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Interferon research abs 1 || Hemoglobin research abs || Stem cell research abs || Nucleic acid research abs || Herpes research abs || Bronchitis research abs || Schizophrenia research abs || Tuberculosis research abs || Pneumonia research abs || Constipation research abs || Laxative research abs || hair research abs || hair related research references

J Neurosci. 2002 Dec 15;22(24):10533-8.
Elementary properties of axonal calcium currents in type B photoreceptors in Hermissenda crassicornis.

Tamse CT, Yamoah EN.

Center for Neuroscience, Department of Otolaryngology, University of California, Davis, Davis, California 95616, USA.

Axons of the type B photoreceptors form synapses with hair cells and interneurons that are involved in classical conditioning in Hermissenda. We examined the differences in the Ca2+ channels expressed in the soma and axons of the B photoreceptors by direct functional recordings of single-channel currents. Although the soma of the B cells express two Ca2+ current subtypes, a transient BayK 8644-insensitive (approximately 17 pS) current and a sustained BayK 8644-sensitive (approximately 10 pS) current, the axons expressed only the latter. The axonal Ca2+ current activated at potentials positive to -20 mV. Moreover, the Ca2+ channels are distributed heterogeneously along the length of the axon, with the higher channel density (approximately 10-15 channel microm(-2)) occurring at the distal one-third of the isolated axons, with respect to the soma. The regions of Ca2+ channel clusters may represent the presynaptic site of the photoreceptor-interneuron synapses. Furthermore, the high-density clusters of Ca2+ channels may augment postsynaptic responses. The results of the present study represent the first direct recordings of Ca2+ currents at presumed synaptic sites. Expression of different Ca2+ channel subtypes at distinct compartments of the type B photoreceptors may generate diverse Ca2+ domains that may be required for neuronal plasticity in Hermissenda.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12486145&dopt=Abstract

Audiol Neurootol. 2002 May-Jun;7(3):180-4.
Potential role of purinergic signalling in cochlear pathology.

Thorne PR, Munoz DJ, Nikolic P, Mander L, Jagger DJ, Greenwood D, Vlajkovic S, Housley GD.

Discipline of Audiology, University of Auckland, New Zealand. pr.thornuckland.ac.nz

Adenosine triphosphate (ATP) is a major intercellular signalling molecule that is involved in neurotransmission in the central and autonomic nervous systems, regulation of blood flow, and neuroendocrine function. It is also a key signalling molecule involved in normal cochlear homoeostasis, regulating hearing sensitivity, controlling vascular tone and acting as a candidate neurotransmitter at the hair cell afferent synapses. It has also been established that extracellular ATP mediates some pathological processes such as inflammation, apoptosis and cell proliferation. Evidence for a profound influence of extracellular ATP on normal cochlear function offers the tantalizing possibility that extracellular purine nucleotides may play a role in disease processes in the inner ear. This review draws on the current understanding of the pathophysiological role of extracellular ATP in tissues, and the evidence for the functional expression of purinergic signalling elements in the inner ear, to speculate on the potential role of purine nucleotides in cochlear pathology. 2002 S. Karger AG, Basel

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12053142&dopt=Abstract

Acta Otolaryngol. 2002 Jun;122(4):370-3.
Protective effect of basic fibroblast growth factor on auditory hair cells after noise exposure.

Zhai SQ, Cheng JC, Wang JL, Yang WY, Gu R, Jiang SC.

Institute of Otorhinolaryngology, General Hospital of PLA, Beijing, People's Republic of China. zhaislagh.com.cn

The purpose of this study was to observe the protective effects of basic fibroblast growth factor (bFGF) on the cells of the inner ear using in vivo experiments. The studies were carried out using guinea pigs in which bFGF or artificial perilymph was perfused into the cochlea. The compound action potential (CAP) was measured before and after exposure to a sound simulating an explosion. The difference in CAP was significant between the bFGF-perfused group and the control group (p < 0.01, t = 3.896) and between the bFGF-perfused group and the artificial perilymph-perfused group (p < 0.05, t = 2.520). The cochleae were removed and hair cell loss estimated from surface preparations. Acoustic trauma caused loss of outer hair cells in the first and second turns of the cochlea in the bFGF-perfused group and the artificial perilymph-perfused group and partial loss of inner hair cells in the control group. Treatment with bFGF reduced the loss of inner hair cells compared to that of control animals. Our results demonstrate that treatment with bFGF protects the hair cells from acoustic trauma and may facilitate the recovery of hearing.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12125991&dopt=Abstract

J Biol Chem. 2002 Sep 6;277(36):33092-8. Epub 2002 Jun 03.
The crystal structure of metal-free human EF-hand protein S100A3 at 1.7-A resolution.

Fritz G, Mittl PR, Vasak M, Grutter MG, Heizmann CW.

Department of Pediatrics, Division of Clinical Chemistry and Biochemistry, Universitat Zurich, Steinwiesstrasse 75, CH-8032 Zurich, Switzerland. gfritioc.unizh.ch

S100A3 is a unique member of the EF-hand superfamily of Ca(2+)-binding proteins. It binds Ca(2+) with poor affinity (K(d) = 4-35 mm) but Zn(2+) with exceptionally high affinity (K(d) = 4 nm). This high affinity for Zn(2+) is attributed to the unusual high Cys content of S100A3. The protein is highly expressed in fast proliferating hair root cells and astrocytoma pointing toward a function in cell cycle control. We determined the crystal structure of the protein at 1.7 A. The high resolution structure revealed a large distortion of the C-terminal canonical EF-hand, which most likely abolishes Ca(2+) binding. The crystal structure of S100A3 allows the prediction of one putative Zn(2+) binding site in the C terminus of each subunit of S100A3 involving Cys and His residues in the coordination of the metal ion. Zn(2+) binding induces a large conformational change in S100A3 perturbing the hydrophobic interface between two S100A3 subunits, as shown by size exclusion chromatography and CD spectroscopy.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12045193&dopt=Abstract

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