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At least 577 records · Page 32Linked to original sources
PubMed1992

Deduced amino acid sequence and E1-E2 equilibrium of the sarcoplasmic reticulum Ca(2+)-ATPase of frog skeletal muscle. Comparison with the Ca(2+)-ATPase of rabbit fast twitch muscle.

The cDNA encoding a Ca(2+)-transport ATPase of frog (Rana esculenta) skeletal muscle was isolated and characterized. The deduced amino acid sequence, consisting of 994 residues, showed 89% identity to the fast twitch muscle sarcoplasmic reticulum Ca(2+)-ATPases of chicken and rabbit. Northern blot analysis using a fragment of this cDNA as probe detected a 5.0 kb message in frog skeletal muscle but did not detect any mRNA encoding sarcoplasmic reticulum Ca(2+)-ATPase in frog cardiac muscle. The enzymatic properties of the amphibian skeletal muscle Ca(2+)-ATPase were compared with those of the rabbit fast twitch muscle Ca(2+)-ATPase by functional expression of the cDNAs in COS-1 cells. The amphibian Ca(2+)-ATPase displayed a reduced apparent affinity for Ca2+ and an increased apparent affinity for the inhibitors, vanadate and thapsigargin, relative to the mammalian enzyme. This may be explained by a mechanism in which relatively more of the E2 conformation accumulated in the frog Ca(2+)-ATPase than in the mammalian enzyme.

Amino Acid Sequence↗
PubMed1983

In vitro study of frog (Rana ridibunda Pallas) neurointermediate lobe secretion by use of a simplified perifusion system. III. Effect of neuropeptides on alpha-MSH secretion.

It has been previously demonstrated that thyrotropin-releasing hormone (TRH) stimulates in vitro the release of alpha-melanocyte-stimulating hormone (alpha-MSH) in frog. In the present study, the effects of various neuropeptides on spontaneous and/or TRH-induced alpha-MSH secretion were investigated, using a well-defined perifusion system technique. Vasoactive intestinal peptide, (VIP) a neurohormone which stimulates TRH target cells in mammals, was totally devoid of effect on frog melanotrophs although VIP-like material could be detected in neurointermediate lobe extracts. Somatostatin-like immunoreactive material was found in high concentrations in the frog neurointermediate lobe complex, but synthetic somatostatin (from 10(-10) to 10(-6) M) did not modify the spontaneous release of alpha-MSH. At doses of 10(-8) and 10(-6) M, synthetic somatostatin did not modify TRH-induced alpha-MSH secretion. Morphine (10(-5) M) and opioid peptides (10(-10) to 10(-6) M) had no effect on spontaneous alpha-MSH secretion. In addition, methionine enkephalin (10(-5) M) did not modify the stimulatory effect of TRH on alpha-MSH secretion. From these results we conclude that, among the neuropeptides which modulate prolactin secretion in mammals, only TRH is involved in alpha-MSH secretion in the frog.

Animals↗
PubMed1983

Androgen and gonadotropin effects on male mate calls in South African clawed frogs, Xenopus laevis.

Mate calling is a prominent reproductive behavior of male South African clawed frogs. Calls consist of alternating slow- and fast-amplitude-modulated trills. Each trill is made up of a series of clicks. The effects of administration of exogenous gonadotropin and androgen on mate calling were studied in male Xenopus laevis. Males were paired with unreceptive female frogs to elicit maximal calling. The amount of time each animal spent calling during the testing period, the peak fundamental frequency of the calls, the rate of calling, and the interclick interval (ICI, a measure of the temporal patterning of the calls) were measured in intact, castrated, and hormone-replaced frogs. Injection of human chorionic gonadotropin (HCG) into intact frogs increased the amount of time spent calling and the ICI relative to measures taken after water injection. Castrated males did not call even when given HCG. Testosterone and dihydrotestosterone treatment reinstated calling in castrates and increased circulating levels of androgens. When androgen-replaced castrated males were injected with HCG, the amount of time spent calling increased and approached levels of intact, HCG-injected males. The above results suggest that androgens are necessary for the production of calls. Gonadotropins appear to play an important role in mate calling, a role at least partly independent of effects on testicular androgen synthesis.

