Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:Q86TM3 (cage)
 29,987 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The 23 kDa protein was localized by immunocytochemistry to photoreceptor cells of the mouse retina, and bovine and mouse cDNA clones were isolated and sequenced. The deduced amino acid sequences showed that the mouse 23 kDa protein is 91% identical to the bovine protein, and is the same as S-modulin, the CAR (cancer-associated retinopathy) protein and recoverin, the Ca(2+)-dependent activator of photoreceptor guanylate cyclase. The amino acid sequence reveals two Ca2+ binding sites, no internal repeats, 59% homology to the chicken visinin protein and 40% homology to calmodulin while Northern analysis demonstrated a single 1.0 kb mRNA species in bovine and mouse retina.
 ...
PMID:Cloning and sequencing of the 23 kDa mouse photoreceptor cell-specific protein. 138 25

In the present study protein overlays were used to study the molecular interactions of clathrin with clathrin coat-associated proteins. Coated vesicles (CV) were isolated, subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), and transferred to nitrocellulose. The transfers were quenched and equilibrated in buffer, containing 1% Triton X-100. Alpha-Actinin and calmodulin, proteins known to interact with coated vesicles, were iodinated, placed in buffer, and incubated over the transfer for 1 h. After being rinsed extensively, the total amount of 125I associated with the filters was measured, and the filters were then processed for autoradiography. For alpha-actinin, the clathrin heavy chain and a series of lower molecular weight proteins were labeled. The binding of 125I alpha-actinin was inhibited with cold ligand and selectively released from the transfer with a buffer know to strip alpha-actinin from plasma membrane preparations. For 125I calmodulin the predominant binding site was also the clathrin heavy chain. Cold ligand inhibited binding and 60% of the detectable binding were calcium dependent. In addition, when these ligands were used in competition with each other, no significant inhibition was detected in the amount of binding associated with the clathrin heavy chain. These studies show that the clathrin heavy chain is a primary site of the clathrin cage receptive to intracellular interactions and furthermore suggest that the clathrin heavy chain consists of domains of biochemical specificity which may selectively affect the activities of coated vesicles.
 ...
PMID:Evidence for the interaction of alpha-actinin and calmodulin with the clathrin heavy chain. 286 5

Mitotic spindles were isolated from Chinese hamster ovary (CHO) cells and examined morphologically and biochemically. The isolated spindles were observed to be intact structures containing associated chromosomes and were surrounded by a cage of vimentin-containing filaments. Two-dimensional gel electrophoresis of isolated spindles versus whole cell homogenates indicated that isolated spindles were free from significant cytoplasmic contamination and contained tubulin, actin, vimentin and an 80 X 10(3) Mr quadrapeptide as their major protein constituents. Five calmodulin-binding proteins with molecular weights of 200, 160, 130, 60 and 52 (X 10(3] Mr were identified within isolated spindles. These calmodulin-binding proteins may be involved in regulating microtubule organization and depolymerization during karyokinesis.
 ...
PMID:Biochemical characterization of isolated CHO cell mitotic spindles: identification of calmodulin-binding proteins. 331 52

One current hypothesis for the initiation of Ca2+ entry into nonelectrically excitable cells proposes that Ca2+ entry is linked to the state of filling of intracellular Ca2+ stores. In the human T lymphocyte cell line Jurkat, stimulation of the antigen receptor leads to release of Ca2+ from internal stores and influx of extracellular Ca2+. Similarly, treatment of Jurkat cells with the tumor promoter thapsigargin induced release of Ca2+ from internal stores and also resulted in influx of extracellular Ca2+. Initiation of Ca2+ entry by thapsigargin was blocked by chelation of Ca2+ released from the internal storage pool. The Ca2+ entry pathway also could be initiated by an increase in the intracellular concentration of Ca2+ after photolysis of the Ca(2+)-cage, nitr-5. Thus, three separate treatments that caused an increase in the intracellular concentration of Ca2+ initiated Ca2+ influx in Jurkat cells. In all cases, Ca(2+)-initiated Ca2+ influx was blocked by treatment with any of three phenothiazines or W-7, suggesting that it is mediated by calmodulin. These data suggest that release of Ca2+ from internal stores is not linked capacitatively to Ca2+ entry but that initiation is linked instead by Ca2+ itself, perhaps via calmodulin.
 ...
PMID:Increased intracellular Ca2+ induces Ca2+ influx in human T lymphocytes. 844 15

Recoverin is an EF-hand calcium-binding protein reportedly involved in the transduction of light by vertebrate photoreceptor cells. It also is an autoantigen in a cancer-associated degenerative disease of the retina. Measurements by circular dichroism presented here demonstrate that the binding of calcium to recoverin causes large structural changes. increasing the alpha-helical content of the protein and decreasing its beta-turn, beta-sheet and 'other' structures. The maximum helical content (67%) was observed at 100 microM free calcium and, unlike calmodulin, decreased as the calcium concentration was modulated in either direction from this value. Fluorescence measurements indicated that recoverin may aggregate or undergo structural changes independent of calcium binding as the calcium concentration is increased above 100 microM. EGTA also appeared to affect the structure of recoverin independent of its chelation of calcium. While calcium-induced conformational changes have been proposed to alter the membrane binding of recoverin through association of its myristoylated amino terminus, in the experiments presented here the partitioning of recoverin between the cytoplasmic and membrane compartments of the rod photoreceptor outer segment was unaffected by the concentration of calcium, therefore it appears unlikely that a calcium-myristoyl switch acts alone to anchor recoverin directly to the membrane. These experiments were conducted with native recoverin which is heterogeneously acylated, but mass spectrometry confirmed that simple chromatographic methods could be devised to isolate the different forms of recoverin for further studies.
 ...
PMID:Calcium binding to recoverin: implications for secondary structure and membrane association. 939 25

