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At least 19 recordsLinked to original sources
PubMed1986

The structure of the carapace and plastron of juvenile turtles, Chelonia mydas (the green turtle) and Caretta caretta (the loggerhead turtle).

Consistent with their primary function as a protective covering, the carapace and plastron are heavily keratinised. In both species, the carapace is heavily pigmented and during the development and translocation of basal cells from the germinal layer of the epidermis, pigment granules migrate towards the surface layers. The epidermis is generally 2-4 cells thick; however at the growing points it can attain 6 cell layers. The epidermis is much thicker over the plastron of the loggerhead turtle. The ultrastructure of the epidermal cells supports the observation that the keratin scales are of the hard variety and the microfolds which characterise the scutes covering the carapace are discussed in relation to the lowering of frictional drag in water.

Animals↗
PubMed1985

Turtle-associated salmonellosis in Puerto Rico. Hazards of the global turtle trade.

After the Puerto Rico Department of Health received a report of salmonellosis in an infant who had contact with a pet turtle, we conducted a case-control study in two urban areas in Puerto Rico to measure the extent of pet turtle-associated salmonellosis there. Ten (17%) of 60 infants with salmonellosis but none of their matched controls had a history of exposure to a pet turtle in the two weeks before onset of illness. Two other case patients were also exposed to a pet turtle--an 8-year-old child and an adult with acquired immunodeficiency syndrome and Salmonella bacteremia. A variety of Salmonella serogroups were represented in the turtle-associated cases. All turtle lots collected from pet shops in Puerto Rico were culture-positive for Salmonella; 89% yielded Salmonella pomona. Contamination of the turtles probably occurred at the farm before distribution, since S pomona was also isolated from turtles exported from the same farm to Guam and to Yugoslavia. The estimated 3 to 4 million turtles exported annually from the United States are an important potential route for global dissemination of human salmonellosis.

Adult↗
PubMed1986

Kinetic studies on turtle pancreatic ribonuclease: a comparative study of the base specificities of the B2 and P0 sites of bovine pancreatic ribonuclease A and turtle pancreatic ribonuclease.

Kinetic constants for the transesterification of eight dinucleoside phosphates CpX and UpX by bovine and turtle pancreatic ribonuclease were determined. Both ribonucleases have a preference for purine nucleotides at the position X. However, bovine ribonuclease, like other mammalian ribonucleases, prefers 6-amino bases at this site, while turtle ribonuclease prefers 6-keto bases. This difference in specificity at the B2 site may be explained by the substitution of glutamic acid at position 111 by valine in turtle ribonuclease. These results have been confirmed by inhibition studies with the four nucleoside triphosphates. Inhibition studies with pT and pTp showed that a cationic binding group (P0) for the 5'-phosphate of the pyrimidine nucleotides bound at the primary B1 site is present in turtle ribonuclease, although lysine at position 66 in bovine ribonuclease is absent in turtle ribonuclease. However, the side chain of lysine 122 in turtle ribonuclease is probably located in the correct position to take over the role as cationic P0 site.

Animals↗
PubMed1987

Acquisition of Salmonella flora by turtle hatchlings on commercial turtle farms.

A commercial turtle pond in South Louisiana was studied to identify the mechanism by which turtle hatchlings acquire Salmonella flora. The visceral organs and mature eggs removed from 31 adult gravid female turtles over the course of two egg-laying seasons and from 37 adult females during one winter dormant period were examined bacteriologically for Salmonella. Pond water, egg nest soil, and hatchlings produced by eggs removed from the oviducts and nest soil were also tested. Eighty-eight turtles hatched from eggs removed from the oviducts of 15 turtles at necropsy did not excrete or harbor systemically Salmonella, nor were these pathogens isolated from ovarian tissue or immature eggs. The findings suggest transovarian transmission of these pathogens does not occur frequently. Turtles hatched from eggs retrieved from soil nests 1 to 2 h after deposition harbor and excrete these organisms. This result coupled with the isolation of these pathogens from the cloaca, colon contents, and bursal fluid from 18 females captured in the act of egg laying supports the cloaca to egg and nest soil to egg mode for salmonellae infection in the resultant hatchling. Salmonella arizonae and Salmonella serogroups B, C2, and E1 were isolated from the cloaca, colon contents, pond water, and nest soil, and were excreted by hatchlings produced from eggs removed from the soil nests. These same serogroups were isolated from the colon contents of 19 of 37 females tested during the dormant period, suggesting the salmonellae persist in the pond environment in the adult throughout the year.