Androgens↗
PubMed1987

Characterization of steroid receptors in the gut and kidney of the frog (Rana catesbeiana) and in the gut of the turtle (Chrysemys picta).

Paraglucocorticoid- and paramineralocorticoid-binding cytosolic receptors (pGR, pMR) were demonstrated in the intestine and kidney of the frog, Rana catesbeiana and in the intestine of the turtle, Chrysemys picta, in the presence of sodium molybdate. These receptors were of high affinity and low capacity with the following binding parameters: pGR:Kd:frog intestine (FI), triamcinolone acetonide (TA): 3.3 nM, corticosterone (B): 3.4 nM; frog kidney (FK), TA:4.3 nM, B: 9.3 nM; turtle intestine (TI), TA: 4.8 nM; Nmax: FI, TA: 357, B: 371; FK, TA: 301, B: 157; TI, TA: 350 fmol/mg protein. pMR:Kd: FI, aldosterone: 0.9 and 90 nM (biphasic curves); FK, aldosterone: 0.6 and 36 nM (biphasic curves); Nmax: FI, 13 and 147 fmol/mg protein; FK, 78 and 109 fmol/mg protein. The receptor had the following ligand affinities: pGR: FI and FK: triamcinolone acetonide greater than DOC greater than 11 beta-hydroxyprogesterone greater than progesterone greater than corticosterone greater than cortisol greater than aldosterone greater than 11-dehydrocorticosterone greater than 17 alpha-hydroxyprogesterone greater than cortisone; TI: triamcinolone acetonide greater than corticosterone greater than progesterone greater than DOC greater than cortisol greater than aldosterone; pMR: FI and FK: corticosterone greater than 11 beta-hydroxyprogesterone greater than aldosterone greater than triamcinoline acetonide = cortisol greater than DOC greater than 11-dehydrocorticosterone greater than progesterone greater than 17 alpha-hydroxyprogesterone greater than cortisone. Androgens, estrogens or 18-hydroxycorticosterone did not compete for binding in either tissue. The heat activated frog receptors did not bind to naked DNA, though the turtle receptor did. It was possible to show that cytosol receptor-ligand complexes from all tissues were bound by nuclear acceptor sites. On linear sucrose gradients, the FI TA-receptor complex sediments with a single peak (7.5S), the FK TA-receptor complex gave two peaks (8.0 and 4.4S) and the TI TA-receptor complex showed a single peak (9.0S). The hydrodynamic parameters of the pGR's were determined by gel exclusion on Sephacel S-300. The following results were obtained: Mr: FI, 265, 80, 40 kDa (multiple proteins); FK, 280, 60, 20 kDa (multiple proteins); TI, 366 kDa; Rs: FI, 6.9, 3.9 nm; FK, 6.9, 2.9 nm; TI, 7.6 nm; f/f0: FI, 1.6; FK, 1.6; TI, 1.6. It is suggested on the basis of the binding and hydrodynamic parameters that non-mammalian epithelia corticosterone receptors have undergone biochemical evolution from one class of vertebrates to another.

Aldosterone↗
PubMed1988

Changes in immunohistochemical properties of beta-adrenergic receptors in frog erythrocytes by isoproterenol-induced desensitization.

Immunohistochemical properties of beta-adrenergic receptor (BAR) in frog erythrocytes have been studied by using antiserum raised against purified guinea pig BAR. Immunoblotting of frog erythrocyte membranes with the anti-BAR serum revealed prominent staining of a protein with Mr of 65,000-67,000. BARs present in intact frog erythrocytes were made visible by incubation with the anti-BAR serum and then goat-anti rabbit IgG conjugated with colloidal gold. About 50-60% of the cells showed small, punctate dots by staining with the anti-BAR serum. After 4 hr exposure of the cells to isoproterenol, the density of the staining was markedly increased. Labeling of BAR after permeabilization of erythrocytes with saponin was markedly enhanced in isoproterenol-desensitized, but not in control cells. The BARs present in cytoslic fraction of desensitized cells migrated in the void volume of Sepharose-4B and were effectively labeled by a lipophilic BAR ligand capable of penetrating the cell membranes, but not by a hydrophilic ligand. Thus, isoproterenol-induced desensitization is associated with alteration of the immunoreactivity of BAR. Moreover, our immunochemical and biochemical data provide further evidence for the internalization of BAR in desensitized frog erythrocytes.

