TY - JOUR
T1 - Characterization of a novel 66 kd subunit of mammalian neurofilaments
AU - Chiu, F. C.
AU - Barnes, E. A.
AU - Das, K.
AU - Haley, J.
AU - Socolow, P.
AU - Macaluso, F. P.
AU - Fant, J.
N1 - Funding Information:
We wish to thank Dr Wrliram T. Norton for his support and advrce on this study. We also thank Drs. Stephen Snyder (University of Tennessee), Cedric Raine, and Irene Ceorgieff for their valuable discussions, Mr. Bill Bear and Dr. James Labdon fortherr assistance in protein sequencrng, Dr. Ken Williams (Yale University) for his heip rn the amino acrd analysis, and Drs. Kay Fields and Ed Masurovsky for gifts of antisera. This work was supported by USPHS grants NS23840 (to F.-C. C.), NS23705, and NS02476 (both to Dr. Norton).
PY - 1989/5
Y1 - 1989/5
N2 - A 66 kd protein, pi 5.4, was purified from the Triton-insoluble fraction of rat spinal cord. This protein formed 10 nm filaments in vitro. The 66 kd protein was unique, although it shared homology with the 70 kd neurofilament protein (NF-L) and vimentin. An antiserum (anti-66) specific to the 66 kd protein did not cross-react with any of the neurofilament triplet proteins. In the spinal cord, anti-66 intensely stained the axons of the anterior and lateral columns. However, afferents from dorsal root ganglia and the efferents from the motoneurons were negative. In the cerebellum, anti-66 intensely stained most axons. The 66 kd protein was readily detectable in homogenates of forebrain, cerebellum, brainstem, and spinal cord, but was found only in trace amounts in adult sciatic nerves and was not found in extraneural tissues. The 66 kd protein constituted 0.5% of total protein in the spinal cord, whereas NF-L constituted about 1.5%.
AB - A 66 kd protein, pi 5.4, was purified from the Triton-insoluble fraction of rat spinal cord. This protein formed 10 nm filaments in vitro. The 66 kd protein was unique, although it shared homology with the 70 kd neurofilament protein (NF-L) and vimentin. An antiserum (anti-66) specific to the 66 kd protein did not cross-react with any of the neurofilament triplet proteins. In the spinal cord, anti-66 intensely stained the axons of the anterior and lateral columns. However, afferents from dorsal root ganglia and the efferents from the motoneurons were negative. In the cerebellum, anti-66 intensely stained most axons. The 66 kd protein was readily detectable in homogenates of forebrain, cerebellum, brainstem, and spinal cord, but was found only in trace amounts in adult sciatic nerves and was not found in extraneural tissues. The 66 kd protein constituted 0.5% of total protein in the spinal cord, whereas NF-L constituted about 1.5%.
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U2 - 10.1016/0896-6273(89)90189-X
DO - 10.1016/0896-6273(89)90189-X
M3 - Article
C2 - 2516728
AN - SCOPUS:0024660341
SN - 0896-6273
VL - 2
SP - 1435
EP - 1445
JO - Neuron
JF - Neuron
IS - 5
ER -