Animals↗
PubMed1985

Prolonged diving and recovery in the freshwater turtle, Pseudemys scripta--IV. Effects of profound acidosis on O2 consumption in turtle vs rat (mammalian) brain and heart slices.

The oxygen consumption of rat versus turtle brain and heart slices was compared as a function of extracellular pH and temperature. At pH = 6.20 rat (mammalian) brain and heart slices show a significant depression of oxygen consumption as compared to pH = 7.50 at temperatures of both 24 degrees and 37 degrees C. In the turtle oxygen consumption in brain and heart slices was not depressed at pH = 6.20 compared to pH = 7.50 at 24 degrees C and brain oxygen consumption was not significantly different at the two pH values at 37 degrees C. Turtle heart QO2 was depressed at 37 degrees C. The results suggest that extracellular acidosis depresses mitochondrial O2 uptake in mammalian brain and heart, playing a role in the bioenergetic manifestations of O2 depletion. Turtle brain mitochondria do not show a depression of QO2 at the acidotic pH. The resistance to acidosis of turtle brain mitochondria presumably enhances the possibility of survival following prolonged diving by maintaining ATP generation during the early diving period and during recovery.

Acidosis↗
PubMed1985

Isolation and properties of sea turtle (Chelonia mydas) pituitary prolactin.

Sea turtle prolactin (PRL) was isolated in a highly purified state from sea turtle pituitary side fractions obtained from other studies and some of its biological, chemical, and immunological properties were determined. Sea turtle PRL is a protein of 22-24 kDa [sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis]. Its sole amino terminal amino acid residue is leucine. The amino acid composition of sea turtle PRL is similar to ovine PRL and is characterized by a high content of aspartic acid (20 residues), glutamic acid (34 residues), serine (19 residues), and leucine (24 residues). It possess three disulfide bonds and 2 tryptophan residues which is also characteristic of many species of PRL. As with PRLs of other species, it displayed multiple stained bands in disc gel electrophoresis, at pH 8.3. Biologically, sea turtle PRL was active in pigeon crop-sac assay but the dose-response characteristics were nonparallel when compared to ovine PRL. An antiserum against sea turtle PRL was raised in rabbit and a homologous radioimmunoassay was developed with a sensitivity of 2.8 ng for sea turtle PRL. Sea turtle gonadotropins did not cross-react, but sea turtle growth hormone showed a 5% cross-reactivity. Pituitary extracts from other species of turtles displayed parallel inhibition curves to the sea turtle PRL. Extracts and prolactin preparations from several birds, snakes, alligator, and marsupials cross-reacted, but in a nonparallel fashion. Bullfrog pituitary extract and Tilapia PRL showed no cross-reaction at high doses. Several purified mammalian PRLs (pig, sheep, human, horse, dog) showed minimal or no ability to cross-react in the RIA.

Amino Acids↗
PubMed1988

In vivo environmental temperature and the in vitro pattern of luminal acidification in turtle bladders. Evidence for HCO3 ion reabsorption.

In this study, it is shown how to transfer tared aliquots of (HCO3 + CO2)-containing luminal fluids directly into the mercury-sealed chamber of a modified Van Slyke apparatus and how to obtain direct as well as indirect manometric determinations of dissolved CO2 ([CO2]f) in each aliquot of such fluids. It is next shown that the pattern of in vitro luminal acidification in an isolated turtle bladder sac depends upon the prior in vivo ambient temperature to which the donor turtle had become adapted. Under in vivo conditions, the food intake, physical activity, and acid excretion of 32 degrees C-adapted turtles are greater than those of 21 degrees C or 26 degrees C-adapted turtles. Under in vitro conditions of incubating isolated bladder sacs (from 21, 26, and 32 degrees C turtles) in (HCO3 + CO2)-containing Ringer media at a single temperature (21 degrees C), the patterns of luminal acidification are as follows: (a) The rate of depletion of luminal [HCO3] is greatest in bladders from the 32 degrees C-adapted turtles. (b) Concomitant decreases in luminal [CO2]f, [HCO3], and pH (the 'CO2-decreasing patterns' of luminal acidification) develop in all bladders from 32 degrees C turtles, in half of those from 26 degrees C turtles, but in less than one-fifth of those from 21 degrees C-adapted turtles: and (c) a CO2-increasing pattern of luminal acidification is found in most of the bladders from 21 degrees C-adapted turtles. A postulated bicarbonate ion-reabsorbing pump is consistent with all of these patterns of luminal acidification.