Animals↗
PubMed1989

Effects of oxymorphazone in frogs: long lasting antinociception in vivo, and apparently irreversible binding in vitro.

Oxymorphazone (at doses of 50-200 mg/kg) was found to be a relatively weak antinociceptive drug in intact frog (Rana esculenta) when acetic acid was used as pain stimulus. Frogs remained analgesic for at least 48 hrs following oxymorphazone (200 mg/kg) administration. The ligand increased the latency of wiping reflex in spinal frogs too. These effects were blocked by naloxone. In equilibrium binding studies (3H)oxymorphazone had high affinity to the opioid receptors of frog brain and spinal cord as well (apparent Kd values were 8.9 and 10.6 nM, respectively). Kinetic experiments show that only 25% of the bound (3H)oxymorphazone is readily dissociable. Preincubation of the membranes with labeled oxymorphazone results in a washing resistant inhibition of the opioid binding sites. At least 70% of the (3H)oxymorphazone specific binding is apparently irreversible after reaction at 5 nM ligand concentration, and this can be enhanced by a higher concentration of tritiated ligand.

Analgesics↗
PubMed1989

Melanin concentrating hormone. V. Isolation and characterization of alpha-melanocyte-stimulating hormone from frog pituitary glands.

The structure of alpha-melanocyte-stimulating hormone (alpha-MSH) has been determined in the pars intermedia of the frog Rana ridibunda. Pulse-chase labeling of frog neurointermediate lobes with selective amino acids revealed that the composition of frog alpha-MSH is similar to that of alpha-MSH from all mammalian species yet studied. Tryptic mapping of nexly synthetized alpha-MSH generated two fragments with the following amino acid composition: (T1) Trp, Pro, Lys, Gly, Val and (T2) Tyr, Arg, Phe, His, Ser, Glu. Concurrently, alpha-MSH was purified from 100 neurointermediate lobes to apparent homogeneity by reverse-phase HPLC. The sequence of the peptide determined by automated Edman degradation was Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val. The structure of frog alpha-MSH is thus identical to mammalian des-N alpha-acetyl alpha-MSH and differs from the sequence of toad (Xenopus laevis) alpha-MSH only by the first residue (Ser instead of Ala). These results confirm that the sequence of alpha-MSH has been highly preserved during evolution.

Amino Acid Sequence↗
PubMed1984

Occurrence of the "capillary contractility" phenomenon and its significance in the distribution of microvascular flow in frog skeletal muscle.

The phenomenon of "capillary contractility" was first described more than 100 years ago. Recent reports on this phenomenon in the frog mesentery have been based on the observation of dramatic reductions of luminal diameter and blood flow during electrical stimulation of the capillary wall. The aim of this study was to establish the presence and the occurrence of this phenomenon in the frog sartorius muscle and to evaluate its contribution to the distribution of flow. Eight 1.3 X 1.7-mm areas of the muscle surface in eight anesthetized frogs were visualized by means of a microscope and also video-recorded during stimulation experiments. Microelectrodes and semitransparent surface electrodes introduced constant currents (0.1 to 1.0 microA) or pulse trains (5-msec pulse width, 1 to 64 Hz frequency, -0.2 to -5.4 V amplitude) either to individual capillaries or to whole populations of capillaries situated in these areas. Caution was exercised that stimuli did not cause muscle twitching. Red cell velocity in capillaries was measured from video recordings by the flying spot technique. Microelectrode stimulations caused flow stoppages in 4 out of 60 individual stimulated capillaries. Surface electrode stimulations had practically no effect on the mean red cell velocity in any of these populations but an appreciable effect on individual velocities in 7.5% of all capillaries in these populations. It is concluded that the phenomenon of electrically induced reductions of flow exists in the frog sartorius muscle, but it is scarce. It seems unlikely, therefore, that it represents a major mechanism of flow distribution in this tissue.

