Serine Proteases Affecting Blood Coagulation and Fibrinolysis from Snake Venoms

Kini, R. Manjunatha

doi:10.1159/000092424

Cited by 160 publications

(124 citation statements)

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“…Use of anti-coagulants reduces the risk of clot formation and thus various anti-coagulants are being sought (Hart and Halperin, 1999;van Walraven et al, 2006). Snake venoms, particularly crotalid and viperid venoms are rich in proteases that affect the blood coagulation cascade by various mechanisms (Kini, 2005). Anticoagulant activity of snake venom proteases is mainly due to fibrinogen degradation.…”

Section: Resultsmentioning

confidence: 99%

“…Snake venoms contain many biologically active proteins that interact with the hemostatic system by interfering with various steps of coagulation cascade (Markland, 1998a,b;Kini, 2005). Venom proteases from the families Viperidae and Crotalidae are functionally classified as pro-coagulants or anti-coagulants (Kornalik, 1991), depending upon their specific action on selective factors of the blood coagulation cascade including fibrinogen, prothrombin, factor-X and factor-V (Braud et al, 2000;Kini, 2005).…”

Section: Introductionmentioning

confidence: 99%

“…Venom proteases from the families Viperidae and Crotalidae are functionally classified as pro-coagulants or anti-coagulants (Kornalik, 1991), depending upon their specific action on selective factors of the blood coagulation cascade including fibrinogen, prothrombin, factor-X and factor-V (Braud et al, 2000;Kini, 2005). Proteases that hydrolyze fibrinogen are termed as snake venom fibrinogenolytic enzymes (SVFEs).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Malabarase, a serine protease with anticoagulant activity from Trimeresurus malabaricus venom

Kumar

Manjunath

Joshi

et al. 2013

Comparative Biochemistry and Physiology Part B: Biochemistry an

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Malabarase, a serine protease with anticoagulant activity from Trimeresurus malabaricus venom

Kumar

Manjunath

Joshi

et al. 2013

Comparative Biochemistry and Physiology Part B: Biochemistry an

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“…Cerastes) and colubrids (Dispholidus typus) (9). Some TLE from snake venoms with known complete amino acid sequences are: ancrod (Calloselasma rhodostoma,…”

Section: Bothrops Crotalus Lachesis and Trimeresurus) As Well As Imentioning

confidence: 99%

Purification and partial characterization of a coagulant serine protease from the venom of the Iranian snake Agkistrodon halys

Ghorbanpur

Mirakabadi

Zokaee

et al. 2009

J. Venom. Anim. Toxins incl. Trop. Dis

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ABSTRACT:Agkistrodon halys is one of several dangerous snake species in Iran. Among the most important signs and symptoms in patients envenomated by this snake is disseminated intravascular coagulation. A thrombin-like enzyme, called AH143, was isolated from Agkistrodon halys venom by gel filtration on a Sephadex G-50 column, ion-exchange chromatography on a DEAE-Sepharose and high performance liquid chromatography (HPLC) on a C18 column. In the final stage of purification, 0.82 mg of purified enzyme was obtained from 182.5 mg of venom. The purified enzyme showed a single protein band by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), under reducing conditions, and its molecular mass was found to be about 30 kDa. AH143 revealed clotting activity in human plasma, which was not inhibited by EDTA or heparin. This enzyme still demonstrated coagulation activity when exposed to variations in temperature and pH ranging, respectively, from 30 to 40°C and from 7.0 to 8.0. It also displayed proteolytic activities on synthetic substrate. The purified enzyme did not show any effect on casein. We concluded that the venom of the Iranian snake Agkistrodon halys contains about 0.45% single procoagulant protein which appears to be a thrombin-like enzyme.

