISSN	1349-2896 ; 0386-2208
ISSN (online)	1349-2896
ISSN	0386-2208
DOI	10.2183/pjab.83.110
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Article: The molecular basis of innate immunity in the horseshoe crab.

Iwanaga, Sadaaki

Current opinion in immunology

2002 Volume 14, Issue 1, Page(s) 87–95

Abstract: During the past two decades, the molecular structures and functions have been established for various defense molecules, using horseshoe crab (Limulus) as a model animal. These defense molecules include clotting factors, proteinase inhibitors, lectins, ... ...

Abstract	During the past two decades, the molecular structures and functions have been established for various defense molecules, using horseshoe crab (Limulus) as a model animal. These defense molecules include clotting factors, proteinase inhibitors, lectins, antimicrobial peptides and other humoral factors found mainly in the hemolymph. These components of the cellular and humoral systems, which together comprise innate immunity, defend horseshoe crab effectively from invading microbes.
MeSH term(s)	Animals ; Defensins/immunology ; Horseshoe Crabs/immunology ; Immunity, Innate ; Lectins/immunology
Chemical Substances	Defensins ; Lectins
Language	English
Publishing date	2002-01-28
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1035767-1
ISSN	1879-0372 ; 0952-7915
ISSN (online)	1879-0372
ISSN	0952-7915
DOI	10.1016/s0952-7915(01)00302-8
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Article: Snake venom metalloproteinases: structure, function and relevance to the mammalian ADAM/ADAMTS family proteins.

Takeda, Soichi / Takeya, Hiroyuki / Iwanaga, Sadaaki

Biochimica et biophysica acta

2012 Volume 1824, Issue 1, Page(s) 164–176

Abstract: Metalloproteinases are among the most abundant toxins in many Viperidae venoms. Snake venom metalloproteinases (SVMPs) are the primary factors responsible for hemorrhage and may also interfere with the hemostatic system, thus facilitating loss of blood ... ...

Abstract	Metalloproteinases are among the most abundant toxins in many Viperidae venoms. Snake venom metalloproteinases (SVMPs) are the primary factors responsible for hemorrhage and may also interfere with the hemostatic system, thus facilitating loss of blood from the vasculature of the prey. SVMPs are phylogenetically most closely related to mammalian ADAM (a disintegrin and metalloproteinase) and ADAMTS (ADAM with thrombospondin type-1 motif) family of proteins and, together with them, constitute the M12B clan of metalloendopeptidases. Large SVMPs, referred to as the P-III class of SVMPs, have a modular architecture with multiple non-catalytic domains. The P-III SVMPs are characterized by higher hemorrhagic and more diverse biological activities than the P-I class of SVMPs, which only have a catalytic domain. Recent crystallographic studies of P-III SVMPs and their mammalian counterparts shed new light on structure-function properties of this class of enzymes. The present review will highlight these structures, particularly the non-catalytic ancillary domains of P-III SVMPs and ADAMs that may target the enzymes to specific substrates. This article is part of a Special Issue entitled: Proteolysis 50years after the discovery of lysosome.
MeSH term(s)	ADAM Proteins/chemistry ; ADAM Proteins/genetics ; ADAM Proteins/metabolism ; ADAM Proteins/physiology ; Animals ; Humans ; Mammals/genetics ; Mammals/metabolism ; Metalloproteases/chemistry ; Metalloproteases/genetics ; Metalloproteases/metabolism ; Metalloproteases/physiology ; Models, Biological ; Models, Molecular ; Protein Conformation ; Protein Interaction Domains and Motifs/genetics ; Protein Interaction Domains and Motifs/physiology ; Snake Venoms/chemistry ; Snake Venoms/enzymology ; Snake Venoms/metabolism ; Structural Homology, Protein ; Structure-Activity Relationship
Chemical Substances	Snake Venoms ; Metalloproteases (EC 3.4.-) ; ADAM Proteins (EC 3.4.24.-)
Language	English
Publishing date	2012-01
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbapap.2011.04.009
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Article: Recent advances in the innate immunity of invertebrate animals.

