2005
Discovery and pre-clinical development of antithrombotics from hematophagous invertebrates.
Ledizet M, Harrison LM, Koskia RA, Cappello M. Discovery and pre-clinical development of antithrombotics from hematophagous invertebrates. Cardiovascular & Hematological Agents In Medicinal Chemistry 2005, 3: 1-10. PMID: 15638739, DOI: 10.2174/1568016052773315.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsNumerous invertebrate speciesHematophagous invertebratesInvertebrate speciesSpecific inhibitorUnique specificityInvertebratesFunctional strategiesCritical roleImpressive arrayActivation of thrombosisUseful therapeutic agentPre-clinical developmentNatural productsInhibitorsPlatelet inhibitorsHeart diseaseHuman illnessPlatelet functionClinical developmentSpeciesTherapeutic agentsAntithromboticsParasitesBloodmealThrombosis
2004
Disruption of Ixodes scapularis anticoagulation by using RNA interference
Narasimhan S, Montgomery RR, DePonte K, Tschudi C, Marcantonio N, Anderson JF, Sauer JR, Cappello M, Kantor FS, Fikrig E. Disruption of Ixodes scapularis anticoagulation by using RNA interference. Proceedings Of The National Academy Of Sciences Of The United States Of America 2004, 101: 1141-1146. PMID: 14745044, PMCID: PMC337020, DOI: 10.1073/pnas.0307669100.Peer-Reviewed Original ResearchConceptsAnti-factor Xa activityNumerous infectious diseasesIxodes scapularis ticksRNA interferenceMultiple anticoagulantsReduction of mRNAXa activityVaccine candidatesInfectious diseasesTick salivaAnticoagulantsBabesia microtiPhysiologic functionI. scapularis salivaSalivary glandsBorrelia burgdorferiTick feedingScapularis ticksAnticoagulant activityAnaplasma phagocytophilumTick engorgementSuch interventionsEngorgement weightEngorgementKey target
2002
A novel family of anticoagulants from the saliva of Ixodes scapularis
Narasimhan S, Koski RA, Beaulieu B, Anderson JF, Ramamoorthi N, Kantor F, Cappello M, Fikrig E. A novel family of anticoagulants from the saliva of Ixodes scapularis. Insect Molecular Biology 2002, 11: 641-650. PMID: 12421422, DOI: 10.1046/j.1365-2583.2002.00375.x.Peer-Reviewed Original ResearchConceptsN-terminal amino acid sequenceSalivary gland cDNA libraryAmino acid sequenceN-terminal sequenceCDNA libraryAcid sequenceAnticoagulant proteinsIxodes scapularisMolecular approachesTerminal sequenceIntrinsic pathwayEscherichia coliSpecific inhibitorNovel familyProteinSalp14Different functionsTick salivaSequenceBiological activityDose-dependent mannerProtease inhibitorsReversed-phase HPLCParaloguesScapularis
2001
Molecular Characterization of Ancylostoma Inhibitors of Coagulation Factor Xa HOOKWORM ANTICOAGULANT ACTIVITY IN VITRO PREDICTS PARASITE BLOODFEEDING IN VIVO *
Harrison LM, Nerlinger A, Bungiro RD, Córdova JL, Kuzmič P, Cappello M. Molecular Characterization of Ancylostoma Inhibitors of Coagulation Factor Xa HOOKWORM ANTICOAGULANT ACTIVITY IN VITRO PREDICTS PARASITE BLOODFEEDING IN VIVO *. Journal Of Biological Chemistry 2001, 277: 6223-6229. PMID: 11741914, DOI: 10.1074/jbc.m109908200.Peer-Reviewed Original ResearchConceptsCoagulation factor XaAdult A. ceylanicumHookworm speciesHuman vaccine developmentIron deficiency anemiaAnticoagulant activityFactor Xa inhibitory activityFactor Xa activityDog hookworm Ancylostoma caninumFactor XaXa inhibitory activityMechanism of actionFirst anticoagulantGastrointestinal hemorrhageDeficiency anemiaReverse transcription-PCRSpecies of hookwormXa activityPeptide-1Vaccine developmentHookworm Ancylostoma caninumA. ceylanicumAncylostoma ceylanicumHookwormAncylostoma caninum
