Skip to main content

A new cleavage site for elastase within the complement component 3

Buy Article:

$51.00 plus tax (Refund Policy)

Claesson R, Kanasi E, Johansson A, Kalfas S. A new cleavage site for elastase within the complement component 3. APMIS 2010; 118: 765–68.

The lysosomal enzyme elastase was earlier shown to cleave the complement molecule C3. During some preliminary experiments on the interactions of certain pathogenic bacteria with the innate defence mechanisms, we observed C3 cleavage, in the presence of elastase, to fragments not previously described. To elucidate this proteolytic reaction, the present study was conducted. Degradation of C3 in mixtures with elastase or cathepsin G was detected by an immunoblot procedure using anti-C3c and anti-C3d antibodies after separating the proteins by SDS-PAGE. Certain C3 fragments were analysed for amino acid sequence. The results revealed the existence of a cleavage site for elastase at the position alanine1350/lysine1351 of the C3 molecule, which has not been previously described. The fragment resulted from this cleavage has a size of about 39 kDa and it contains a part or the whole of C3d. This cleavage was distinct from the one previously described at position 987/988, which gives a 34 kDa C3d-containing fragment.
No References
No Citations
No Supplementary Data
No Data/Media
No Metrics

Keywords: C3; Elastase; cleavage

Document Type: Research Article

Affiliations: 1: Department of Odontology, Umeå University, Umeå, Sweden 2: School of Dentistry, Aristotle University of Thessaloniki, Thessaloniki, Greece

Publication date: 2010-10-01

  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more