Structure-function studies of human ciliary neurotrophic factor.
Ciliary neurotrophic factor (CNTF) is a polypeptide that promotes the survival and/or differentiation of a number of neural cell types. Here we present a structural and functional analysis of the human CNTF molecule. Variant proteins were synthesized by Escherichia coli transformed with mutant cDNA constructs, and purified by SDS-polyacrylamide gel electrophoresis and reverse phase high pressure liquid chromatography. Most variant CNTF proteins lacked neurotrophic activity, but two N- and C-terminal deletions (delta 2-14 and delta 173-200, respectively) actually displayed a several-fold increase in specific activity. Loss of biological activity was accompanied by changes in the alpha-helical nature of CNTF as measured by circular dichroism. These data strengthen the proposed similarity between CNTF and the family of hematopoietic cytokines.
Negro
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A
Fidia Research Laboratories, FIDIA S.p.A., Abano Terme, Italy.
Corsa
V
V
Corona
G
G
Grandi
C
C
Skaper
S D
SD
Callegaro
L
L
D000818:Animals; D001681:Biological Assay; D002642:Chick Embryo; D020934:Ciliary Neurotrophic Factor; D006801:Humans; D016296:Mutagenesis; D009414:Nerve Growth Factors / Q000737:chemistry* / Q000494:pharmacology; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000494:pharmacology; D011994:Recombinant Proteins / Q000737:chemistry / Q000494:pharmacology; D013329:Structure-Activity Relationship
D020934:Ciliary Neurotrophic Factor; D009414:Nerve Growth Factors; D009419:Nerve Tissue Proteins; D011994:Recombinant Proteins