Iwanaga, Sadaaki / Lee, Bok Luel

Journal of biochemistry and molecular biology

2005 Volume 38, Issue 2, Page(s) 128–150

Abstract: Invertebrate animals, which lack adaptive immune systems, have developed other systems of biological host defense, so called innate immunity, that respond to common antigens on the cell surfaces of potential pathogens. During the past two decades, the ... ...

Abstract	Invertebrate animals, which lack adaptive immune systems, have developed other systems of biological host defense, so called innate immunity, that respond to common antigens on the cell surfaces of potential pathogens. During the past two decades, the molecular structures and functions of various defense components that participated in innate immune systems have been established in Arthropoda, such as, insects, the horseshoe crab, freshwater crayfish, and the protochordata ascidian. These defense molecules include phenoloxidases, clotting factors, complement factors, lectins, protease inhibitors, antimicrobial peptides, Toll receptors, and other humoral factors found mainly in hemolymph plasma and hemocytes. These components, which together compose the innate immune system, defend invertebrate from invading bacterial, fungal, and viral pathogens. This review describes the present status of our knowledge concerning such defensive molecules in invertebrates.
MeSH term(s)	Animals ; Astacoidea/immunology ; Horseshoe Crabs/immunology ; Immunity, Innate ; Immunologic Factors/chemistry ; Immunologic Factors/physiology ; Insecta/immunology ; Invertebrates/chemistry ; Invertebrates/immunology ; Invertebrates/microbiology ; Urochordata/immunology
Chemical Substances	Immunologic Factors
Language	English
Publishing date	2005-04-07
Publishing country	Korea (South)
Document type	Journal Article ; Review
ZDB-ID	1238454-9
ISSN	0219-1024 ; 1225-8687
ISSN (online)	0219-1024
ISSN	1225-8687
DOI	10.5483/bmbrep.2005.38.2.128
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Article: Primitive Coagulation Systems and their Message to Modern Biology

Iwanaga, Sadaaki

Thrombosis and Haemostasis

1993 Volume 70, Issue 01, Page(s) 48–55

Language	English
Publishing date	1993-01-01
Publisher	Schattauer GmbH
Publishing place	Stuttgart ; New York
Document type	Article
ZDB-ID	518294-3
ISSN	2567-689X ; 0340-6245
ISSN (online)	2567-689X
ISSN	0340-6245
DOI	10.1055/s-0038-1646158
Database	Thieme publisher's database

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Article ; Online: Avathrin: a novel thrombin inhibitor derived from a multicopy precursor in the salivary glands of the ixodid tick,

Iyer, Janaki Krishnamoorthy / Koh, Cho Yeow / Kazimirova, Maria / Roller, Ladislav / Jobichen, Chacko / Swaminathan, Kunchithapadam / Mizuguchi, Jun / Iwanaga, Sadaaki / Nuttall, Patricia A / Chan, Mark Y / Kini, R Manjunatha

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

2017 Volume 31, Issue 7, Page(s) 2981–2995

Abstract: Tick saliva is a rich source of antihemostatic compounds. We amplified a cDNA from the salivary glands of the tropical bont tick ( ...

Abstract	Tick saliva is a rich source of antihemostatic compounds. We amplified a cDNA from the salivary glands of the tropical bont tick (
MeSH term(s)	Amino Acid Sequence ; Animals ; Carotid Artery Thrombosis/chemically induced ; Carotid Artery Thrombosis/drug therapy ; Cattle ; Chlorides/toxicity ; Cloning, Molecular ; Female ; Ferric Compounds/toxicity ; Fibrinogen/metabolism ; Humans ; Ixodidae/metabolism ; Kallikreins/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Nymph ; Peptides/pharmacology ; Salivary Glands/chemistry ; Salivary Glands/metabolism ; Thrombin/antagonists & inhibitors ; Trypsin/metabolism
Chemical Substances	Chlorides ; Ferric Compounds ; Peptides ; avathrin, Amblyomma variegatum ; Fibrinogen (9001-32-5) ; Kallikreins (EC 3.4.21.-) ; Trypsin (EC 3.4.21.4) ; Thrombin (EC 3.4.21.5) ; ferric chloride (U38V3ZVV3V)
Language	English
Publishing date	2017-07
Publishing country	United States
Document type	Journal Article
ZDB-ID	639186-2
ISSN	1530-6860 ; 0892-6638
ISSN (online)	1530-6860
ISSN	0892-6638
DOI	10.1096/fj.201601216R
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Zs.MO 296: Show issues