Acetylcholine↗
PubMed1975

Biological activity of some steroidal compounds in the adult and larval frogs.

Four steroids were tested for their biological activity, using the sex-steroid-dependent redevelopment of the secondary sex characteristics in adult frogs and gonadal sex differentiation in larval frogs as end points. In adult frogs, 19-norprogesterone and 6-chloro-17alpha-hydroxy-4, 6-pregnadiene-3,20-dione had antiandrogenic and antiestrogenic effects. 2alpha, 17alpha-Dimethyl-DHT and 2alpha-methyl-DHT were potent androgens and effective antiestrogens. In the larval frogs, all four compounds had a masculinizing effect upon the undifferentiated gonads.

Animals↗
PubMed1994

An uptake system for dietary alkaloids in poison frogs (Dendrobatidae).

The skin of poison frogs (Dendrobatidae) contains a wide variety of alkaloids that presumably serve a defensive role. These alkaloids persist for years in captivity, but are not present in captive-raised frogs. Alkaloids fed to poison frogs (Dendrobates, Phyllobates, Epipedobates) are readily accumulated into skin, where they remain for months. The process can be selective; an ant indolizidine is accumulated, while an ant pyrrolidine is not. Frogs (Colostethus) of the same family, which do not normally contain alkaloids, do not accumulate alkaloids. Such an alkaloid uptake system provides a means of maintaining skin alkaloids and suggests that some if not all such 'dendrobatid alkaloids' may have a dietary origin.

Alkaloids↗
PubMed1982

Local stimulation induces shedding throughout the frog retina.

Our previous work has demonstrated that rod shedding in the frog retina can be driven by environmental cues such as light onset. Although shedding normally occurs binocularly, we found that shedding could be initiated independently in either eye of the frog by monocular stimulation. Further, rod shedding occurs in vitro in the isolated eyecup under appropriate incubation conditions when provided with a light stimulus following a dark incubation period. Thus, the control mechanism for light induced rod shedding in the frog seems to be located within the eye, and does not seem to be systemically or centrally located. However, the exact link between light onset and shedding of the distal rod tips remains unknown. To elucidate further the control site for initiation of rod shedding, we used a variety of stimulus conditions, including front and rear screens as well as spots and slits projected directly on the retina, to stimulate a small portion of the frog retina with a range of light intensities and stimulus paradigms. In all cases where shedding occurred, it was uniform throughout the retina. Thus, it appears that the light-cued message received by a small population of photoreceptors is sufficient to initiate shedding throughout the retina. These results differ significantly from those found by Easter and Macy for light-induced photomechanical movements, which were found to be locally controlled.

Animals↗
PubMed1983

A comparison of spatio-temporal receptive fields of ganglion cells in the retinas of the tadpole and adult frog.

Receptive fields formed by ganglion cells were measured simultaneously in time and space in the adult and tadpole retinas. The spatio-temporal receptive-fields (STRFs) were measured by cross-correlating the spatio-temporal white-noise stimulus with the cells' spike discharges. Crosscorrelation was made photographically to extract the first order STRF kernel (approximately linear component of the STRFs). The time-course of STRF formed by the frog ganglion cells was twice as fast as that of the tadpole cells. The STRF formed by the tadpole ganglion cells was either a center-brightening or a center-dimming type whereas in the frog there was another class of cells which produced either complex STRFs or did not show any linear component in their STRFs. Size of the STRFs in frog and tadpole was similar in both frog and tadpole retinas.

Action Potentials↗
PubMed1983

Utilization of exogenous retinol by frog pigment epithelium.

