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. 2015 Mar 15;128(6):1139–1149. doi: 10.1242/jcs.163063

Fig. 3.

Fig. 3.

Fz4 inhibits ADAM13 proteolytic activity. (A) Western blot showing the cleavage of the proto-cadherin PAPC by ADAM13. The medium from transfected cells was collected and glycoproteins purified using concanavalin-A–agarose beads (ConA). The extracellular fragment of PAPC (60 kDa) is present when ADAM13 is co-transfected (lane 1) but absent when the protease dead ADAM13-E/A is used (lane 2). Co-transfection of Fz4-v1 decreases PAPC cleavage by about 50%, whereras Fz4 completely inhibits the cleavage (compare lanes 1, 3 and 4). Neither form inhibits ADAM13 self-shedding. (B) Co-immunoprecipitation of ADAM13 and PAPC. ADAM13 was co-transfected either with PAPC, Fz4-mt or Fz4-v1-mt alone, or in various combinations. ADAM13 was immunoprecipitated with g877 antibody and associated PAPC and Fz4 or Fz4-v1 were detected by western blot. Fz4 and Fz4-v1 do not compete for the binding of PAPC to ADAM13 (compare lanes 1 with 3, 4 and 6).