Migratory history of the spotted flagtail, <Emphasis Type="Italic">Kuhlia marginata</Emphasis>

The spotted flagtail, Kuhlia marginata (Kuhliidae) is commonly found in streams throughout the Ryukyu Archipelago, including Okinawa Island, Japan. Although it has been suggested that they spawn at sea, little is known about their migratory history. The aim of the study was to clarify their migration history based on otolith microchemistry analysis, size composition and the gonadal development of fish collected from the Genka River on Okinawa Island. All strontium/calcium (Sr/Ca) ratios of otoliths remained high around their cores, and then dropped rapidly at some distance from the core. The estimated standard length corresponding to decreases correlated with the size of new recruits collected in the river (ca. 20 mm in standard length: SL). Multiple increases, the sign for migrations into the high saline area, were recognized intermittently around the otolith margin. As the estimated SL at these increases in the Sr/Ca ratio occurred above the minimum maturation size (female: 95.5 mm SL; male: 83.5 mm SL), such multiple increases in Sr/Ca ratios were caused by spawning migration. Therefore, we conclude that the catadromous pattern of K. marginata is as follows; this species grows in the sea during the early life stage until ca. 20 mm SL and then grow in the freshwater area until maturation, before they migrate again to the sea for spawning. Sr/Ca ratio profiles also suggested that a large number of males did not return to the freshwater area after spawning, whereas females might spawn several times during their lives around the inshore area.     

Gut loading to enhance the nutrient content of insects as food for reptiles: A mathematical approach

A variety of commercially raised insects are fed to insectivorous reptiles, but information concerning appropriate diets used to feed these insects is limited. In the present study, house crickets (Acheta domesticus adults and nymphs), mealworms (Tenebrio molitor larvae), and silkworms (Bombyx mori larvae) were fed diets containing graded levels of calcium (Ca) and/or vitamin A–nutrients that are low or absent in most insects. Diets and insects were analyzed for moisture, Ca, phosphorus (P), and vitamin A. For adult crickets and cricket nymphs, body Ca and vitamin A concentrations increased in a linear fashion with increasing levels of dietary Ca or vitamin A. Ca concentrations of silkworms also increased in a linear fashion with increasing levels of dietary Ca. For mealworms, body Ca and vitamin A concentrations increased in a nonlinear fashion with increasing levels of dietary Ca or vitamin A. These regression equations, in conjunction with insect nutrient composition, allow for the calculation of the optimum nutrient concentration for gut‐loading diets. Final recommendations were based on National Research Council (NRC) requirements for rats, adjustments for the energy content of the insects, and nutrient overages as appropriate. Gut‐loading diets for crickets (adults and nymphs) should be supplemented to contain the following nutrients, respectively: Ca (51 and 32 g/kg), vitamin A (8,310 and 5,270 µg retinol/kg), vitamin D (300 and 190 µg cholecalciferol/kg), vitamin E (140 and 140 mg RRR‐α‐tocopherol/kg), thiamin (31 and 21 mg/kg), and pyridoxine (20 and 10 mg/kg). Gut‐loading diets for mealworms should be supplemented to contain the following nutrients: Ca (90 g/kg), iron (51 mg/kg), manganese (31 mg/kg), vitamin A (13,310 µg retinol/kg), vitamin D (460 µg cholecalciferol/kg), vitamin E (660 mg RRR‐α‐tocopherol/kg), thiamin (5 mg/kg), vitamin B₁₂ (650 µg/kg), and methionine (29 g/kg). Gut‐loading diets for silkworms should be supplemented to contain the following nutrients: Ca (23 g/kg), iodine (0.7 mg/kg), vitamin D (140 µg cholecalciferol/kg), vitamin E (70 mg RRR‐α‐tocopherol/kg), and vitamin B₁₂ (226 µg/kg). Zoo Biol 22:147–162, 2003. © 2003 Wiley‐Liss, Inc.     

Mechano- and pH-sensing convergence on Ca2+-mobilising proteins – A recipe for cancer?