High-performance liquid chromatography was used to investigate the utilization of exogenous 11,12-3H2-retinol by frog pigment epithelium (RPE) in vitro or after intraocular injection into the dark-adapted, whole animal. Isolated frog RPE contains an adequate supply of acyl donors and can esterify all-trans, 11-cis and 13-cis isomers of retinol. The esterifying activity is restricted to the particulate fraction. Homogenates of choroid cannot esterify retinol. The ester formed by the RPE is primarily palmitate, and is therefore identical with the endogenous retinyl ester. Frog RPE also formed 13-cis retinyl palmitate from all-trans retinol, probably by esterification of 13-cis retinol formed non-enzymatically from the all-trans isomer. None of the in vitro experiments provided any evidence for the formation of 11-cis retinoid. There was slow appearance of label in 11-cis retinyl palmitate when 3H-all-trans retinol was injected intraocularly into the intact frog. After 15 hr its specific activity was only 20% of that of the all-trans retinyl palmitate. This rate of formation of 11-cis retinoid is inadequate for rhodopsin regeneration. However, it is more than an order of magnitude too fast to be accounted for by phagocytosis of rhodopsin. It is suggested that 11-cis retinoid is generated in the retina and is slowly transferred to the site of esterification in the RPE.

Animals↗
PubMed1995

Distinct hydro-osmotic receptors for the neurohypophysial peptides vasotocin and hydrins in the frog Rana esculenta.

The biological properties of vasotocin, hydrin 1 (vasotocinyl-Gly-Lys-Arg) and hydrin 2 (vasotocinyl-Gly), in particular the hydro-osmotic activities on the frog skin, the frog urinary bladder and the frog kidney, have been compared. Hydrins are as active or more active than vasotocin on the first two organs but they are virtually devoid of antidiuretic activity in the rat and the frog, in contrast to vasotocin. It appears that where the oxytocin ring (residues 1-6), present in the three peptides, is necessary for the action on the three organs, the C-terminal amidated group of vasotocin is necessary for the renal receptor but not for the skin and bladder receptors. It is known that amphibians have two types of vasotocin receptors, V1 and V2, homologous to the vascular/hepatic V1 and the renal V2 vasopressin receptors of mammals, respectively. We suggest that adaptation has led to specialization of (at least) two subtypes of hydro-osmotic V2 receptors, the renal subtype on which vasotocin is mainly active for the reabsorption of tubular water, and the skin/bladder subtype on which hydrin 2 is specifically involved in ensuring the rehydration of the animal. Cooperative evolution might have created in anuran Amphibia, on the one hand, two hydro-osmotic peptides, vasotocin and hydrin 2, derived from a single precursor through differential processing; and on the other hand, two corresponding receptors in kidney and skin for internal and external water recovery.

Amino Acid Sequence↗
PubMed1992

Isolation and structural characterization of peptides related to alpha- and gamma-melanocyte-stimulating hormone (MSH) from the frog brain.

Peptides that are derived from the processing of proopiomelanocortin were isolated in pure form from the brain of the frog Rana ridibunda. The primary structure of the most abundant of those peptides was established as: Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val. This amino acid sequence is identical to that of mammalian and frog pituitary alpha-melanocyte-stimulating hormone (MSH) and the peptide co-eluted with synthetic desacetyl alpha-MSH, indicating that it is COOH-terminally alpha-amidated. A second component, which exhibited a shorter retention time, co-eluted with the glycine-extended form of desacetyl alpha-MSH [ACTH(1-14)]. The primary structure of the third peptide isolated in pure form from the brain extract was established as: Lys-Tyr-Val-Met-Ser-His-Phe-Arg-Trp-Asn-Lys-Phe-NH2. This sequence corresponds to Lys-gamma 1-MSH as predicted from the nucleotide sequence of frog proopiomelanocortin. The presence of substantial amounts of desacetyl alpha-MSH and Lys-gamma 1-MSH in the frog brain supports the concept that, in amphibia, melanotropins may act as neurotransmitters and/or neuromodulators as well as hormonal peptides.

Amino Acid Sequence↗
PubMedDate not supplied

Two chemically and immunologically distinct forms of luteinizing hormone-releasing hormone are differentially expressed in frog neural tissues.

Immunoreactive luteinizing hormone-releasing hormone (IR-LRF) has been measured in several neural tissues of the frog Rana catesbeiana and characterized by bioassay, chromatography and immunological analysis. Frog brain contains the mammalian form of LRF (mLRF), whereas, sympathetic ganglia and adrenal glands contain a form of LRF (pLRF) chromatographically and immunologically similar to the IR-LRF found in the central nervous systems of several piscine species. Frog retina contains both mLRF and pLRF, in a ratio of about 1:2. The two forms of LRF are apparently equipotent in their ability to release LH from rat gonadotrophs in vitro. Immunological analysis of the pLRF found in the frog nervous system suggests that it is a decapeptide, like mLRF, with one or more amino acid substitutions in the mLRF molecule.

