Journals / Kocatepe Veteriner Dergisi / 2018 / Cilt: 11 - Sayı: 1

Apoptotic and Non-Apoptotic Effects of Granzyme

Granzimlerin Apoptotik ve Non-Apoptotik Etkileri

Pages
96–103
Publication Date
2018-03-01
DOI
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AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

The increased levels of circulating granzymes and disintegration of extracellular substrates into granules in various inflammatory processes indicate that these proteases may have extracellular effects on pathogenesis of chronic inflammatory diseases, rejection of tumor cells and viral infections.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:Granzymes (granule enzymes) are proteases that are released from the granules of cytotoxic lymphocytes into target cells to protect mammals from altered cells and virus infections.
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Key Findings & Data:Granzymes released into the target cell cytoplasm activate some specific pathways to effect the death of these cells.
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Conclusion & Impact:The increased levels of circulating granzymes and disintegration of extracellular substrates into granules in various inflammatory processes indicate that these proteases may have extracellular effects on pathogenesis of chronic inflammatory diseases, rejection of tumor cells and viral infections.
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:Granzim · Granzim A · Granzim B

Abstract

Granzymes (granule enzymes) are proteases that are released from the granules of cytotoxic lymphocytes into target cells to protect mammals from altered cells and virus infections. Granzymes released into the target cell cytoplasm activate some specific pathways to effect the death of these cells. Although the realization of death of the target cell is regarded as the main function of these proteases, the findings show that they have other functions besides cell death. Granzymes can display antiviral activity directly by breaking down the proteins they encode so that the virus can survive life cycles in the host. The increased levels of circulating granzymes and disintegration of extracellular substrates into granules in various inflammatory processes indicate that these proteases may have extracellular effects on pathogenesis of chronic inflammatory diseases, rejection of tumor cells and viral infections.

Özet

Granzimler (granül enzimler), değişime uğramış hücreler ve virüs enfeksiyonlarından memelileri korumak için hedef hücreler içerisine sitotoksik lenfositlerin granüllerinden salınan proteazlardır. Hedef hücre sitoplazmalarının içerisine salınan granzimler bu hücrelerin ölümünü gerçekleştirmek amacıyla bazı spesifik yolları harekete geçirirler. Hedef hücrenin ölümünün gerçekleştirilmesi bu proteazların esas fonksiyonları olarak değerlendirilse de elde edilen bulgular hücre ölümü dışında başka fonksiyonlara da sahip olduklarını göstermektedir. Granzimler, virusların konakçıda hayat sikluslarını devam ettirebilmeleri için kodladıkları proteinleri parçalamak suretiyle doğrudan antiviral aktivite de gösterebilmektedirler. Çeşitli yangısal süreçlerde dolaşımdaki granzimlerin seviyelerinin artması ve ekstraselüler substratların granzimlerce parçalanması bu proteazların kronik inflamatuar hastalıkların patogenezisi, tümör hücrelerinin rejeksiyonu ve viral enfeksiyonlarla ilgili ekstraselüler etkilere sahip olabileceğini de göstermektedir.

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Cite This Article

KESKİN, E., HATİPOĞLU, D. (2018). Apoptotic and Non-Apoptotic Effects of Granzyme. Kocatepe Veteriner Dergisi, Cilt: 11 - Sayı: 1, 96–103. https://ajindex.com/articles/124846

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References (13)

  1. Adrain C, Murphy BM, Martin SJ. Molecular ordering of the caspase activation cascade initiated by the cytotoxic T lymphocyte/natural killer (CTL/NK) protease granzyme B. 2005; Journal of Biological Chemistry, 280, 6, 4663-4673.
  2. Andrade F, Bull HG, Thornberry NA, Ketner GW, Casciola-Rosen LA, Rosen A. Adenovirus L4-100K assembly protein is a granzyme B substrate that potently inhibits granzyme B-mediated cell death. 2001; Immunity, 14, 6, 751-761.
  3. Andrade F, Casciola-Rosen LA, Rosen A. Granzyme B-induced cell death. 2004; Acta haematologica, 111, 1-2, 28-41.
  4. Andrade F, Casciola-Rosen LA, Rosen A. A novel domain in adenovirus L4-100K is required for stable binding and efficient inhibition of human granzyme B: possible interaction with a species-specific exosite. 2003; Molecular and cellular biology, 23, 17, 6315-6326.
  5. Andrade F, Fellows E, Jenne DE, Rosen A, Young C. Granzyme H destroys the function of critical adenoviral proteins required for viral DNA replication and granzyme B inhibition. 2007; The EMBO Journal, 26, 8, 2148-2157.
  6. Bade B, Boettcher HE, Lohrmann J, Hink-Schauer C, Bratke K, Jenne DE, Virchow Jr JC, Luttmann W. Differential expression of the granzymes A, K and M and perforin in human peripheral blood lymphocytes. 2005; International immunology, 17, 11, 1419-1428.
  7. Beresford PJ, Xia Z, Greenberg AH, Lieberman J. Granzyme A loading induces rapid cytolysis and a novel form of DNA damage independently of caspase activation. 1999; Immunity, 10, 5, 585-595.
  8. Boya P, Pauleau A-L, Poncet D, Gonzalez-Polo R-A, Zamzami N, Kroemer G. Viral proteins targeting mitochondria: controlling cell death. 2004; Biochimica et Biophysica Acta (BBA)-Bioenergetics, 1659, 2, 178-189.
  9. Brunner G, Simon MM, Kramer MD. Activation of pro-urokinase by the human T cell-associated serine proteinase HuTSP-1. 1990; FEBS letters, 260, 1, 141-144.
  10. Buzza MS, Bird PI. Extracellular granzymes: current perspectives. 2006; Biological chemistry, 387, 7, 827-837.
  11. Buzza MS, Zamurs L, Sun J, Bird CH, Smith AI, Trapani JA, Froelich CJ, Nice EC, Bird PI. Extracellular matrix remodeling by human granzyme B via cleavage of vitronectin, fibronectin, and laminin. 2005; Journal of Biological Chemistry, 280, 25, 23549-23558.
  12. Casciola-Rosen L, Andrade F, Ulanet D, Wong WB, Rosen A. Cleavage by granzyme B is strongly predictive of autoantigen status. 1999; Journal of Experimental Medicine, 190, 6, 815-826.
  13. Casciola-Rosen L, Garcia-Calvo M, Bull HG, Becker JW, Hines T, Thornberry NA, Rosen A. Mouse a