Katepsin

Katepsin
Struktura katepsina K
Identifikatori
SimbolCTP
PfamPF00112
Pfam klanCL0125
InterProIPR000668
SMARTPept_C1
PROSITEPDOC00126
MEROPSC1
SCOP1aec
SUPERFAMILY1aec

Katepsini (grč. kata = dole + hepsein = vri; skr. CTS) su proteazni (enzimi koji razgrađuju proteine), nađeni kod svih životinja, kao i ostalih organizama.

Postoji oko desetak članova ove porodice, koji se izdvajaju po svojoj strukturi, katalitičkom mehanizmu i proteinskim suptratima. Većina članova koji postaju aktivni na niskom pH nađena je u lizosomima. Aktivnost enzima ove porodice se odvija gotovo u potpunosti unutar tih organela. Postoje, međutim, izuzeci kao što je katepsin K, koji deluje vanćelijski, nakon lučenja osteoklasta u resorpciji kosti.[1][2][3]

Katepsin S ima ključnu ulogu u ćelijskom prometu sisara, npr. u resorpciji kostiju. Oni degradiraju polipeptide i odlikuju se specifičnošću za odgovarajuće supstrate.[4][5][6][7]

Klasifikacija

Klinički značaj

Katepsini uzimaju učešća u više bolesnih stanja i poremećaja, kao što su:

Vidi još

Reference

  1. ^ Cornish-Bowden A. (2004): Fundamentals of enzyme kinetics, 3rd Ed. Portland Press. ISBN 9781855781580; ISBN 1855781581.
  2. ^ Međedović S., Maslić E., Hadžiselimović, Rifat (2000). Biologija 2. ISBN 9958-10-222-6. . Svjetlost, Sarajevo, .
  3. ^ Bajrović K, Jevrić-Čaušević A., Hadžiselimović, Rifat, Ed. (2005): Uvod u genetičko inženjerstvo i biotehnologiju. Institut za genetičko inženjerstvo i biotehnologiju (INGEB), Sarajevo, ISBN 9958-9344-1-8.
  4. ^ Palmer T., Bonner P. L. (2007). Enzymes: Biochemistry, biotechnology, clinical hemistry. Woodhead Publishing. ISBN 978-1-904275-27-5. 
  5. ^ Bugg T. (1997). An introduction to enzyme and coenzyme chemistry. ISBN 0-86542-793-3. . Blackwell Science, Oxford, .
  6. ^ Alberts B. (2002)ː Molecular biology of the cell Garland Science, New York, ISBN 0-8153-3218-1.
  7. ^ Voet D., Voet J. (1995): Biochemistry, 2nd Ed. Wiley, http://www.wiley.com/college/math/chem/cg/sales/voet.html.
  8. ^ Nomura T, Katunuma N (2005). „Involvement of cathepsins in the invasion, metastasis and proliferation of cancer cells” (PDF). J. Med. Invest.. 52 (1–2): 1—9. PMID 15751268. doi:10.2152/jmi.52.1. 
  9. ^ Lipton P (1999). „Ischemic cell death in brain neurons”. Physiol. Rev.. 79 (4): 1431—568. PMID 10508238. doi:10.1152/physrev.1999.79.4.1431. 
  10. ^ Yamashima T (2013). „Reconsider Alzheimer's disease by the 'calpain-cathepsin hypothesis'--a perspective review”. Progress in Neurobiology. 105: 1—23. PMID 23499711. doi:10.1016/j.pneurobio.2013.02.004. 
  11. ^ Raptis SZ, Shapiro SD, Simmons PM, Cheng AM, Pham CT (2005). „Serine protease cathepsin G regulates adhesion-dependent neutrophil effector functions by modulating integrin clustering”. Immunity. 22 (6): 679—91. PMID 15963783. doi:10.1016/j.immuni.2005.03.015. 
  12. ^ Chandran K (2005). „Endosomal Proteolysis of the Ebola Virus Glycoprotein Is Necessary for Infection”. Science. 308 (5728): 1643—1645. Bibcode:2005Sci...308.1643C. PMC 4797943 Слободан приступ. PMID 15831716. doi:10.1126/science.1110656. 
  13. ^ Im E, Kazlauskas A (2007). „The role of cathepsins in ocular physiology and pathology”. Exp. Eye Res.. 84 (3): 383—8. PMID 16893541. doi:10.1016/j.exer.2006.05.017. 

Spoljašnje veze

  • The MEROPS online database for peptidases and their inhibitors: „A01.010”. Архивирано из оригинала 23. 12. 2012. г. Приступљено 19. 11. 2016. 
  • Cathepsins на US National Library of Medicine Medical Subject Headings (MeSH)

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