Precipitin production in chickens. XXI. Antibody production in bursectomized chickens and in chickens injected with 19-nortestosterone on the fifth day of incubasion.
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[Oviduct and egg of the chicken. The correlation of morphology and function in the comparison of secretory organ and secretory product. I. Morphology of oviductal mucosa in the chicken. II. Formation and structure of membranes for the egg cells in the chicken].
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[The oviduct and egg of the chicken. The correlation of morphology and function comparing secretory organs and secretion products. I. Morphology of the oviduct mucous membrane of the chicken. II. Formation and structure of the shells of the chicken egg cell].
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Animals↗
Coinfection of specific-pathogen-free chickens with Marek's disease virus (MDV) and chicken infectious anemia virus: effect of MDV pathotype.
Both Marek's disease virus (MDV) and chicken infectious anemia virus (CIAV) infections are prevalent in chickens throughout the world. In the past decade, MDV strains with increased virulence (very virulent plus MDV pathotype [vv+MDV]) have been isolated. The purpose of this experiment was to determine the effects of coinfection of chickens with CIAV and a vv+MDV isolate. Specific-pathogen-free chickens were inoculated at 1 day posthatch with RB1B (very virulent MDV pathotype [vvMDV]) only, 584A (vv+MDV) only, CIAV only, RB1B + CIAV, 584A + CIAV, or nothing. Samples of spleen, thymus, and bursa of Fabricius were collected at 4, 7, 10, and 13 days postinoculation (DPI). Thymic and bursal atrophy at 13 DPI and final mortality at 30 DPI were significantly greater in chickens inoculated with 584A with or without added CIAV, or with RB1B plus CIAV, compared with birds inoculated with RB1B alone. Both amounts of virus reisolated and levels of virus detected by quantitative-competitive polymerase chain reaction were greater at 4 DPI in 584A inoculates compared with RB1B inoculates. To monitor the early cytolytic infection, northern analysis was done with a probe for the MDV immediate early gene ICP4 (infected cell protein 4). In the absence of CIAV, ICP4 expression was more apparent in chickens inoculated with 584A than in those inoculated with RB1B. CIAV coinfection increased ICP4 expression in the spleens of chickens infected with RB1B. These results indicated that inoculation of chickens with the 584A isolate caused a more robust early cytolytic infection compared with inoculation with RB1B alone and support the classification of 584A as a vv+MDV strain. Coinfection with CIAV exacerbated vvMDV strain RB1B infection. The extent of this exacerbation was less evident when birds were coinfected with 584A and CIAV.
Animals↗
Isolation and characterisation of chicken L- and H-kininogens and their interaction with chicken cysteine proteinases and papain.
We have isolated L- and H-kininogens from chicken egg white and plasma using affinity chromatography on CM-papain Sepharose, Con-A Sepharose, gel filtration and ion exchange chromatography, in pure form. In chicken plasma mostly HK was present, whereas in chicken egg white both LK and HK were identified. The determined Mr of LK and HK were 69000 and about 96000, respectively. They occurred in multiple forms with pI 4.3-5.2. The inhibitory activity of chicken HK was tested against cysteine proteinases cathepsins B and L, isolated from chicken liver, and papain. The obtained Ki values demonstrated that chicken H-kininogen is a strong inhibitor of chicken cathepsin L and papain, but much weaker inhibitor of chicken cathepsin B.
Amino Acid Sequence↗
Village chicken flock dynamics and the contribution of chickens to household livelihoods in a smallholder farming area in Zimbabwe.
The development of successful production strategies for poultry rearing depends on an accurate description of village chicken production systems. In Rushinga District of Zimbabwe, participatory rural appraisals (PRAs) followed by checklists and intensive case studies were carried out in three villages. The role of chickens in the livelihoods of households was evaluated. Flock dynamics were monitored monthly for 24 months. Women who were resident on the farm headed 19% of the households. A household comprised 4.8 +/- 2.5 members with arable land of approximately 2.6 ha. In addition to chickens, households grew maize, cotton and sunflower and kept large animals. Flocks ranging from 1 to 50 village chickens per household were reared under a scavenging system of management with suboptimal housing, inadequate feeding and poor health care. The use of ethno-veterinary medicine was common in treating sick chickens. The largest flock sizes were observed in the hot-wet season. Over 90% of an average of 5.4 entries/household per month were from hatched chicks. Mortality claimed an average of 80% of the total exits. Chicken production potential (CPP), which defined the proportion of chickens that could be utilized by a household, averaged 50%. Chicken production efficiency (CPE) was approximately 15% of the CPP. Egg consumption patterns were low and similar across seasons.
Animal Husbandry↗
2-[125I]iodomelatonin labels sites with identical pharmacological characteristics in chicken brain and chicken retina.
The binding and pharmacological characteristics of the melatonin site labeled by the radioligand 2-[125I]iodomelatonin in chicken brain membranes were determined and compared with those of the melatonin site of chicken retinal membranes. The specific binding of 2-[125I]iodomelatonin to chicken brain membranes was found to be stable, saturable, reversible and of high affinity. Scatchard analysis of the binding revealed an affinity constant (Kd) of 344 +/- 24 pM (n = 4) and a total number of binding sites (Bmax) of 57.6 +/- 10.1 fmol/mg protein (n = 4). The Kd value correspond closely with that found in kinetic studies (Kd = 407 pM) and that reported in chicken retinal membranes. Competition experiments were carried out with various compounds revealing the following order of pharmacological affinities: 6-chloromelatonin greater than or equal to 2-iodomelatonin greater than melatonin greater than 2-methyl-6,7-dichloromelatonin greater than 6-hydroxymelatonin greater than N-acetyl-5-hydroxytryptamine greater than luzindole greater than N-acetyl-5-methoxykynurenamine greater than 6-methoxymelatonin greater than N-acetyltryptamine greater than 5-methoxytryptamine greater than 5-hydroxytryptamine greater than 5-methoxy-N,N-dimethyltryptamine greater than 5-methoxytryptophol. This order of pharmacological affinities is identical to that found in chicken retinal membranes. Correlation between affinity constants for various melatonin receptor agonists and putative melatonin receptor antagonists obtained in chicken brain and retinal membranes yielded a correlation coefficient (r) of 0.966 (slope = 0.652, n = 14, P less than 0.01). We conclude that the high affinity site labeled by 2-[125I]iodomelatonin in chicken brain membranes has identical binding and pharmacological characteristics to the ML-1 melatonin receptor site previously described in chicken retinal membranes.