Absorption↗
PubMed1989

Relationship between energy expenditure and ion channel density in the turtle and rat brain.

Synaptosomes were isolated from turtle and rat brains to determine whether differences in brain ion channel densities accounted for the turtle's ability to survive anoxia compared with the mammal. The Na(+)-channel binding neurotoxin brevetoxin showed high-affinity specific binding in both turtle and rat synaptosomes, suggesting specific ligand-receptor interaction. The maximum binding capacity (Bmax) value for the turtle was only about one-third of that found for the rat synaptosomes, suggesting that the turtle synaptosome has a correspondingly lower Na+ channel density than the rat. This apparent difference in Na+ channel density is not reflected in metabolic rates, since at the same temperature (31 degrees C) the O2 consumption of both the rat and turtle synaptosome was almost identical. The large reductions in energy expenditure seen in synaptosomes incubated in Na(+)-free media and in media containing ouabain (approximately 50% turtle, 80% rat) are probably related to the halting of transmembrane Na(+)-K+ exchange. The greater reduction in the rat may be related to the apparent greater density of Na+ channels in the rat brain. However, compared with the 90% reduction in brain metabolism that occurs when the turtle brain becomes anoxic, the differences in ion channel density and in the costs of ion pumping between the rat and turtle brain are trivial. Closing Na+ channels with tetrodotoxin and increasing Na+ channel activation with veratridine caused substantial decreases and increases in synaptosome energy consumption, respectively. This suggests that the modulation of ion channel conductance has a significant effect on metabolic cost and may be an important mechanism to reduce energy consumption and electrical activity in the anoxic turtle brain, while still maintaining ionic gradients.

Animals↗
PubMed1988

Spermiogenesis in the red-ear turtle (Pseudemys scripta) and the domestic fowl (Gallus domesticus): a study of cytoplasmic events including cell volume changes and cytoplasmic elimination.

Nuclear and cytoplasmic volume changes as well as the elimination of residual spermatid cytoplasm were investigated in the red-ear turtle (Pseudemys scripta) and the rooster (Gallus domesticus). Nuclei of newly formed spermatids which were originally centrally located became eccentrically located within the cell in both species. Shortly thereafter the nuclear pole of the spermatid was found situated within deep crypts of a Sertoli cell. The cytoplasm of elongating spermatids was displaced along the nonacrosomal region of the nucleus and the proximal flagellum. In both species sheetlike Sertoli cell processes indented spermatid cytoplasm adjacent to the nucleus and appeared to segregate small packets of the cytoplasm. In the turtle, these packets of cytoplasm were separated from the spermatid. In both the turtle and rooster, a portion of the spermatid cytoplasm was displaced forward over the acrosomal region of the spermatid to resemble a hood. As spermatids were transported to the seminiferous tubular lumen, cytoplasmic lobes which projected forward of the spermatid head were formed by preferential flow of cytoplasm into one aspect of the cytoplasmic hood. In both species, at sperm release the cytoplasmic lobe was disengaged from the spermatid head to form a large residual body that was internalized and degraded within the Sertoli cell. Medium-sized cytoplasmic lobes were pinched from the head and neck region of the turtle and rooster spermatids, respectively. In the turtle, small-sized mitochondrial-rich cytoplasmic fragments budded from the caudal head and midpiece of the spermatids and were phagocytosed by the Sertoli cell. Thus, cytoplasmic elimination occurred through 1) segregation of cytoplasmic packets by Sertoli penetrating processes (turtle), 2) elimination of large and medium-sized residual bodies from the head (turtle and bird), and 3) budding of small mitochondrial-rich cytoplasmic fragments from the region of the midpiece (turtle). In the turtle a 79% reduction in total cell volume occurred during spermiogenesis which was the result of an 84% cytoplasmic reduction and a 78% nuclear reduction. During spermiogenesis, the rooster lost 97% of its total cell volume due to a 97% cytoplasmic volume change and a 96% nuclear volume change.