Alterations in the (bio)chemical and physical microenvironment of cells accompany and often promote disease formation and progression. This is particularly well established for solid cancers, which are typically stiffer than the healthy tissue in which they arise, and often display profound acidification of their interstitial fluid. Cell surface receptors can sense changes in the mechanical and (bio)chemical properties of the surrounding extracellular matrix and fluid, and signalling through these receptors is thought to play a key role in disease development and advancement. This review will look at ion channels and G protein coupled receptors that are activated by mechanical cues and extracellular acidosis, and stimulation of which results in increases in intracellular Ca²⁺ concentrations. Cellular Ca²⁺ levels are dysregulated in cancer as well as cancer-associated cells, and mechano- and proton-sensing proteins likely contribute to these aberrant intracellular Ca²⁺ signals, making them attractive targets for therapeutic intervention.     

Ischemia-Induced Translocation of Ca2+/Calmodulin-Dependent Protein Kinase II: Potential Role in Neuronal Damage

The activities of Ca2+/calmodulin (CaM)-dependent, Ca2+/phospholipid-dependent, and cyclic AMP-dependent protein kinases (CaM-KII, PKC, and PKA, respectively) were determined in rat brains after global ischemia. Both CaM-KII and PKC activities were significantly depressed in both hippocampal and cerebral cortical regions of ischemic animals, whereas no change was detected in PKA activity. The loss of CaM-KII activity was more dramatic and more sustained than the loss of PKC activity and correlated with the duration of ischemia. These decreases in enzyme activity were found in both supernatant and pellet fractions from crude homogenates. When the supernatant and pellet were analyzed for the amount of CaM-KII 50-kDa protein, a significant decrease was detected in supernatant fractions that paralleled a gain in the amount of CaM-KII in the pellet. Thus, the loss of CaM-KII activity in the supernatant can be explained by translocation of the enzyme to the pellet. Whether inactivation of CaM-KII occurs during or after the enzyme translocates from the supernatant to the pellet is unknown. Our results indicate that loss in CaM-KII activity parallels neuronal damage associated with ischemia; down-regulation of CaM-KII activity coincided with translocation of the enzyme to the particulate fraction, and it is proposed that this may be, in fact, a mechanism for controlling excessive CaM-KII phosphorylation.     

Regulation of the L-Type Ca2+ Channel Current in Rat Pinealocytes

Abstract : In the present study, the role of phosphoprotein phosphatase in the regulation of L-type Ca²⁺ channel currents in rat pinealocytes was investigated using the whole-cell version of the patch-clamp technique. The effects of three phosphatase inhibitors, calyculin A, tautomycin, and okadaic acid, were compared. Although all three inhibitors were effective in inhibiting the L-type Ca²⁺ channel current, calyculin A was more potent than either tautomycin or okadaic acid, suggesting the involvement of phosphoprotein phosphatase-1. To determine the kinase involved in the regulation of these channels, cells were pretreated with H7 (a nonspecific kinase inhibitor), H89 (a specific inhibitor of cyclic AMP-dependent kinase), KT5823 (a specific inhibitor of cyclic GMP-dependent kinase), or calphostin C (a specific inhibitor of protein kinase C). Pretreatment with either H7 or calphostin C decreased the inhibitory effect of calyculin A on the L-type Ca²⁺ channel current. In contrast, pretreatment with H89 or KT5823 had no effect on the inhibition caused by calyculin A. Based on these observations, we conclude that basal phosphatase activity, probably phosphoprotein phosphatase-1, plays an important role in the regulation of L-type Ca²⁺ channel currents in rat pinealocytes by counteracting protein kinase C-mediated phosphorylation.     

Tunable luminescence and energy transfer in Ca3SiO4Cl2:Ce3+,Li+,Mn2+,Eu2+ phosphors

A series of color‐tunable Ca_{3–2x‐y‐z}SiO₄Cl₂ (CSC):xCe³⁺,xLi⁺,yMn²⁺,zEu²⁺ phosphors with low temperature phase structure was synthesized via the sol–gel method. An energy transfer process from Ce³⁺ to Mn²⁺ in CSC:0.01Ce³⁺,0.01Li⁺,yMn²⁺ (y = 0.03–0.09) and the mechanism was verified to be an electric dipole–dipole interaction. The Ce³⁺ and Mn²⁺ emission intensities were greatly enhanced by co‐doping Eu²⁺ ions into CSC:0.01Ce³⁺,0.01Li⁺,0.07Mn²⁺ phosphors due to competitive energy transfers from Eu²⁺/Ce³⁺ to Mn²⁺, and Ce³⁺ to Eu²⁺. Under 332 nm excitation, CSC:0.01Ce³⁺,0.01Li+,0.07Mn²⁺,zEu²⁺ (z = 0.0005–0.002) exhibited tunable emission colors from green to white with coexisting orange, green and violet‐blue emissions. These phosphors could have potential application in white light‐emitting diodes.     