Rats were given repeated infusions of i.v. amphetamine in association with placement in a novel test environment, a protocol that produces behavioral sensitization, or in the home cage, a protocol that fails to induce sensitization. In several brain areas amphetamine altered calmodulin content, but only in the group treated in a novel environment, suggesting that amphetamine-induced alterations in calmodulin may occur only when drug treatments induce behavioral sensitization.
 ...
PMID:The effect of environment on the changes in calmodulin in rat brain produced by repeated amphetamine treatment. 966 66

The effect of exercise on blood pressure in spontaneously hypertensive rats (SHR) was investigated assuming a mechanism involving calcium-dependent dopamine synthesis in the brain. Male SHR (13 weeks of age) were forced to run for 1 h at a speed of 10 m/min using a programmed motor-driven wheel cage. Systolic blood pressure was reduced after running, and this effect of exercise was decreased by prior intracerebroventricular administration of EDTA (1 nmol/rat), alpha-methyltyrosine (inhibitor of tyrosine hydroxylase, 1 mg/rat), sulpiride (D2 receptor antagonist, 50 microg/rat) or eticlopride (D2 receptor antagonist, 100 microg/rat), but was not changed by administration of SCH 23390 (D1 receptor antagonist, 30 microg/rat). Also, the calcium levels in the serum and brain were increased by exercise. Combining these results with our previous reports, it is suggested that exercise leads to an increase in the serum calcium level and subsequently an increase in the brain calcium level. This, in turn, leads to increased brain dopamine synthesis through a calmodulin-dependent system, with the increased dopamine levels inhibiting sympathetic nerve activity via the dopamine D2 receptor in the brain and causing a reduction in blood pressure.
 ...
PMID:Rectifying effect of exercise on hypertension in spontaneously hypertensive rats via a calcium-dependent dopamine synthesizing system in the brain. 1009 21

Current population studies characterize idiopathic scoliosis as a single-gene disorder that follows the patterns of mendelian genetics, including variable penetrance and heterogeneity. The role of melatonin and calmodulin in the development of idiopathic scoliosis is likely secondary, with indirect effects on growth mechanisms. Reported abnormalities of connective tissue, skeletal muscle, platelets, the spinal column, and the rib cage are all thought to be secondary to the deformity itself. Although no consistent neurological abnormalities have been identified in patients with idiopathic scoliosis, it is possible that a defect in processing by the central nervous system affects the growing spine. The true etiology of idiopathic scoliosis remains unknown; however, it appears to be multifactorial.
 ...
PMID:Etiology of idiopathic scoliosis: current trends in research. 1095 7

The effects of a liquid nutritive and tonic drug (NTD) on the neurochemical changes elicited by physical fatigue in mice were investigated in terms of the calcium-dependent dopamine synthesizing function of the brain. In this study, Zena F-III (Taisho Pharmaceutical Co., Ltd., Japan), one of the most popular NTDs in Japan, containing 15 crude drug extracts together with taurine, caffeine, and vitamins, and formulated based on the precepts of traditional Chinese medicine, was used. Male mice were forced to walk for 0-6 h at a speed of 3 m/min using a programmed motor-driven wheel cage. The serum and brain calcium levels in the mice were significantly increased following forced walking. The increase in brain calcium level began later and was more gradual than that in the serum calcium level, and reached its maximum value following forced walking for 3 h. The neostriatal dopamine level was also significantly increased, and locomotor activity significantly decreased following forced walking for 3 h. Prior oral administration of F-III (10 ml/kg) attenuated the increases in the serum and brain calcium levels, the increase in the brain dopamine levels, and the decrease in locomotor activity induced by forced walking. Taking into consideration these findings with our previous reports, it is suggested that physical fatigue leads to an increase in dopamine synthesis in the brain through a calcium/calmodulin-dependent system, thereby inducing behavioral changes, and that F-III inhibits this pathway and may alleviate overwork-induced physical fatigue.
 ...
PMID:Effect of Zena F-III, a liquid nutritive and tonic drug, on the neurochemical changes elicited by physical fatigue in mice. 1097 15

Not much is known about the mobility of synaptic vesicles inside small synapses of the central nervous system, reflecting a lack of methods for visualizing these dynamics. We adapted confocal spot detection with fluctuation analysis to monitor the mobility of fluorescently labeled synaptic vesicles inside individual boutons of cultured hippocampal neurons. Using Monte Carlo simulations we were able to propose a simple quantitative model that can describe vesicle mobility in small hippocampal boutons under resting conditions and different pharmacological treatments. We find that vesicle mobility in a time window of 20 s can be well described by caged diffusion (D approximately 5 x 10(-5) microm(2)/s, cage sizes of approximately 50 nm). Mobility can be upregulated by phosphatase blockage and increased further by actin disruption in a dose-dependent manner. Inhibition of the myosin light chain kinase slows down vesicle mobility 10-fold, whereas other kinases like protein kinase C (PKC), A (PKA), and calmodulin kinase II (caMKII) do not affect mobility in unstimulated boutons.
 ...
PMID:Visualization of synaptic vesicle movement in intact synaptic boutons using fluorescence fluctuation spectroscopy. 1598 Jan 75


1 2 3 Next >>