Animals↗
PubMed1979

Bioenergetic pattern of turtle brain and resistance to profound loss of mitochondrial ATP generation.

The adaptations in the freshwater turtle that permit survival despite prolonged loss of mitochondrial ATP generation were investigated by comparing the bioenergetics of turtle brain slices with rat brain slices. Aerobic turtle brain shows no significant difference in basal levels of total ATP generation compared to rat brain; levels in turtle brain and rat brain were 18.4 +/- 2.8 (SD) and 19.4 +/- 2.2 mumol (100 mg of tissue)-1 hr-1, respectively. However, in turtle brain, a significantly greater fraction of ATP is derived from glycolysis both under aerobic and anaerobic conditions [aerobic turtle (24%) and rat (13%), P less than 0.02; anaerobic, turtle (28%) and rat (18%), P less than 0.05]. The increased glycolytic capacity is related to high levels of rate-limiting glycolytic enzymes, such as pyruvate kinase (EC 2.7.1.40). Turtle brain operates close to glycolytic capacity even under aerobic conditions, and no Pasteur effect can be demonstrated. Quantitatively, anaerobic glycolysis accounts for a maximum of 28% of basal aerobic ATP generation, suggesting that prolonged diving is also accompanied by a reduction in brain energy requirements. The adaptation subserving short-term (natural) diving is an increase in brain glycolytic capacity. The adaptation subserving prolonged diving (days to weeks) may be a reduction in the energy requirements of brain (and other cells).

Animals↗
PubMed1987

Adaptation to metabolic acidosis by turtle urinary bladder.

We utilized the turtle urinary bladder to study the mechanisms responsible for adaptation to metabolic acidosis. Bladders removed from acidotic turtles had a higher rate of H+ secretion in vitro than bladders from control turtles, despite identical extracellular pH. HCO3 secretion, however, was not different between the two groups. The increase in H+ secretion could be mediated by a decrease in intracellular pH and/or by an increase in the number of cells thought to be responsible for H+ secretion. To study this issue, we measured intracellular pH with the fluorescent dye 6-carboxyfluorescein diacetate and quantified the number of cells by fluorescence microscopy utilizing acridine orange, rhodamine 123, and 6-carboxyfluorescein diacetate in turtles receiving different acid loads. Urinary acidification measured in vivo was increased in turtles fed a low-acid load for 48 h and in turtles fed a high-acid load for 24-48 h. Intracellular pH was lower in bladders from turtles fed a high-acid load for 48 h but it was not different from controls in the other groups, indicating that intracellular pH cannot account for the adaptive increase in H+ secretion. Bladders from all groups fed an acid load had a higher number of cells with positive staining for acridine orange compared with controls. Double labeling with acridine orange and the mitochondrial stain rhodamine 123 or 6-carboxyfluorescein showed a significant increase in the number of mitochondria-rich cells between control and bladders from turtles fed an acid load. The increase in the number of rhodamine 123- or 6-carboxyfluorescein-positive cells was lower than the increase in acridine orange-positive cells, suggesting that the apparent increase in the number of acridine orange-positive cells is due to an increase in the number of acidic vesicles in the mitochondria-rich cells and in the granular cells rather than solely to an increase in the number of mitochondria-rich cells. Plasma membrane fraction prepared from control and acidotic bladders failed to disclose an increase in the putative H+-ATPase as assessed by enzymatic activity and transport studies. In conclusion, the present study suggests that the adaptive increase in H+ secretion in metabolic acidosis is associated both with an increase in the number of mitochondria-rich cells as well as with an increase in the number of acidic vesicles in these cells.

