関: streptodornase and streptokinase

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/11/21 20:57:51」(JST)

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Streptokinase (SK) is a protein secreted by several species of streptococci that can bind and activate human plasminogen. SK is used as an effective and inexpensive thrombolysis medication in some cases of myocardial infarction (heart attack)^[2] and pulmonary embolism.^[3] Streptokinase belongs to a group of medications known as fibrinolytics, and complexes of streptokinase with human plasminogen can hydrolytically activate other unbound plasminogen by activating through bond cleavage to produce plasmin. There are three domains to Streptokinase, denoted α (residues 1–150), β (residues 151–287), and γ (residues 288–414). Each domain binds plasminogen, although none can activate plasminogen independently.^[4]

Mechanism of action[edit]

Proposed counterion for Asp740 is Lys698 create salt-bridge; structure derived from PDB file 1BML

Youtube Substrate Enzyme Mechanism Movie

Plasmin is produced in the blood to break down fibrin, the major constituent of blood thrombi, thereby dissolving clots once they have fulfilled their purpose of stopping bleeding. Extra production of plasmin caused by streptokinase breaks down unwanted blood clots, for example, in the lungs (pulmonary embolism). The usual activation of Plasminogen (Plgn) is by proteolysis of the Arg561—Val562 bond.^[5] The amino group of Val562 then forms a salt-bridge with Asp740, which triggers a conformational change producing the active protease Plasmin (Pm). When (SK) is present, it binds to Plgn to form a complex (SK. Plgn) that converts substrate Plgn to Pm. Residues 1–59 of SK regulate its capacity to induce an active site in bound Pg by a nonproteolytic mechanism and to activate substrate Pg in a fibrin-independent manner. This complex subsequently rearranges to an active complex although the Arg561–Val562 bond remains intact. Therefore another residue must substitute for the free amino group of Val562 and provide a counterion for Asp740 in this active complex.^[6] Two candidates for this counterion have been suggested: Ile1 of streptokinase and Lys698 of Plgn. Deletion of Ile1 of SK markedly inhibits its capacity to induce an active site in plasminogen, which supports the hypothesis that establishment of a salt bridge between Ile1 of SK and Asp740 of plasminogen is necessary for SK to induce an active site in plasminogen by a nonproteolytic mechanism.^[7] In contrast with the Ile1 substitutions, the Lys698 mutations also decreased the dissociation constant of the SK complex by 15 to 50 fold. These observations suggest that Lys698 is involved in formation of the initial SK·Plgn complex.^[8]

Contraindications[edit]

Severe hypertension recent stroke
Cerebral neoplasm
Recent history of peptic ulcer disease
Ulcerative colitis
Pancreatitis
Subacute bacterial endocarditis
Coagulation defects also due to liver or kidney disease
Recent surgery
Childbirth.
Hypersensitivity
Increased risk of cerebral bleeding
Trauma
Pregnancy
Active internal bleeding
Bleeding GI lesions.

Administration[edit]

Streptokinase is given intravenously as soon as possible after the onset of a heart attack to dissolve clots in the arteries of the heart wall. As Streptokinase is a bacterial product, the body has the ability to build up an immunity to it. Therefore, it is recommended that this medication should not be used again after four days from the first administration, as it may not be as effective and can also cause an allergic reaction. For this reason, it is usually given only for a person's first heart attack. Further thrombotic events could be treated with Tissue plasminogen activator (tPA). Overdose of streptokinase or tPA can be treated with aminocaproic acid.

Laboratory findings in various platelet and coagulation disorders (V - T)
Condition	Prothrombin time	Partial thromboplastin time	Bleeding time	Platelet count
Vitamin K deficiency or warfarin	Prolonged	Normal or mildly prolonged	Unaffected	Unaffected
Disseminated intravascular coagulation	Prolonged	Prolonged	Prolonged	Decreased
Von Willebrand disease	Unaffected	Prolonged or unaffected	Prolonged	Unaffected
Hemophilia	Unaffected	Prolonged	Unaffected	Unaffected
Aspirin	Unaffected	Unaffected	Prolonged	Unaffected
Thrombocytopenia	Unaffected	Unaffected	Prolonged	Decreased
Liver failure, early	Prolonged	Unaffected	Unaffected	Unaffected
Liver failure, end-stage	Prolonged	Prolonged	Prolonged	Decreased
Uremia	Unaffected	Unaffected	Prolonged	Unaffected
Congenital afibrinogenemia	Prolonged	Prolonged	Prolonged	Unaffected
Factor V deficiency	Prolonged	Prolonged	Unaffected	Unaffected
Factor X deficiency as seen in amyloid purpura	Prolonged	Prolonged	Unaffected	Unaffected
Glanzmann's thrombasthenia	Unaffected	Unaffected	Prolonged	Unaffected
Bernard-Soulier syndrome	Unaffected	Unaffected	Prolonged	Decreased or unaffected
Factor XII deficiency	Unaffected	Prolonged	Unaffected	Unaffected
C1INH deficiency	Unaffected	Shortened	Unaffected	Unaffected

