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Structure-function studies of human ciliary neurotrophic factor.

A Negro·V Corsa·G Corona·C Grandi·S D Skaper·L Callegaro
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Abstract

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.

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AnimalsBiological AssayChick EmbryoCiliary Neurotrophic FactorHumansMutagenesisNerve Growth FactorsNerve Tissue ProteinsRecombinant ProteinsStructure-Activity RelationshipJournal Article

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A Negro, V Corsa, G Corona, C Grandi, S D Skaper, L Callegaro. 1994. Structure-function studies of human ciliary neurotrophic factor.. https://doi.org/10.1007/bf00966820

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