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Book: Bitamin K

Iwanaga, Sadaaki

igaku seibutsugaku ryōiki ni okeru shintenkai

1988

Author's details	kanshū Iwanaga Sadaaki, Saitō Hidehiko, Matsuda Michio
MeSH term(s)	Vitamin K
Language	Japanese
Size	iv, 332 p. :, ill.
Edition	Dai 1-han.
Publisher	Medikaru Jānarusha
Publishing place	Tōkyō
Document type	Book
ISBN	9784944012015 ; 4944012012
Database	Catalogue of the US National Library of Medicine (NLM)

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Article: Hemextin AB complex--a snake venom anticoagulant protein complex that inhibits factor VIIa activity.

Banerjee, Yajnavalka / Mizuguchi, Jun / Iwanaga, Sadaaki / Kini, R Manjunatha

Pathophysiology of haemostasis and thrombosis

2005 Volume 34, Issue 4-5, Page(s) 184–187

Abstract: Snake venom is a veritable gold mine of bioactive molecules, capable of binding to a wide variety of pharmacological targets, including the blood coagulation cascade. Here, we report the isolation and characterization of two synergistically acting ... ...

Abstract	Snake venom is a veritable gold mine of bioactive molecules, capable of binding to a wide variety of pharmacological targets, including the blood coagulation cascade. Here, we report the isolation and characterization of two synergistically acting anticoagulant three-finger proteins, hemextin A and hemextin B, from the venom of Hemachatus haemachatus (African Ringhals cobra). Hemextin A but not hemextin B exhibits mild anticoagulant activity. However, hemextin B interacts with hemextin A and forms a complex (hemextin AB complex), and synergistically enhances its anticoagulant potency. Prothrombin time assay showed that these two proteins form a 1:1 complex. Using a 'a dissection approach', we found that hemextins A and AB complex prolong clotting by inhibiting extrinsic tenase activity. Further studies showed that hemextin AB complex potently inhibits the proteolytic activity of factor VIIa (FVIIa) and its complexes. Kinetic studies showed that hemextin AB complex is a non-competitive inhibitor of FVIIa-soluble tissue factor proteolytic activity with a K(i) of 25 nM. Hemextin AB complex is the first reported natural inhibitor of FVIIa that does not require either tissue factor or factor Xa scaffold to mediate its inhibitory activity. Molecular interactions of hemextin AB complex with FVIIa/tissue factor-FVIIa may provide a new paradigm in the search for anticoagulants inhibiting the initiation of blood coagulation.
MeSH term(s)	Animals ; Anticoagulants ; Blood Coagulation/drug effects ; Elapid Venoms/pharmacology ; Elapid Venoms/therapeutic use ; Factor VIIa/antagonists & inhibitors ; Humans ; Kinetics ; Multiprotein Complexes/pharmacology ; Multiprotein Complexes/therapeutic use ; Thromboplastin/metabolism
Chemical Substances	Anticoagulants ; Elapid Venoms ; Multiprotein Complexes ; hemextin A protein, Hemachatus haemachatus ; hemextin B protein, Hemachatus haemachatus ; Thromboplastin (9035-58-9) ; Factor VIIa (EC 3.4.21.21)
Language	English
Publishing date	2005
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2080537-8
ISSN	1424-8840 ; 1424-8832
ISSN (online)	1424-8840
ISSN	1424-8832
DOI	10.1159/000092420
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Article: Hemextin AB complex, a unique anticoagulant protein complex from Hemachatus haemachatus (African Ringhals cobra) venom that inhibits clot initiation and factor VIIa activity.

