In the course of pulse-label studies on the axonal transport of the sm
all, basic, actin-binding proteins - actin depolymerizing factor, cofi
lin and profilin - in chicken motor neurones, we observed a heavily la
belled protein of M-r 18 kDa and pI 8.2 on fluorographs of two-dimensi
onal polyacrylamide gels. On the basis of its M-r, pI and amino acid c
omposition, we tentatively identified it by database searching as cycl
ophilin A and subsequently confirmed its identity by immunostaining. L
ike actin and its associated proteins, cyclophilin A was transported i
n slow component b of axonal transport, but unlike these proteins, cyc
lophilin A did not copurify with actin on DNase I. It was not found am
ongst labelled proteins transported by fast axonal transport. Immunost
aining of chicken dorsal root ganglion cells revealed that it accumula
ted in neurites at points of branching, varicosities and growth cones.
Our results raise the possibility that cyclophilin A is important in
maintaining the native folding of actin and associated proteins during
transit in axons and assembly in growth cones. (C) 1997 Elsevier Scie
nce B.V.