Premium
Caldesmon and low Mr isoform of tropomyosin are localized in neuronal growth cones
Author(s) -
Kira M.,
Tanaka J.,
Sobue Kenji
Publication year - 1995
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.490400303
Subject(s) - caldesmon , tropomyosin , growth cone , gene isoform , actin , myosin , calmodulin , microbiology and biotechnology , biology , microfilament , biochemistry , cytoskeleton , cell , gene , axon , enzyme
Neuronal growth cones move actively, accompanying changes in intracellular Ca 2+ concentration. The movement of growth cones may partly depend on the actomyosin system, considering the presence of actin and myosin II. Yet, Ca 2+ ‐sensitive regulatory proteins for the actomyosin system have not been identified in growth cones. In the present study, caldesmon, an inhibitory protein on actin‐myosin interaction, was detected in the growth cone fraction isolated from embryonic rat brain, using immunoblotting with the antibody to chicken gizzard caldesmon. Morphological evidence of caldesmon in growth cones of cultured rat neurons was obtained using the indirect immunofluorescence method. Since inhibition of caldesmon on actin‐myosin interaction can be overcome by calmodulin and Ca 2+ , caldesmon may be involved in the Ca 2+ ‐dependent regulation in growth cone motility. Tropomyosin is another member of the actomyosin system whose function may be regulated by caldesmon in smooth and nonmuscle cells. A low Mr isoform of tropomyosin was distributed in the growth cone fraction. Using specific antibodies against tropomyosin isoforms, we further clarified morphologically that the low Mr isoform was localized in growth cones, but not the high Mr isoform. High Mr isoforms of tropomyosin were present in nonneuronal cells. Actin filaments in growth cones may be unstable, since low Mr tropomyosin binds to actin filaments with a lower affinity than high Mr isoforms. The instability of actin filaments may be suitable for the rapid movement and shape changes of growth cones. © 1995 Wiley‐Liss, Inc.