Acidosis↗
PubMed1978

Effect of dry versus wet bowl environment on pet turtles.

Recently hatched, certified Salmonella-free, red-eared slider turtles (Pseudemys scripta elegans) were obtained from a commercial breeder. Half of the turtles were kept in a traditional wet-bowl environment, whereas the other half lived in individual dry-bowl environments, except for 30 minutes each day when they were immersed in water and were fed. Both groups were fed commercial turtle food. During the 26 weeks of the study, individual weight and general observations were recorded for each turtle. Neither Salmonella nor Arizona bacteria were recovered from the turtles, their food, or their bowen environments. Histologic observations were completed on organs of both groups. Turtles maintained in the dry-bowl environment ate poorly, were considerably less active and less developed histologically, and lost significantly more weight than those turtles living in the wet bowl environment. Neither the environment nor the feeding program were found to be satisfactory for prolonged household maintenance of pet turtles.

Animals↗
PubMed1986

Monoclonal antibodies to the turtle cortex reveal neuronal subsets, antigenic cross-reactivity with the mammalian neocortex, and forebrain structures sharing a pallial derivation.

The dorsal cortex of the pond turtle (Pseudemys scripta) is a relatively simple structure consisting of two principal classes of neurons that occupy three distinct layers. Morphological, pharmacological, and physiological data suggest many similarities to the mammalian neocortex, rendering it an interesting preparation for comparative studies. We prepared monoclonal antibodies to the turtle dorsal cortex by immunizing mice with cortical tissue from adult turtles. Twelve antibodies were generated that recognize specific components of the turtle cortex. Among these, eight antibodies label only neurons and four label only ependymal glial cells. Differences in tissue staining pattern and immunoglobulin class suggest a heterogeneity of antigenic specificity among the antibodies. The staining patterns of three of our antibodies are described. TC3, like all other neuron-marking antibodies generated, labels a subset of both pyramidal and stellate cell types. It also cross-reacts with a subset of mammalian cortical neurons and labels them with a pattern similar to that observed in the turtle cortex. TC5 stains ependymal cells and their glial processes in the turtle cortex, and cross-reacts with fibrous astrocytelike processes in mammalian neocortical white matter. TC9 appears to recognize antigens of neurons sharing a pallial derivation in turtle.

Animals↗
PubMed1987

Immunohistochemical and biochemical studies on Lys8-Asn9-neurotensin8-13 (LANT6)-related peptides in the basal ganglia of pigeons, turtles, and hamsters.

The distribution of the neurotensin-related hexapeptide LANT6 within the basal ganglia and its projection targets was studied in turtles, pigeons, and hamsters by using immunohistochemical techniques, radioimmunoassay (RIA), gel chromatography, and high performance liquid chromatography (HPLC). The results in turtles and pigeons were fundamentally similar. Within the basal ganglia, LANT6-like immunoreactivity (LLI) was observed in a population of large striatal neurons (comprising 1-5% of the total number of striatal neurons) and in essentially all of the medium-large pallidal neurons. In addition, LLI was observed in neurons of such other "striatal" and "pallidal" cell groups as the olfactory tubercle and ventral pallidum, respectively. Within the dopaminergic cell fields of the tegmentum, to which the pallidal cell groups project, LLI-containing fibers were abundant. Knife-cut studies confirmed that the majority of these LLI-containing fibers arise from telencephalic levels. Biochemical studies with RIA and HPLC showed large amounts of immunoreactive LANT6 (iLANT6) in the basal telencephalon (477 pmol/g) and tegmentum of pigeons (259 pmol/g), and this material was indistinguishable from the synthetic peptide. Lower levels of iLANT6 were demonstrated in the basal telencephalon (82 pmol/g) and tegmentum (156 pmol/g) of turtles, and the majority of this activity appeared to be associated with larger molecular forms of LANT6 or a peptide related to LANT6. In addition, one or more substances resembling Neuromedin N (NMN), a mammalian counterpart to LANT6, were detected in the turtle nervous system. The labeling patterns in hamsters were similar to those in pigeons and turtles, except that in hamsters fewer neurons were labeled and the labeling was generally lighter. The lighter level of labeling may reflect a difference between the LANT6-like material present in hamster nervous system and authentic LANT6. Biochemical studies revealed that a Neuromedin N-like substance, as well as high molecular weight forms of a LANT6-like substance, are present in hamster brain. In hamsters, neurons within globus pallidus, the entopeduncular nucleus, the ventral pallidum, and the polymorph layer of the olfactory tubercle were labeled for the presence of LANT6. Fiber labeling for LANT6 in the dopaminergic tegmental cell groups that receive pallidal input was, however, light. Thus, the present results establish that LANT6 in pigeons and LANT6-related peptides in turtles and hamsters are present within many pallidal neurons. In pigeons and turtles, these pallidal neurons give rise to a major LLI-containing projection to the dopaminergic cell groups of the tegmentum.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗
PubMed1991

