Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “CAMELS”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,783 records · Page 99Linked to original sources

Chloroplast DNA phylogeography of the argan tree of Morocco.

Polymorphisms in the chloroplast genome of the argan tree (Sapotaceae), an endemic species of south-western Morocco, have been detected by restriction site studies of PCR-amplified fragments. A total of 12 chloroplast DNA (cpDNA) and two mitochondrial DNA (mtDNA) fragments were amplified and digested with a single restriction enzyme (HinfI). Polymorphisms were identified in six of the cpDNA fragments, whereas no mtDNA polymorphisms were detected in a survey of 95 individuals from 19 populations encompassing most of the natural range of the species. The cpDNA polymorphisms allowed the identification of 11 haplotypes. Two lineages, one in the south-east and the other in the north-west, divide the range of the argan tree into two distinct areas. The level of genetic differentiation measured at the haplotype level (GSTc = 0.60) (i.e. with unordered haplotypes) was smaller than when phylogenetic relationships were taken into account (NSTc = 0.71-0.74) (ordered haplotypes), indicating that population history must be considered in the study of the geographical distribution of cpDNA lineages in this species. If contrasted with the level of nuclear genetic differentiation measured in a previous study with isozymes (GSTn = 0.25), the results indicate a relatively high level of gene flow by seeds, or conversely a relatively low level of gene flow by pollen, as compared with other tree species. Goats and camels could have played an important role in disseminating the fruits of this tree.

DNA, Chloroplast↗

Structural tolerance of bacterial autotransporters for folded passenger protein domains.

In this report we investigate the capacity of bacterial autotransporters (AT) to translocate folded protein domains across the outer membrane (OM). Polypeptides belonging to the AT family contain a C-terminal domain that supports the secretion of the N-domain (the passenger) across the OM of Gram-negative bacteria. Despite some controversial data, it has been widely accepted that N-passenger domains of AT must be unfolded and devoid of disulphide bonds for efficient translocation. To address whether or not AT are able to translocate folded protein domains across the OM, we employed several types of recombinant antibodies as heterologous N-passengers of the transporter C-domain of IgA protease (C-IgAP) of Neisseria gonorroheae. The N-domains used were single chain Fv fragments (scFv) and variable mono-domains derived from camel antibodies (V(HH)) selected on the basis of their distinct and defined folding properties (i.e. enhanced solubility, stability and presence or not of disulphide bonds). Expression of these hybrids in Escherichia coli shows that stable scFv and V(HH) domains are efficiently (>99%) translocated towards the bacterial surface regardless of the presence or not of disulphide bonds on their structure. Antigen-binding assays demonstrate that surface-exposed scFv and V(HH) domains are correctly folded and thus able to bind their cognate antigens. Expression of scFv- or V(HH)-C-IgAP hybrids in E. coli dsbA or fkpA mutant cells reveals that these periplasmic protein chaperones fold these N-domains before their translocation across the OM. Furthermore, large N-passengers composed of strings of V(HH) domains were secreted in a folded state by AT with no loss of efficacy (>99%) despite having multiple disulphide bonds. Thus AT can efficiently translocate toward the cell surface folded N-passengers composed of one, two or three immunoglobulin (Ig) domains, each with a folded diameter between approximately 2 nm and having disulphide bonds. This tolerance for folded protein domains of approximately 2 nm fits with the diameter of the central hydrophilic channel proposed for the ring-like oligomeric complex assembled by C-IgAP in the OM.

Antigen-Antibody Reactions↗

Secretion of proteins with dimerization capacity by the haemolysin type I transport system of Escherichia coli.

