Effect of calcium ions on the interaction of S-100 protein with microtubule proteins.

Fujii, Toshihiro; Gocho, Naoto; Akabane, Yasuhiro; Kondo, Yoshiyuki; Suzuki, Tatsuo; Ohki, Kosuke

doi:10.1248/cpb.34.2261

Cited by 21 publications

(10 citation statements)

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“…Like other heavy metals, zinc can react with thiol and imidazole moieties on enzymes and other proteins (Chvapil et al, 1972). Zinc also binds to S-100 (Baudier and Gerard, 1983) and tubulin (Eagle et al, 19831, and can disrupt microtubule formation (Fujii et al, 1986;Frederickson, 1989). In addition, zinc can act a t many calcium binding sites including calmodulin (Brewer, 1980) and may dis- rupt intracellular calcium homeostasis at micromolar concentrations (Chao et al, 1984).…”

Section: Discussionmentioning

confidence: 99%

Zinc toxicity and induction of the 72 kD heat shock protein in primary astrocyte culture

Swanson

Sharp

1992

Glia

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Zinc is a potent inducer of the 72 kD heat shock protein (HSP72). In brain, pathological conditions such as ischemia and seizures increase extracellular zinc. The present study examines the effect of zinc on HSP72 expression in rat primary cortical astrocyte culture. Astrocytes were grown to confluence and exposed to zinc chloride in CO2-equilibrated Earle's buffered salt solution. Expression of HSP72 was examined using immunocytochemistry. HSP72 was induced with zinc concentrations of 5 to 100 microM after 4 h exposures, or 200 to 300 microM after 15 min exposures. At the lower concentrations expression occurred in small clusters of contiguous cells. At concentrations high enough to cause cell death, HSP72-positive astrocytes formed a continuous margin around patches of dead cells. These patterns of HSP72 expression are similar to the patterns seen after cerebral ischemia in vivo. Exposure to zinc at 100 microM for 4 h or 400 microM for 15 min caused greater than 90% cell death. Increases in extracellular zinc may contribute to HSP72 induction and astrocyte death under ischemia and other pathological conditions in brain.

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Section: Discussionmentioning

confidence: 99%

Zinc toxicity and induction of the 72 kD heat shock protein in primary astrocyte culture

Swanson

Sharp

1992

Glia

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“…It was reported that SlOOb protein induced total disassembly of microtubules in vitro in a Ca2+-and Zn2+-dependent manner (Baudier et al, 1982b;Deinum et al, 1983;Donato et al, 1985) and that S l O O protein regulated microtubule assembly and stability in rat brain extracts (Hesketh & Baudier, 1986). The observation that purifred microtubuleassociated r proteins specifically bound to the S100b-Sepharose column in the presence of Ca2+ or Zn2+ indicated that SlOOb protein may exert its effect on microtubules through the formation of Ca2+-S 1OOb-7 or Zn2+-S 100b-r complexes (Baudier et al, 1987a;Fujii et al, 1986aFujii et al, ,b, 1987Baudier and Cole, unpublished results). Here, we report that the SlOOb /?-subunit and r protein may form covalently bound complexes, thus confirming the interactions between the two proteins ( Figure 4).…”

Section: Ejject Of Calcium and Zinc On The Cross-linking Reactionmentioning

confidence: 93%

Reinvestigation of the sulfhydryl reactivity in bovine brain S100b (.beta..beta.) protein and the microtubule-associated .tau. proteins. Calcium stimulates disulfide cross-linking between S100b .beta.-subunit and the microtubule-associated .tau.(2) protein

Baudier¹,

Cole²

1988

Biochemistry

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Zn2+ and Ca2+ affect the conformation of bovine brain S100b (beta beta) protein and the exposure of its Cys-84 beta. Zn2+ binding to high-affinity sites of native S100b protected the sulfhydryl groups against the thiol-specific reagent 5,5'-dithiobis(2-nitrobenzoate) and antagonized the Ca2+-stimulated reactivity of Cys-84 beta toward the reagent. Spectroscopic studies on the fluorescence properties of labeled S100b with the fluorescent probes bimane and acrylodan at Cys-84 beta confirmed the antagonistic effect of Ca2+ and Zn2+ with respect to the conformational properties of the protein. Measurements of fluorescence dynamics on bimane-labeled S100b indicated that the slow monomer-dimer equilibrium that characterizes the apoprotein at micromolar concentrations was shifted to the monomer form in the presence of Zn2+, a fact that could explain the previously reported Zn2+-dependent increase of S100b protein affinity for calcium. The difference in the effects of Ca2+ and Zn2+ on the reactivity of Cys-84 beta in S100b was confirmed when we observed that Ca2+ and Zn2+ have opposite actions on the formation of disulfide bridges between Cys-84 beta of the S100b beta-subunit and sulfhydryl groups on the microtubule-associated tau(2) protein. Ca2+ stimulated the covalent complex formation whereas Zn2+ inhibited it. We suggest that Zn2+ may have a modulatory function on Cys-84 beta reactivity in the S100b beta-subunit in vivo. Two types of divalent complexes between tau(2) and beta-subunit were formed in the presence of Ca2+, an equimolar complex tau(2)-beta 1 and a complex of one molecule of tau(2) with two beta-subunits, tau(2)-beta 2.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…For example, it is protective and trophic at low concentrations, but toxic and pro-apoptotic at high concentrations. Interestingly, in health, S100β co-localizes and interacts with Tau to promote neurite outgrowth (Baudier et al, 1992; Fujii et al, 1986). However, extracellular S100β is a ligand for the cell-surface receptor for advanced glycation end products (RAGE), which is mainly expressed on the neuronal plasma membrane (Fig.…”

Section: Serological Biomarkers For Brain Injurymentioning

confidence: 99%

Blood biomarkers for brain injury: What are we measuring?

Kawata

Liu

Merkel

et al. 2016

Neuroscience & Biobehavioral Reviews

187

168

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Accurate diagnosis for mild traumatic brain injury (mTBI) remains challenging, as prognosis and return-to-play/work decisions are based largely on patient reports. Numerous investigations have identified and characterized cellular factors in the blood as potential biomarkers for TBI, in the hope that these factors may be used to gauge the severity of brain injury. None of these potential biomarkers have advanced to use in the clinical setting. Some of the most extensively studied blood biomarkers for TBI include S100β, neuron-specific enolase, glial fibrillary acidic protein, and Tau. Understanding the biological function of each of these factors may be imperative to achieve progress in the field. We address the basic question: what are we measuring? This review will discuss blood biomarkers in terms of cellular origin, normal and pathological function, and possible reasons for increased blood levels. Considerations in the selection, evaluation, and validation of potential biomarkers will also be addressed, along with mechanisms that allow brain-derived proteins to enter the bloodstream after TBI. Lastly, we will highlight perspectives and implications for repetitive neurotrauma in the field of blood biomarkers for brain injury.

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Effect of calcium ions on the interaction of S-100 protein with microtubule proteins.

Cited by 21 publications

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Zinc toxicity and induction of the 72 kD heat shock protein in primary astrocyte culture

Zinc toxicity and induction of the 72 kD heat shock protein in primary astrocyte culture

Reinvestigation of the sulfhydryl reactivity in bovine brain S100b (.beta..beta.) protein and the microtubule-associated .tau. proteins. Calcium stimulates disulfide cross-linking between S100b .beta.-subunit and the microtubule-associated .tau.(2) protein

Blood biomarkers for brain injury: What are we measuring?

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