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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1996-10-2
|
| pubmed:databankReference | |
| pubmed:abstractText |
We report here the sequences of two new proteins from Aplysia, aplycalcin and Aplysia neurocalcin. These proteins belong to a family of calcium-binding proteins, found primarily in vertebrate brain and retina, that have been proposed to play a role in calcium-dependent regulation of enzymes in signal transduction pathways. Like other members of this family, the Aplysia proteins have consensus sequences for myristoylation, bind calcium, and translocate from cytosol to membrane when the calcium level is raised above the resting intracellular concentration. Both proteins are relatively enriched in Aplysia nervous system, but are also found to a significant degree in other tissues. The expression of mRNA for these proteins in Aplysia nervous tissue is regulated during development, roughly paralleling the reported emergence of several forms of synaptic plasticity. The messages are present at low levels in stage 11, show a large increase by late stage 12, and decline to a plateau of approximately 30% of the peak value afterward. On the basis of the properties of these proteins and by analogy with proposed functions of some of the retinal homologues, we suggest that these proteins may play a role in mediating calcium-dependent processes in neuronal function. The presence of both proteins in other tissues may suggest analogous roles for the proteins in other cell types.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
0022-3042
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
67
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
932-42
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading |
pubmed-meshheading:8752098-Animals,
pubmed-meshheading:8752098-Aplysia,
pubmed-meshheading:8752098-Base Sequence,
pubmed-meshheading:8752098-Blotting, Western,
pubmed-meshheading:8752098-Calcium,
pubmed-meshheading:8752098-Calcium-Binding Proteins,
pubmed-meshheading:8752098-Calmodulin,
pubmed-meshheading:8752098-Cloning, Molecular,
pubmed-meshheading:8752098-DNA, Complementary,
pubmed-meshheading:8752098-Gene Expression Regulation, Developmental,
pubmed-meshheading:8752098-Gene Library,
pubmed-meshheading:8752098-Immunohistochemistry,
pubmed-meshheading:8752098-Membrane Proteins,
pubmed-meshheading:8752098-Molecular Sequence Data,
pubmed-meshheading:8752098-Nervous System,
pubmed-meshheading:8752098-Nervous System Physiological Phenomena,
pubmed-meshheading:8752098-Neurons,
pubmed-meshheading:8752098-RNA, Messenger,
pubmed-meshheading:8752098-Rabbits,
pubmed-meshheading:8752098-Sequence Analysis, DNA,
pubmed-meshheading:8752098-Sequence Homology, Amino Acid
|
| pubmed:year |
1996
|
| pubmed:articleTitle |
Cloning and characterization of aplycalcin and Aplysia neurocalcin, two new members of the calmodulin superfamily of small calcium-binding proteins.
|
| pubmed:affiliation |
Clinical Research Institute of Montreal, Quebec, Canada.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|