The tolerance of the haemolysin transport system (Hly) for exporting dimeric protein substrates to the supernatants of Escherichia coli cultures was examined. A strong dimerization domain (i.e. an amphipathic alpha-helix capable of forming a leucine zipper in the yeast transcription factor GCN4) was inserted into an epitope-tagged version of the 23 kDa C-terminal secretion signal of haemolysin (EHlyA). The zipper-containing polypeptide (ZEHlyA) was effectively secreted by E. coli cells carrying the HlyBD transporter and accumulated in the culture media as a stable dimer as determined by gel filtration chromatography. In vivo protein cross-linking experiments and coexpression with a secretion-deficient derivative of ZEHlyA indicated that leucine zipper-dependent dimerization occurs following secretion. To test whether dimerization allows the correct folding of the secreted polypeptide, immunoglobulin V(HH)-domains obtained from camel antibodies were fused to EHlyA and ZEHlyA. Functional dimerization of the ZEHlyA hybrid was anticipated to increase the apparent binding affinity (i.e. avidity) of the V(HH) moiety, thus becoming an excellent reporter of correct protein folding and dimerization. Both V(HH)-EHlyA and V(HH)-ZEHlyA hybrids were quantitatively secreted and found in the extracellular medium as active monomers and dimers respectively. When compared with their monomeric counterparts, the dimeric V(HH)-ZEHlyA molecules showed superior binding properties to their cognate antigen, with a 10-fold increase in their avidity. These data reveal a non-anticipated permissiveness of the Hly type I transport machinery for the secretion of substrates with dimerization capacity.

Amino Acid Sequence↗

The purification of peptides by partition chromatography based on a hydrophobicity scale.

A study of the efficiency of partition chromatography for the purification of peptides as a function of structure has been undertaken. A series of 19 omission analogs of camel beta-endorphin and of some of its partial sequences have been synthesized with each analog missing only a single amino acid. Their chromatographic properties have been examined with use of the Martin hypothesis and the RM concept, and a hydrophobicity scale for the amino acid side chains was obtained. To a first approximation a correlation with the Tanford hydrophobicity scale for amino acids was found. A decrease in hydrophobicity has been observed with increasing chain length and is discussed in terms of column efficiencies required for the purification of synthetic peptides.

Amino Acid Sequence↗

beta-Endorphin: isolation, amino acid sequence and synthesis of the hormone from horse pituitary glands.

Beta-endorphin has been isolated from equine pituitaries. Its amino acid sequence is identical to that of ovine, bovine and camel beta-endorphins except for substitution of the threonine residue at position 6 by serine. The equine beta-endorphin has also been synthesized by the solid-phase method. In comparison with the human hormone, equine beta-endorphin was shown to possess 3 times the receptor-binding activity in rat membrane preparations and 1.6 times the analgesic potency in the mouse tail-flick assay.

Amino Acid Sequence↗

beta-Endorphin: analgesic and receptor binding activity of non-mammalian homologs.

Analgesic potencies of turkey, ostrich and des-acetyl salmon beta-endorphins have been measured in the tail-flick test and binding affinities determined by radio-receptor assay. The duration of analgesia and the slope of the dose-response curves generated by these peptides are similar to those elicited by mammalian beta-endorphins. This suggests that they act in vivo and in vitro on the same population of opiate receptors. The ratio of binding to analgesic potencies observed for these peptides varies nearly sixfold. Structure-activity analysis suggests that a basic side-chain at position 9 is required in order to produce a high opiate activity both in vivo and in vitro. A reexamination of the biological activities of camel beta-endorphin shows that the analgesic potency and binding affinity of this peptide are respectively 171 and 2.7 times higher than human beta-endorphin. His-27 and/or Gln-31 may contribute to this increased potency. The dissociation of radioreceptor binding affinity from analgesic potency in these naturally occurring beta-endorphin homologs suggests that either the conditions under which the binding assay is performed mask the true binding potency in the brain or that, once bound to the appropriate receptor, these homologs do not possess equal ability to produce biological effects.

Amino Acid Sequence↗

Human retinoblastomas have binding sites for the COOH-terminal segment of human beta-endorphin.

