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Cathepsin L

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Cathepsin L
Identifiers
EC no.3.4.22.15
CAS no.60616-82-2
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Cathepsin L (EC 3.4.22.15, Aldrichina grahami cysteine proteinase) is an important lysosomal endopeptidase enzyme which is involved in the initiation of protein degradation.[1][2][3][4] It is a member of the Peptidase C1 family, which play an important role in diverse processes including normal lysosome mediated protein turnover, antigen and proprotein processing, and apoptosis.[5] Cathepsin L has been reported in many organisms including fish,[6] birds, mammals, and sponges.[7]

See also

References

  1. ^ Barrett, A.J.; Kirschke, H. (1981). "Cathepsin B, cathepsin H and cathepsin L". Methods Enzymol. 80: 535–561. doi:10.1016/s0076-6879(81)80043-2. PMID 7043200.
  2. ^ Barrett, A.J.; Buttle, D.J.; Mason, R.W. (1988). "Lysosomal cysteine proteinases". ISI Atlas of Science. Biochemistry. 1: 256–260.
  3. ^ Joseph, L.J.; Chang, L.C.; Stamenkovich, D.; Sukhatme, V.P. (1988). "Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L. An abundant transcript induced by transformation of fibroblasts". J. Clin. Invest. 81: 1621–1629. doi:10.1172/JCI113497. PMC 442598. PMID 2835398.
  4. ^ Kirschke, H.; Wikstrom, P.; Shaw, E. (1988). "Active center differences between cathepsins L and B: the S1 binding region". FEBS Lett. 228 (1): 128–130. doi:10.1016/0014-5793(88)80600-8. PMID 3342870.
  5. ^ Dickinson DP. Cysteine Peptidases of Mammals: Their Biological Roles and Potential Effects in the Oral Cavity and Other Tissues in Health and Disease, CROBM 2002 13: 238.
  6. ^ Venkatesh K, Prasanth B, Rajesh P, Annie JG, Mukesh P, Jesu A (2014). "A murrel cysteine protease, cathepsin L: bioinformatics characterization, gene expression and proteolytic activity". Biologia. 39: 395–406. doi:10.2478/s11756-013-0326-8.
  7. ^ Sevenich L, Pennacchio LA, Peters C, Reinheckel T.Human cathepsin L rescues the neurodegeneration and lethality in cathepsin B/L double-deficient mice. Biol Chem. 2006 Jul;387(7):885-91.