2 edition of Calexcitin B: a new calcium-sensor protein in the nervous system of the squid found in the catalog.
Calexcitin B: a new calcium-sensor protein in the nervous system of the squid
Written in English
Calcium ions (Ca 2+ ) are paramount for cell viability and function. The Ca 2+ signalling pathways utilize specialized proteins, called Ca 2+ binding proteins (CaBPs). Calexcitin (CE) is a CaBP that putatively acts as an intracellular Ca 2+ -mediated messenger. CE is expressed specifically in the nervous system, and may play a critical role in memory. In this work, I elucidated the correct primary structure of CE and characterized its biochemical and biophysical properties. CE can bind three Ca 2+ at affinities similar to other Ca 2+ -sensor proteins. In addition, I have shown that CE is a member of the sarcoplasmic Ca 2+ binding protein (SCP) subfamily of the EF-hand superfamily. Like other SCPs, CE can bind Mg 2+ and has a complex Ca 2+ /Mg 2+ interplay that affects its structure. My studies have identified the physiological role of Mg 2+ binding and has shown that CE is a two domain protein that exists in three distinct conformational states: Apo-CE, has molten-globule characteristics; Mg 2+ -loaded CE possesses one native domain and the other domain is molten-globule like; Ca 2+ -loaded CE has both domains in native configuration. This indicates that under physiological concentrations of Mg 2+ and Ca 2+ , Mg 2+ -CE represents the resting state of the molecule and Ca 2+ -CE is the active state. The backbone nuclei of CE has been assigned by nuclear magnetic resonance and the results show that CE is composed of nine a-helices, eight of which form the four EF-hands and the ninth is near the C-terminus. This result clarified previous discrepancies in the literature regarding the secondary structure of CE and lays the foundation for studying the protein dynamics of CE. Models of CE, based on related proteins, show that, in agreement with biophysical data, CE is composed of two domains that do not interact considerably. Furthermore, in agreement with biophysical data, the model shows a putative recessed hydrophobic pocket that may be involved in target recognition, analogous to other Ca 2+ -sensor proteins. This thesis provides the basis for future investigations into elucidating the precise physiological function of CE. In addition, it enhances our understanding on how CaBPs work and how we can exploit their function for practical neuroprotective applications.
|Statement||by Gombos, Zoltan.|
|The Physical Object|
|Pagination||171 leaves :|
|Number of Pages||171|
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Book 8 Microform 1 Thesis 1 Publication Year. 5 to 3 to Present 1 Author. Nicholls, David G 1 Stanley, P. E.(Philip E.) 1 Bartlett, Roger 1 Laws, Kenneth 1 International Symposium on Bioluminescence and Chemiluminescence(8thCambridge, England).
The endoplasmic reticulum (ER) is the largest single intracellular organelle, which is present in all types of nerve cells. The ER is an interconnected, internally continuous system of tubules and cisterns, which extends from the nuclear envelope to axons and presynaptic terminals, as Cited by: The three-dimensional structure of the neuronal calcium-sensor protein calexcitin from Loligo pealei has been determined by X-ray analysis at a resolution of A.
These findings are consistent with the protein having both a calcium-sensor and calciumbuffering role in neuronal cells. the calexcitin gene from the long-finned squid Loligo pealei were made.
Amajor direction in medical research leading to clinical applications targets the regulation of intracellular calcium and the various human diseases associated with an altered homeostasis of this global second diseases include, for example: cardiomyopathy, inflammation, brain disorders, diabetes and cancer.
In Calcium-Binding Proteins and RAGE:from Structural Basics to. Alix/AIP1 (ALGinteracting protein X/apoptosis-linked geneinteracting protein 1), an adaptor protein that con trols the production of endosomes and trafficking through the endosomal system.
agranular vesicles Synaptic vesicles that do not have a granular appearance in EM; 40–50 nm in diameter, with membrane only 4–5 nm thick. VOCCs are multiple subunit membrane complexes. In the central nervous system, the complexes are comprised of at least α1, α2, and β subunits.
Transcripts encoding a γ subunit have not been identified in RNA from the brain.