Banerjee, Yajnavalka / Mizuguchi, Jun / Iwanaga, Sadaaki / Kini, R Manjunatha

The Journal of biological chemistry

2005 Volume 280, Issue 52, Page(s) 42601–42611

Abstract: During injury or trauma, blood coagulation is initiated by the interaction of factor VIIa (FVIIa) in the blood with freshly exposed tissue factor (TF) to form the TF.FVIIa complex. However, unwanted clot formation can lead to death and debilitation due ... ...

Abstract	During injury or trauma, blood coagulation is initiated by the interaction of factor VIIa (FVIIa) in the blood with freshly exposed tissue factor (TF) to form the TF.FVIIa complex. However, unwanted clot formation can lead to death and debilitation due to vascular occlusion, and hence, anticoagulants are important for the treatment of thromboembolic disorders. Here, we report the isolation and characterization of two synergistically acting anticoagulant proteins, hemextins A and B, from the venom of Hemachatus haemachatus (African Ringhals cobra). N-terminal sequences and CD spectra of the native proteins indicate that these proteins belong to the three-finger toxin family. Hemextin A (but not hemextin B) exhibits mild anticoagulant activity. However, hemextin B forms a complex (hemextin AB complex) with hemextin A and synergistically enhances its anticoagulant potency. Prothrombin time assay showed that these two proteins form a 1:1 complex. Complex formation was supported by size-exclusion chromatography. Using a "dissection approach," we determined that hemextin A and the hemextin AB complex prolong clotting by inhibiting TF.FVIIa activity. The site of anticoagulant effects was supported by their inhibitory effect on the reconstituted TF.FVIIa complex. Furthermore, we demonstrated their specificity of inhibition by studying their effects on 12 serine proteases; the hemextin AB complex potently inhibited the amidolytic activity of FVIIa in the presence and absence of soluble TF. Kinetic studies showed that the hemextin AB complex is a noncompetitive inhibitor of soluble TF.FVIIa amidolytic activity, with a Ki of 50 nm. Isothermal titration calorimetric studies showed that the hemextin AB complex binds directly to FVIIa with a binding constant of 1.62 x 10(5) m(-1). The hemextin AB complex is the first reported natural inhibitor of FVIIa that does not require a scaffold to mediate its inhibitory activity. Molecular interactions of the hemextin AB complex with FVIIa/TF.FVIIa will provide a new paradigm in the search for anticoagulants that inhibit the initiation of blood coagulation.
MeSH term(s)	Amino Acid Sequence ; Animals ; Anticoagulants/pharmacology ; Binding Sites ; Blood Coagulation/drug effects ; Calorimetry ; Chromatography ; Chromatography, Gel ; Circular Dichroism ; Cysteine Endopeptidases/chemistry ; Dose-Response Relationship, Drug ; Elapid Venoms/chemistry ; Elapid Venoms/metabolism ; Elapid Venoms/pharmacology ; Elapidae ; Factor VIIa/antagonists & inhibitors ; Factor VIIa/chemistry ; Factor X/antagonists & inhibitors ; Factor Xa Inhibitors ; Humans ; Inhibitory Concentration 50 ; Kinetics ; Models, Statistical ; Molecular Sequence Data ; Neoplasm Proteins/chemistry ; Prothrombin Time ; Sequence Homology, Amino Acid ; Serine Endopeptidases/chemistry ; Spectrometry, Mass, Electrospray Ionization ; Thrombin Time
Chemical Substances	Anticoagulants ; Elapid Venoms ; Factor Xa Inhibitors ; Neoplasm Proteins ; hemextin A protein, Hemachatus haemachatus ; hemextin B protein, Hemachatus haemachatus ; Factor X (9001-29-0) ; Serine Endopeptidases (EC 3.4.21.-) ; Factor VIIa (EC 3.4.21.21) ; Cysteine Endopeptidases (EC 3.4.22.-) ; cancer procoagulant (EC 3.4.22.26)
Language	English
Publishing date	2005-10-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M508987200
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