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环磷酸腺苷刺激的分离神经微管亚基的磷酸化作用

Cyclic adenosine 3':5'-monophosphate-stimulated phosphorylation of isolated neurotubule subunits.

作者信息

Goodman D B, Rasmussen H, DiBella F, Guthrow C E

出版信息

Proc Natl Acad Sci U S A. 1970 Oct;67(2):652-9. doi: 10.1073/pnas.67.2.652.

DOI:10.1073/pnas.67.2.652
PMID:4331718
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC283255/
Abstract

The possible relationship between cyclic adenosine 3':5'-monophosphate (cAMP) and neurotubules in synaptic transmission has been explored. The neurotubular subunit protein from bovine cerebral cortex has been prepared. The addition of cAMP to this preparation in the presence of ATP stimulates the phosphorylation of serine residue(s) in the principal component of the preparation. The neurotubule subunit thus serves as a substrate for an intrinsic, cyclic nucleotide-dependent protein kinase closely associated with the neurotubule subunit. The significance of this finding is discussed in terms of a general model for cellular secretion involving microtubules, cyclic AMP, protein kinase, and calcium ion.

摘要

已经探讨了环磷酸腺苷（cAMP）与神经微管在突触传递中的可能关系。制备了来自牛大脑皮质的神经微管亚基蛋白。在ATP存在的情况下，向该制剂中添加cAMP可刺激制剂主要成分中丝氨酸残基的磷酸化。因此，神经微管亚基可作为与神经微管亚基紧密相关的内在环核苷酸依赖性蛋白激酶的底物。根据涉及微管、环磷酸腺苷、蛋白激酶和钙离子的细胞分泌通用模型，讨论了这一发现的意义。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/adea/283255/5dc26863121a/pnas00100-0181-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/adea/283255/5dc26863121a/pnas00100-0181-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/adea/283255/5dc26863121a/pnas00100-0181-a.jpg

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