Interaction between zinc and calcium in skeletal muscle in young growing rats

The purpose of the present study was to determine whether zinc and calcium could interact at the tissue level. In the first part of the study, adult rats were injected with ZnCl₂ dissolved in a physiological saline solution to determine the effects of Zn on Ca levels in various tissues. In the second part of the study, weaned rats (at day 22 postnatally) were fed a diet supplemented with Zn until day 50 and were then sacrificed. In both instances, blood, brain, heart, liver, and skeletal muscle were taken and analyzed. In the Zn-injected group, the brain, heart, and liver showed no interaction between Zn and Ca. The skeletal muscle, in contrast, showed a decrease in Ca in the homogenate, whereas Zn contents showed a significant increase at the sarcoplasmic reticulum (SR). Likewise, in the Zn-supplemented group, the Zn content of the SR vesicle of the skeletal muscle showed an increase, whereas Ca content of the pellet (14,000 g), which contains cell debris, nucleus, mitochondria, and SR vesicles of this group, showed a decrease. Current findings suggest antagonistic effects between Zn and Ca on this tissue. Zn may play a critical role in cellular function through the alteration of itnracellular distribution of Ca in skeletal muscle.     

Adherence of human neutrophils changes Ca signaling during activation with opsonized particles

Changes in the cytosolic free Ca²⁺ concentration ([Ca²⁺]_i) upon activation of human neutrophils by opsonized particles (serum-treated zymosan; STZ) were evaluated by three different methods: (i) measurement of total fluorescence changes in indo-1 loaded neutrophils activated in suspension; (ii) measurement of fluorescence changes in individual indo-1 loaded neutrophils in a flow cytometer and (iii) measurement of fluorescence changes in individual fura-2 loaded neutrophils adherent to serum-coated coverslips. Our study shows that the opsonized particle-induced change in [Ca²⁺]_i in neutrophils is altered during adherence of the cells to a serum-coated surface. These observations might be of importance for neutrophil function in vivo, since adherence is a prerequisite for diapedesis and chemotaxis.     

Generation of inositol phosphates, cytosolic Ca and secretion of noradrenaline in PC12 cells treated with glutamate

Glutamate transiently stimulated rat pheochromocytoma PC12 cells and caused an inositol trisphosphate formation and an increase in levels of Ca⁺ in the cytosol. The rank order of potency of glutamate> N-methyl-D-aspartate (NMDA) > KAINATE = quisqualate is characteristic of an interaction with NMDA receptors. The effect of glutamate on inositol trisphosphate formation disappeared in a low Mg²⁺ buffer and was not blocked by DL-2-amino-5-phosphonovalerate, an antagonist for NMDA receptors coupled to ion channels. Although glutamate failed to stimulate noradrenaline secretion, glutamate enhanced the effect of bradykinin, but not of Ca ionophore A23187, or KC1. These results suggest the existence of metabotropic glutamate receptors, different from previously reported receptors, in PC12 cells.     

Human bone cell cultures: a new model for studying the mechanism of action of calcitonin

An investigation on cell cultures obtained from temporal human bone fragments showed that they provide a suitable model for studying the mechanism involved in calcitonin action on bone cells. Furthermore they demonstrated: a transitory increase in 45Ca uptake that returned to control values ten minutes after the hormone was added; a relation between 45Ca uptake and increased cAMP concentrations when these were measured at the same time intervals; a reproduction of the salmon calcitonin (sCT) effect after incubation of the cultures with either db-cAMP or db-cGMP and inhibition of 45Ca uptake and parallel decrease in cAMP levels with propanol. These results suggest that in human bone cell cultures, sCT acts as a temporary promoter of 45Ca uptake, probably by activating an adenylate-cyclase system through a beta-receptor.