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“…They mainly affect the haemostatic system of the prey or victim [6]. Indeed, a number of snake venom serine proteases that affect haemostasis have been reported, including procoagulant, anticoagulant, platelet aggregating or fibrinolytic proteases [7][8][9].…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning and sequence analysis of serine protease cDNA from the venom of the centipede Scolopendra subspinipes dehaani

Meunchan¹,

Thammasirirak²,

Daduang³

et al. 2015

Turk J Bioch

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Molecular cloning and sequence analysis of serine protease cDNA from the venom of the centipede Scolopendra subspinipes dehaani [Scolopendra subspinipes dehaani kırkayak zehrinden elde edilen serin proteaz cDNA'sının moleküler klonlaması ve dizi analizi] ABSTRACT Objective: Proteolytic enzymes are one of the well-known components of animal venom. The aim of this study was to identify protease from the venom gland of Scolopendra subspinipes dehaani. Methods: After total RNA extraction, a cDNA encoding a serine protease was identified by RT-PCR and was subsequently sequenced. The sequence was analysed by multiple alignment and homology modelling. Results: A cDNA encoding the precursor of a centipede venom serine protease was identified. The full-length cDNA was 1,014 nucleotides with 780 nucleotides of open reading frame. The precursor nucleotide sequence encoded a signal peptide of 19 residues and a mature protein of 260 residues. It belonged to clan PA of serine proteases in the MEROPS database classification. Catalytic residues were identified by multiple alignments, including an unusual hydrogen bond network in the catalytic site. Secondary structure prediction and homology modelling revealed a chymotrypsin-like fold, which is characteristic of PA clan proteases. Conclusion:The sequence of the identified serine protease showed unusual features, making this centipede venom serine protease an interesting candidate to investigate. A better understanding of the molecular mechanism of venom components will be useful for further applications and help to improve envenomation treatment. Key Words: Scolopendra subspinipes dehaani, cDNA, serine protease Conflict of Interest: The authors have no conflict of interest. ÖZETAmaç: Proteolitik enzimler hayvan zehirlerinin en çok bilinen bileşenlerinden biridir. Bu ça-lışmanın amacı Scolopendra subspinipes dehaani zehir salgı bezinden proteaz enziminin tanımlanmasıdır. Metod: Toplam RNA eldesinin ardından, RT-PCR tekniği kullanılarak serin proteaz proteinini kodlayan gene ait cDNA tanımlanmış ve dizi analizine tabi tutulmuştur. Elde edilen dizi çoklu dizi hizalama ve homoloji modelleme ile analiz edilmiştir. Bulgular: Kırkayak zehirinde bulunan serin proteaz öncülünü kodlayan bir cDNA tanımlan-mıştır. cDNA, 780 nükleotit açık okuma çerçevesinde olmak üzere, toplam 1.014 nükleotit uzunluğundadır. Öncül nükleotit dizisi 19 amino asitlik bir sinyal peptidini ve 260 amino asitlik olgun proteini kodlamaktadır. Bu protein MEROPS veritabanı sınıflandırmasına göre serin proteazlardan PA grubuna aittir. Çoklu dizi hizalama kullanılarak alışılmadık bir hidrojen bağı örgüsüne sahip katalitik bölge ve bu bölgedeki katalitik aminoasitler tanımlanmıştır. İkincil yapı tahmin ve homoloji modelleme çalışmaları PA grup proteazlara özgün olan kimotiripsin benzeri katlanmayı göstermiştir. Sonuç: Tanımlanan serin proteaz dizisi alışılmadık özellikler göstermesi sebebiyle kırkayak zehrindeki serin proteaz enzimini ileri çalışmalar için aday yapmıştır. Venom bileşenlerinin moleküler mekanizmalarının...

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Serine Proteases Affecting Blood Coagulation and Fibrinolysis from Snake Venoms

Cited by 160 publications

References 103 publications

Malabarase, a serine protease with anticoagulant activity from Trimeresurus malabaricus venom

Malabarase, a serine protease with anticoagulant activity from Trimeresurus malabaricus venom

Purification and partial characterization of a coagulant serine protease from the venom of the Iranian snake Agkistrodon halys

Molecular cloning and sequence analysis of serine protease cDNA from the venom of the centipede Scolopendra subspinipes dehaani

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