Current research applications[edit]

Streptokinase may find a use in helping to prevent postoperative adhesions, a common complication of surgery, especially abdominal surgery (appendectomy, gall stones, hysterectomy, etc.) One study using animal models (rats) found that when used with a PHBV membrane drug-delivery system, it was 90 percent effective in preventing adhesions.^[9]

Marketing[edit]

It is marketed in Chile as Streptase by Alpes Selection, under license of ZLB Behring from Marburg, Germany.

Available in Viet Nam under the name Mutose. Available in Cuba, Venezuela, Ecuador and other Latin American countries under the trademark Heberkinasa, commercialized by Heber Biotech, Havana, Cuba. Available in India under the name STPase by Cadila Pharmaceuticals Limited & Myokinase by Biocon Limited

References[edit]

^ Rabijns A, De Bondt HL, De Ranter C (May 1997). "Three-dimensional structure of staphylokinase, a plasminogen activator with therapeutic potential". Nat. Struct. Biol. 4 (5): 357–60. doi:10.1038/nsb0597-357. PMID 9145104.
^ Sikri N, Bardia A (2007). "A history of streptokinase use in acute myocardial infarction". Tex Heart Inst J 34 (3): 318–27. PMC 1995058. PMID 17948083.
^ Meneveau N, Schiele F, Vuillemenot A, et al. (July 1997). "Streptokinase vs alteplase in massive pulmonary embolism. A randomized trial assessing right heart haemodynamics and pulmonary vascular obstruction". Eur. Heart J. 18 (7): 1141–8. PMID 9243149.
^ Mundada L, Prorok, M (2003). "Structure-Function Analysis of Streptokinase Amino Terminus". Journal of Biological Chemistry 278 (3): 24421–24427. doi:10.1074/jbc.M301825200. PMID 5746739.
^ Young, K Shi, G (1997). "Plasminogen Activation by Streptokinase iva a Unique Mechanism". Texas Heart Institute journal / from the Texas Heart Institute of St. Luke's Episcopal Hospital, Texas Children's Hospital 34 (3): 1–13. PMID 5643782. ^{[dead link]}
^ Loy, J, Lin,X (2001). "Domain Interactions between Streptokinase and Human Plasminogen". Biochemistry 48 (3): 14686–14695. doi:10.1021/bio11309d. PMID 45675.
^ Wang, S, Reed, GL, Hedstrom, L (1999). "Deletion of Ile1 changes the mechanism of streptokinase: evidence for the molecular sexuality hypothesis". Biochemistry 38 (16): 5232–5240. doi:10.1021/bi981915h. PMID 10213631.
^ Wang X, Lin X (1998). "Crystal Structure of Catalytic Domain of Human Plasmin Complexed with Streptokinase". Science Magazine 281 (3): 1662–1665. PMID 76543.
^ A. Yagmurlu, M. Barlas, I. Gursel, I.H. Gokcora (2003). "Reduction of Surgery-Induced Peritoneal Adhesions by Continuous Release of Streptokinase from a Drug Delivery System". Eur Surg Res 35 (1): 46–49. doi:10.1159/000067035. PMID 12566787.

English Journal

Delayed-type hypersensitivity skin test responses to PPD and other antigens among BCG-vaccinated HIV-1-infected and healthy children and adolescents.

Costa NM, Albuquerque M, Lins JB, Alvares-Junior JT, Stefani MM.SourceInstituto de Patologia Tropical e Saúde Pública, Universidade Federal de Goiás, Goiânia, Brazil.
Revista da Sociedade Brasileira de Medicina Tropical.Rev Soc Bras Med Trop.2011 Oct;44(5):542-5. Epub 2011 Aug 26.
INTRODUCTION: Among HIV-1-infected patients, CD4+ T cell counts are well-established markers of cell-mediated immunity. Delayed-type hypersensitivity (DTH) skin tests can be used to evaluate in vivo cell-mediated immunity to common antigens.METHODS: DTH responses to tuberculin purified protein deriv
PMID 21877065

Virulence gene pool detected in bovine group C Streptococcus dysgalactiae subsp. dysgalactiae isolates by use of a group A S. pyogenes virulence microarray.