1998
Tsetse thrombin inhibitor: Bloodmeal-induced expression of an anticoagulant in salivary glands and gut tissue of Glossina morsitans morsitans
Cappello M, Li S, Chen X, Li C, Harrison L, Narashimhan S, Beard C, Aksoy S. Tsetse thrombin inhibitor: Bloodmeal-induced expression of an anticoagulant in salivary glands and gut tissue of Glossina morsitans morsitans. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 14290-14295. PMID: 9826693, PMCID: PMC24366, DOI: 10.1073/pnas.95.24.14290.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAnticoagulantsAntithrombin ProteinsAntithrombinsBase SequenceBloodCloning, MolecularDigestive SystemDNA, ComplementaryEatingEscherichia coliFemaleGene Expression RegulationInsect ProteinsMaleMolecular Sequence DataPupaRecombinant ProteinsRNA, MessengerSalivary GlandsThrombinTranscription, GeneticTsetse FliesConceptsTsetse thrombin inhibitorPutative secretory signal peptideNative proteinGlossina morsitans morsitansFull-length cDNADegenerate oligonucleotide probeSecretory signal peptideSalivary gland cDNA libraryLack of homologyMorsitans morsitansUntranslated segmentSignal peptideInhibitor geneCDNA librarySingle copyTsetse genomeAdult tsetse fliesFamily of moleculesSegment codesEscherichia coliOptimal inhibitory activityOligonucleotide probesTsetse fliesSalivary glandsGut tissueAncylostoma caninum Anticoagulant Peptide Blocks Metastasis In Vivo and Inhibits Factor Xa Binding to Melanoma Cells In Vitro
Donnelly K, Bromberg M, Milstone A, Madison McNiff J, Terwilliger G, Konigsberg W, Cappello M. Ancylostoma caninum Anticoagulant Peptide Blocks Metastasis In Vivo and Inhibits Factor Xa Binding to Melanoma Cells In Vitro. Thrombosis And Haemostasis 1998, 79: 1041-1047. PMID: 9609244, DOI: 10.1055/s-0037-1615117.Peer-Reviewed Original ResearchConceptsAnti-metastatic activityThrombin generationAntimetastatic effectFactor XaEffector cell protease receptor-1Melanoma cellsTissue factor pathway inhibitorDose-dependent reductionFactor pathway inhibitorHuman coagulation factor XaHuman melanoma cellsFactor V/VaPulmonary metastasesSubcutaneous injectionSCID miceCoagulation factor XaVein injectionBlock metastasisReceptor 1Inhibits factor XaPathway inhibitorTumor cellsXa concentrationsProthrombinase activityPotential mechanisms
1993
Ancylostoma Factor Xa Inhibitor: Partial Purification and Its Identification as a Major Hookworm-Derived Anticoagulant In Vitro
Cappello M, Clyne L, McPhedran P, Hotez P. Ancylostoma Factor Xa Inhibitor: Partial Purification and Its Identification as a Major Hookworm-Derived Anticoagulant In Vitro. The Journal Of Infectious Diseases 1993, 167: 1474-1477. PMID: 8501344, DOI: 10.1093/infdis/167.6.1474.Peer-Reviewed Original ResearchMeSH KeywordsAncylostomaAnimalsAnticoagulantsChromatography, GelDogsFactor Xa InhibitorsHumansSolubilityConceptsPotent factor Xa inhibitorsIon-exchange column chromatographyColumn chromatographyAnticoagulant activityAncylostoma hookwormsPartial thromboplastin timePeptide substratesColumn fractionsProthrombin timeChromogenic peptide substratesPartial purificationAnti-Xa activityFactor Xa inhibitorsChromatographyTime assaysPurificationSoluble protein extractsThromboplastin timeXa inhibitors