Major differences in CNS sulfonylurea receptor distribution between the rat (newborn, adult) and turtle.

Our previous results have shown that KATP channels play an important role in K+ efflux and extracellular K+ accumulation in the rat brain, and this role was quantitatively more important in the adult than in the newborn brain. The purpose of this study was to localize by autoradiographic techniques the binding sites of glibenclamide, a potent sulfonylurea ligand that targets KATP channels, in the adult and newborn rat central nervous system (CNS). Since the adult turtle is resistant to anoxia, we also compared the rat to the turtle brain sulfonylurea receptor distribution. In all three animal groups (newborn rat, adult rat, adult turtle), specific glibenclamide binding was saturable. Scatchard plots were curvilinear in the rat, thus suggesting that glibenclamide binds to two types of sites, i.e., high and low affinity sites. Scatchard analysis on turtle brain tissue showed evidence of one binding site only. We also found that the distribution of glibenclamide binding sites was heterogeneous in the adult rat CNS with a higher density in rostral than in caudal regions. The highest binding densities were seen in the cortex, hippocampus, cerebellum, substantia nigra, and a few thalamic nuclei; intermediate densities were observed in the basal ganglia, septum, thalamus, and the hypoglossal nucleus. There was a low density in most areas of the hypothalamus, midbrain, brainstem, and spinal cord. Compared with the adult rat, the newborn had a very homogeneous distribution of binding sites and densities were very low throughout the CNS; the level of binding density was even lower in some regions undetectable in the adult turtle. Our results indicate that (1) there are high and low affinity sulfonylurea receptors in the rat CNS, (2) there is a striking heterogeneity in the distribution and density of sulfonylurea receptors in the adult rat CNS and this is in sharp contrast to the homogeneous distribution and low density in both newborn rat and adult turtle; (3) sulfonylurea receptors increase in number postnatally in the rat since binding density increases and the Kd in the newborn rat is similar to that in the adult rat. We speculate that KATP channels and sulfonylurea receptors are poorly developed in the turtle and develop mostly after birth in the rat, reaching highest density in adulthood.

ATP-Binding Cassette Transporters↗
PubMed1988

Measurement of plasma renin activity in the freshwater turtle.

Components of the renin angiotensin system have been identified in many nonmammalian vertebrates. However, in many of these animals, including reptiles, the physiological functions and importance of the system remain unclear. To aid in the study of the system in a reptile we modified a commercially available radioimmunoassay (RIA) kit containing antibody against human angiotensin I (ANG I) for use in the freshwater turtle, Pseudemys scripta. Cross-reactivity between anti-human ANG I antibodies (Rainen Angiotensin I RIA Kit, New England Nuclear) and turtle ANG I was demonstrated. Cross-reactivity with the antibody in two other human ANG I assay kits (Travenol-Genentech and Biotecx) was very limited. Blood for assay was collected from conscious turtles in EDTA, centrifuged, and the plasma frozen at -20 degrees. Turtle ANG I was generated by incubation at 0.5 ml plasma at pH 5.5 for 2 hr at 30 degrees with addition of dimercaprol and 8-hydroxyquinoline. Angiotensin generation increased with temperature and with generation time. The recovery of turtle ANG I added to turtle plasma prior to incubation was 92-97%. The assay procedure was used to measure plasma renin activity (ng/ml/hr incubation) from unstimulated turtles.

Angiotensin I↗