Two human retinoblastoma cell lines (Y79 and McA) were evaluated for the presence of binding sites for human beta-endorphin (beta h-EP). Using tritiated beta h-EP (3H-beta h-EP) and synthetic beta-EP analogues, it was possible to demonstrate binding sites for 3H-beta h-EP with an ED50 of 3.5 nM in Y79 cells and 8 nM in McA cells respectively. The non-opioid segment [beta h-EP-(6-31)] retained about 20% relative potency in Y79 and 40% in McA in displacing the tritiated hormone when compared with beta h-EP. Camel beta-EP had a relative potency of less than 1% and beta h-EP-(1-27) was inactive in both cells in doses as high as 4 microM. Taken together with previous reports on similar binding sites in human neuroblastoma and glioblastoma cell lines, it appears that cell lines of neural origin have binding sites for the COOH-terminal of human beta-EP.

Cell Line↗

Beta-endorphin. Biological activity of analogs containing dermorphin and dynorphin sequences: ileum and vas deferens assays.

Biological activity of synthetic beta-endorphin (beta-EP) analogs containing dermorphin or dynorphin-A-(1-13) structure has been investigated using the guinea pig ileum and the vas deferens of the mouse, rat and rabbit. Replacement of NH2-terminal 1-7 segment of camel beta-EP [beta c-EP-(1-7)] with dermorphin caused a great increase in opiate potency of the analog. [Dermorphin (1-7)]-beta c-EP was 120 times more potent than beta c-EP in the guinea pig ileum assay, 49 times more potent in the mouse vas deferens assay; and only 4 times more potent in the rat vas deferens assay. Replacement of NH2-terminal 1-13 segment of human beta-EP [beta h-EP-(1-13)] with dynorphin-A-(1-13) caused an increase in opiate potency in both the guinea pig ileum and rabbit vas deferens assays, a complete loss of potency in the rat vas deferens assay, and no change in the mouse vas deferens assay. In comparison with dynorphin-A-(1-13), the hybrid peptide was less potent in the guinea pig ileum assay as well as in mouse and rabbit vas deferens assay. It is suggested that beta c-EP-(8-31) facilitates the dermorphin moiety to act on opiate mu and delta receptors but not on the epsilon receptor, while beta h-(14-31) reduces the action of dynorphin on mu, delta and kappa receptors.

Amino Acid Sequence↗

Beta-endorphin: peripheral opioid activity of homologues from six species.

The peripheral opioid activity of six homologous beta-endorphins (beta-EPs) were assayed on the guinea pig ileum and the vas deferens of the mouse, the rat and the rabbit. In the guinea pig ileum assay, human beta-EP (beta h-EP) was less potent than camel, turkey, and ostrich beta-EPs, of the same potency as equine beta-EP and more active than des-acetyl salmon beta-EP. In the rat vas deferens, mammalian beta-EPs showed higher activity than those from the bird and the fish, whereas in the mouse vas deferens assay, beta h-EP is more active than those from other species. In the rabbit vas deferens, however, all homologous beta-EPs show very weak activity. The relative potency of beta-EP homologues obtained from rat vas deferens assay is in good correlation with the analgesic potency, while the receptor binding activity does not correlate with any of the four bioassays, but appears to be related to the charge properties of the peptides.

Amino Acid Sequence↗

Endogenous nitric oxide in the airways of different animal species.

BACKGROUND: High amounts of endogenous nitric oxide (NO) have been demonstrated in the human upper airway, but the role of nasal NO is still unclear. The present study aims to describe nasal NO excretion in different animal species with special living conditions or anatomy. METHODS: Domestic animals (horse, cow, pig, sheep, dog, cat) and zoo-animals (Rhesus monkey, chimpanzee, gorilla, elephant, fur seal, alpaca, yak, dolphin, camel, capybara, bear, tiger, wolf, giraffe, alligator, Harris' hawk, kangaroo) were studied awake, resting or anaesthetised. NO concentrations were measured by chemiluminescence using different analysers and techniques, including measurements on mixed exhaled air, during continuous or intermittent gas sampling, and on single breaths. RESULTS: Rhesus monkeys (number of individuals N = 5) and pigs (N = 2) were compared and displayed quite different excretion patterns. Allowing NO to accumulate in the nose during timed occlusions yielded peak concentrations in monkeys of 0.46 +/- 0.07 parts per million (ppm, mean +/- SEM), 0.59 +/- 0.08 ppm, 0.70 +/- 0.08 ppm and 1.02 +/- 0.05 ppm NO after 15, 30, 60 and 120 s of occlusion. In pigs, 0.012-0.021 ppm NO were recorded, independent of occlusion time. The chimpanzee was similar to the Rhesus monkey and the highest NO value, 2.9 ppm, was recorded after 4-5 min of occlusion. In single breaths from 3 elephants 0.031-0.082 ppm, from 1 gorilla 0.029 ppm, and from 1 chimpanzee 0.069 +/- 0.003 ppm NO (8 observations) were recorded. CONCLUSIONS: We found considerable species difference in nasal NO excretion with pronounced amounts only in primates and elephants. The physiological implications of these findings remain to be defined.