Rato MG, Nerlich A, Bergmann R, Bexiga R, Nunes SF, Vilela CL, Santos-Sanches I, Chhatwal GS.SourceCentro de Recursos Microbiológicos, Departamento de Ciências da Vida, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Campus de Caparica, 2829-516 Caparica, Portugal.
Journal of clinical microbiology.J Clin Microbiol.2011 Jul;49(7):2470-9. Epub 2011 Apr 27.
A custom-designed microarray containing 220 virulence genes of Streptococcus pyogenes (group A Streptococcus [GAS]) was used to test group C Streptococcus dysgalactiae subsp. dysgalactiae (GCS) field strains causing bovine mastitis and group C or group G Streptococcus dysgalactiae subsp. equisimilis
PMID 21525223

Japanese Journal

Effect of Varidase (streptodornase) on biofilm formed by Pseudomonas aeruginosa

Nemoto K,Hirota K,Murakami K,Taniguti K,Murata H,Viducic D,Miyake Y
CHEMOTHERAPY 49(3), 121-125, 2003
NAID 120004211197

ポリアクリル酸ナトリウム添加ストレプトキナーゼゼリーを使用した酵素的デブリドマン

岡本泰岳,中根織絵,深津雅史,鵜飼潤
日形会誌 : 日本形成外科学会会誌 = Journal of Japan Society of Plastic and Reconstructive Surgery 20(4), 253-257, 2000-04-20
NAID 10011319860

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リンク元	「バリダーゼ」「streptodornase and streptokinase」

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Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Staphylokinase/Streptokinase family
	; Structure of staphylokinase, a plasminogen activator.
Identifiers
Symbol	Staphylokinase
Pfam	PF02821
InterPro	IPR004093
SCOP	2sak
SUPERFAMILY	2sak
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Streptokinase C
	; Complex of Catalytic Domain of Human Plasmin and Streptokinase; structure derived from PDB file 1BML.
Identifiers
Symbol	skc
Entrez	8110746
PDB	1BML (RCSB PDB PDBe PDBj)
UniProt	P00779
Other data
EC number	3.4.24.29

　　[★]

英: varidase
関: ストレプトドルナーゼ・ストレプトキナーゼ

「streptodornase and streptokinase」

　　[★]

ストレプトドルナーゼ・ストレプトキナーゼ

関: varidase

[pmid9145104-1] Rabijns A, De Bondt HL, De Ranter C (May 1997). "Three-dimensional structure of staphylokinase, a plasminogen activator with therapeutic potential". Nat. Struct. Biol. 4 (5): 357–60. doi:10.1038/nsb0597-357. PMID 9145104.

[pmid17948083-2] Sikri N, Bardia A (2007). "A history of streptokinase use in acute myocardial infarction". Tex Heart Inst J 34 (3): 318–27. PMC 1995058. PMID 17948083.

[pmid9243149-3] Meneveau N, Schiele F, Vuillemenot A, et al. (July 1997). "Streptokinase vs alteplase in massive pulmonary embolism. A randomized trial assessing right heart haemodynamics and pulmonary vascular obstruction". Eur. Heart J. 18 (7): 1141–8. PMID 9243149.

[pmid5746739-4] Mundada L, Prorok, M (2003). "Structure-Function Analysis of Streptokinase Amino Terminus". Journal of Biological Chemistry 278 (3): 24421–24427. doi:10.1074/jbc.M301825200. PMID 5746739.

[pmid5643782-5] Young, K Shi, G (1997). "Plasminogen Activation by Streptokinase iva a Unique Mechanism". Texas Heart Institute journal / from the Texas Heart Institute of St. Luke's Episcopal Hospital, Texas Children's Hospital 34 (3): 1–13. PMID 5643782. ^{[dead link]}

[pmid45675-6] Loy, J, Lin,X (2001). "Domain Interactions between Streptokinase and Human Plasminogen". Biochemistry 48 (3): 14686–14695. doi:10.1021/bio11309d. PMID 45675.

[PMID10213631-7] Wang, S, Reed, GL, Hedstrom, L (1999). "Deletion of Ile1 changes the mechanism of streptokinase: evidence for the molecular sexuality hypothesis". Biochemistry 38 (16): 5232–5240. doi:10.1021/bi981915h. PMID 10213631.

[pmid76543-8] Wang X, Lin X (1998). "Crystal Structure of Catalytic Domain of Human Plasmin Complexed with Streptokinase". Science Magazine 281 (3): 1662–1665. PMID 76543.

[pmid12566787-9] A. Yagmurlu, M. Barlas, I. Gursel, I.H. Gokcora (2003). "Reduction of Surgery-Induced Peritoneal Adhesions by Continuous Release of Streptokinase from a Drug Delivery System". Eur Surg Res 35 (1): 46–49. doi:10.1159/000067035. PMID 12566787.

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varidase