Adrenal Glands↗
PubMedDate not supplied

Localization and identification of neuropeptide Y (NPY)-like immunoreactivity in the frog brain.

The distribution of neuropeptide Y (NPY) in the central nervous system of the frog Rana ridibunda was determined by immunofluorescence using a highly specific antiserum. NPY-like containing perikarya were localized in the infundibulum, mainly in the ventral and dorsal nuclei of the infundibulum, in the preoptic nucleus, in the posterocentral nucleus of the thalamus, in the anteroventral nucleus of the mesencephalic tegmentum, in the part posterior to the torus semicircularis, and in the mesencephalic cerebellar nucleus. Numerous perikarya were also distributed in all cerebral cortex. Important tracts of immunoreactive fibers were found in the infundibulum, in the preoptic area, in the lateral amygdala, in the habenular region, and in the tectum. The cerebral cortex was also densely innervated by NPY-like immunoreactive fibers. A rich network of fibers was observed in the median eminence coursing towards the pituitary stalk. Scattered fibers were found in all other parts of the brain except in the cerebellum, the nucleus isthmi and the torus semicircularis, where no immunoreactivity could be detected. NPY-immunoreactive fibers were observed at all levels of the spinal cord, with particularly distinct plexus around the ependymal canal and in the distal region of the dorsal horn. At the electron microscope level, NPY containing perikarya and fibers were visualized in the ventral nuclei of the infundibulum, using the peroxidase-antiperoxidase and the immunogold techniques. NPY-like material was stored in dense core vesicles of 100 nm in diameter. A sensitive and specific radioimmunoassay was developed. The detection limit of the assay was 20 fmole/tube. The standard curves of synthetic NPY and the dilution curves for acetic acid extracts of cerebral cortex, infundibulum, preoptic region, and mesencephalon plus thalamus were strictly parallel. The NPY concentrations measured in these regions were (pmole/mg proteins) 163 +/- 8, 233 +/- 16, 151 +/- 12 and 60 +/- 13, respectively. NPY was not detectable in cerebellar extracts. After Sephadex G-50 gel filtration of acetic acid extracts from whole frog brain, NPY-like immunoreactivity eluted in a single peak. Reverse phase high performance liquid chromatography (HPLC) and radioimmunoassay were used to characterize NPY-like peptides in the frog brain. HPLC analysis revealed that infundibulum, preoptic area and telencephalon extracts contained a major peptide bearing NPY-like immunoreactivity. The retention times of frog NPY and synthetic porcine NPY were markedly different. HPLC analysis revealed also the existence, in brain extracts, of several other minor components cross-reacting with NPY antibodies.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗
PubMed1983

Heart lesions in the frog at high environmental temperature.

Frogs (R. pipiens) adapted to 12 degrees C were exposed to increased environmental temperature during 2 hr. At 33 degrees C gross heart lesions started to appear in a few cases and at 37 degrees C, 71% of the frogs showed ventricular aneurysms and some died. Critical thermal maximum (CTM) was around 37 degrees C in autumn, winter and early spring, whereas in late spring and summer CTM was at 39 degrees C and during these last-mentioned periods of the year gross heart lesions at high temperature did not start until at 37 degrees C. After 2 hr at 37 and 39 degrees C respectively, ECG-abnormalities occurred indicating myocardial injury. Isolated strips of the heart ventricle from frogs with gross heart lesions showed a deteriorated resistance towards cyanide anoxia as measured by an isometric procedure. The ultrastructure was deranged by the high temperature, the changes mainly involving the mitochondria and the myofibrils. These alterations were focal but depletion of glycogen particles was diffuse. As the high temperature induced changes similar to those provoked by catecholamines, propranolol was given in some frogs before the heat exposure. This beta-adrenoceptor blockade did only reduce some of the abnormal changes by 37 degrees C.

Animals↗