Animals↗

The poll glands of the dromedary (Camelus dromedarius): ultrastructural characteristics.

The poll glands of the camel are tubuloalveolar glands. They consist of lobules separated by interlobular connective tissue. Adrenergic axons and blood vessels including fenestrated capillaries are present in the intralobular connective tissue in close proximity to the secretory cells. The prominent features of the secretory cell cytoplasm are many mitochondria, smooth endoplasmic reticulum, and many vesicles in various secretory stages. It is concluded that the secretory cells have apocrine as well as merocrine modes of secretion. The glands may have the ability to uptake hormones and concentrate them. Additional work is needed before considering these glands as steroid-secreting glands.

Animals↗

The ultrastructure of cells and cell fragments in mammary secretions of Camelus bactrianus.

The fine structure of leucocytes from the udders of 7 lactating and 3 non-lactating bactrian camels and from peripheral blood were studied. The most important finding was the presence of large numbers of cell fragments in milk. The cell fragments were bounded by a plasma membrane, had no nuclei and contained mitochondria and abundant rough endoplasmic reticulum (RER). Macrophages were the dominant cells recovered from milk and udder washings during the dry period. Neutrophils and lymphocytes were also present. The dominating leucocytes in blood were neutrophils, followed by lymphocytes, eosinophils, monocytes and basophils.

Animals↗

Phycomycosis of the abomasum in Camelus dromedarius.

Two cases of phycomycosis of the abomasum in dromedary camels are described. In one of the cases there is evidence of spread to the liver. The pathology and pathogenesis of the disease are discussed. We believe this is the first report of phycomycosis in Camelidae.

Abomasum↗

In Vitro and in vivo developmental competence of dromedary (Camelus dromedarius) embryos produced in vitro using two culture systems (mKSOMaa and oviductal cells).

Development competence and pregnancy rate of in vitro-produced (IVP) dromedary embryos were studied in two culture systems: (i) semi-defined modified medium (mKSOMaa) and (ii) co-culture using camel epithelial oviducal cells. Five hundred and three cumulus-oocytes complexes (COCs) were selected, allowed to mature, fertilized and cultured in vitro (38.5 degrees C; 5% CO2, maximum humidity > 95%, with concentration of oxygen of 5% for semi-defined medium and 20% for co-culture cells). Maturation was accomplished by incubation in TCM-199 medium supplemented with 10% heat-treated foetal calf serum (FCS), 10 ng/ml epidermal growth factor, 1 microg/ml follicle-stimulating hormone, 1 microg/ml oestradiol and 500 microM cysteamine for 30 h. In vitro fertilization (IVF) was performed using fresh semen (0.5 x 10(6) spermatozoa/ml in modified TALP solution). Fertilized COCs were denuded by vortexing, then cultured in either mKSOMaa (10% heat-treated FCS was added 24 h post-IVF), under 5% O2 and 90% N2 (group 1; n = 249) or with dromedary epithelial oviducal cell monolayers in TCM-199 with 10% heat-treated FCS under 20% O2 (group 2; n = 254). The rate of cleavage was significant higher (p < 0.05) for group 1 (63%, 156/249) than for group 2 (51%, 130/254). No significant difference was found between the two groups in the rate of development to blastocyst (21% vs 16.5%) and their hatchability (21% vs 14%). Pregnancy rates were similar for the first 60 days. However, all pregnancies were lost after 60 days with the exception of two of six (33%) from recipients of hatched blastocysts from group 1. We conclude that both systems support in vitro production of dromedary embryos by in vitro maturation (IVM)/IVF of oocytes. However, embryos obtained by culture in the semi-defined medium (mKSOMaa) appear to have a better in vivo development ability.

Animals↗

Evidence for the neurotrophic regulation of collagen-tailed acetylcholinesterase in immature skeletal muscle by beta-endorphin.

Acetylcholinesterase (AChE) was extracted in a high-saline medium from gastrocnemius muscles of rat embryos and young rats aged 14 days' gestation to 40 days post partum. The molecular forms of the enzyme were separated by low-salt precipitation, followed by velocity sedimentation. During gestation, all molecular forms increased in activity, particularly the 16 S (A12) form. During the first 2 weeks of life, there was a large increase in the activity of soluble AChE (G forms), whilst the activity of insoluble AChE (A forms) was reduced. Denervation of the muscle reversed the change in the relative proportions of the molecular forms. The embryonic pattern of activities of AChE forms persisted in cultures of myotubes obtained at 20 days' gestation and maintained in the absence of spinal cord. When myotubes were maintained in medium previously conditioned by developing spinal cord explants, 16 S AChE declined while the soluble (4 and 6 S) forms increased in activity in a manner resembling that seen in early postnatal muscles in vivo. beta-Endorphin (beta-EP) immunoreactivity was detected in the spinal cord-conditioned medium and was identified by HPLC and ion-exchange chromatography as beta-EP-(1-31) plus its shortened and N-acetylated forms. Cultivation of myotubes in the presence of synthetic camel beta-EP resulted in a reversible change in the pattern of AChE forms which was similar to that seen with spinal cord-conditioned medium. These studies provide evidence for the neuroregulation of AChE A and G forms in immature skeletal muscle. A major candidate for this role is beta-EP, produced and released by developing spinal cord.

Acetylcholinesterase↗

Agreement between A-mode and B-mode ultrasonography in the measurement of ocular distances.

It is generally accepted that A-mode ultrasonography is more accurate than B-mode in measuring intraocular dimensions. Consequently, A-mode ultrasonography is the procedure of choice in ocular biometry while B-mode ultrasonography is used principally for diagnostic purposes. In this study, we investigated the agreement between measurement of intraocular distances using A- and B-mode ultrasonography on freshly enucleated camel eyes. Our results suggest that relative to average A-mode values, B-mode overestimates corneal thickness (bias = 0.06 mm) and anterior chamber depth (bias = 0.03 mm), while it underestimates lens thickness (bias = -0.11 mm), vitreous chamber depth (bias = -0.32 mm) and axial length (bias = -0.40 mm). In general, difference between A- and B-mode values is larger for deeper intraocular dimensions. This implies that the two methods are more likely to give different readings for measurements of lens thickness, vitreous chamber depth and axial length.

Animals↗

The role of wild animals in the spread of exotic diseases in Australia.

The distributions of the following feral animals are given -- cattle, buffalo, pig, goat, deer, camel, horse, donkey, fox, dog and cat -- and the native dingo. The possible role these and the native rodents, marsupials and monotremes would play should an exotic disease of livestock enter Australia is discussed. It is considered that feral animals would be important in creating foci from which the disease would spread.

Animal Diseases↗

Antibodies to Akabane virus in Australia.

Neutralising antibody to Akabane virus was shown to develop in cattle in northern Australia throughout the year and also on the east coast of New South Wales in the summer during 1975/1976. Other species found to have antibody to Akabane virus were buffaloes, horses, camels and sheep, but no antibody was found in domestic chickens, ducks, wallabies or man. The biting midge Culicoides brevitarsis has been detected in all the major areas where antibody was demonstrated in this study.

Animals↗