Animals↗
Chicken beta B1 crystallin: gene sequence and evidence for functional conservation of promoter activity between chicken and mouse.
The complete sequence was determined for the chicken beta B1-crystallin gene and 2.2 kbp of its 5' flanking region; the chicken gene was then compared to its rat ortholog. Although both have a 5' non-coding exon followed by 5 protein coding exons, the chicken gene is only 2.2 kbp while the rat gene is 13.6 kpb due to longer introns. The coding exons of the chicken beta B1-crystallin gene, like those of the rat and other beta-crystallin genes, each correspond to one of the four 'Greek key' motifs of the encoded protein. The only obvious similarity between the 5' flanking sequences of the chicken and rat beta B1-crystallin gene is associated with the TATA box. A CR1 repetitive element is present at positions -559 to -730 of the chicken beta B1-crystallin gene. In vivo footprinting using dimethyl sulfate/ligation mediated PCR showed that the PL-1 (-116/-102), PL-2 (-90/-76), OL-2 (-75/-68) and OL-1 (-125/-118) control elements identified previously (Roth et al. (1991) Mol. Cell. Biol. 11, 1488-1499) bind proteins within the chromatin of cultured embryonic chicken lens cells. Both -2448/+30 and -434/+30 promoter fragments from the chicken beta B1-crystallin gene directed lens-specific CAT gene expression in a copy number and position independent manner in transgenic mice. These data indicate that the structure and lens-specific expression of this gene are highly conserved although, like other crystallin genes, the 5' flanking sequences have diverged appreciably during evolution.
Amino Acid Sequence↗
The effect of short-time microwave exposures on Escherichia coli O157:H7 inoculated onto chicken meat portions and whole chickens.
Small portions of fresh chicken breasts weighting 20 g each and fresh whole chickens, weighting on average 1310 g each, were inoculated with Escherichia coli O157:H7 (10(5)-10(6) cfu/g) and cooked, using two different domestic microwave ovens at full power. The chicken portions were heated for 5, 10, 15, 20, 25, 30, and 35 s and the whole chickens for 22 min. Following exposures, viable counts and temperature measurements were performed. Although the chicken breast portions looked well-cooked after 30 s of MW heating at a mean end-point surface temperature of 69.8 degrees C, a mean concentration of 83 cfu/g E. coli O157:H7 cells was recovered. Elimination of E. coli O157:H7 cells occurred only after 35 s of MW exposure at 73.7 degrees C. When whole chickens were thoroughly cooked by MW heating, the final subsurface temperatures, measured in the thighs and wings, ranged from 60.2 degrees C to 92 degrees C and viable cells of E. coli O157:H7 were recovered from all samples of whole chicken. The results indicate that short time exposures of chicken portions to microwave heating do not eliminate E. coli O157:H7.
Animals↗
Characterization of turkey and chicken ghrelin genes, and regulation of ghrelin and ghrelin receptor mRNA levels in broiler chickens.
Ghrelin, a peptide hormone produced by the stomach in mammals, stimulates growth hormone release and food intake. Recently, ghrelin was identified and characterized in chicken proventriculus and shown to stimulate growth hormone release but inhibit feed intake. The purpose of this work was to identify and further characterize the ghrelin gene in chickens and in turkeys. Using molecular cloning techniques we have sequenced cDNAs corresponding to chicken (White Leghorn) and turkey ghrelin mRNAs. A total of 844 (chicken) or 869 (turkey) bases including the complete coding regions (CDS), and the 5'- and 3'-untranslated regions (UTRs) were determined. Nucleotide sequence (CDS) predicted a 116 amino acid precursor protein (preproghrelin) for both the chicken and the turkey that demonstrated complete conservation of an N-terminal 'active core' (GSSF) including a serine (position 3 of the mature hormone) known to be a modification (acylation) site important for ghrelin bioactivity. Additional nucleotide sequence was found in the 5'-UTRs of both Leghorn and turkey cDNAs that was not present in broilers or the red jungle fowl. The turkey ghrelin gene, sequenced from genomic DNA templates, contained five exons and four introns, a structure similar to mammalian and chicken ghrelin genes. Ghrelin was highly expressed in proventriculus with much lower levels of expression in other tissues such as pancreas, brain, and intestine. RT-PCR was used to quantify ghrelin mRNA levels relative to 18S rRNA in 3-week-old male broiler chickens. The level of ghrelin mRNA increased in proventriculus in response to fasting but did not decline with subsequent refeeding. Plasma ghrelin levels did not change significantly in response to fasting or refeeding and did not appear to reflect changes in proventriculus ghrelin mRNA levels. Ghrelin mRNA levels declined in broiler pancreas after a 48 h fast and increased upon refeeding. Expression of the gene encoding the receptor for ghrelin (growth hormone secretagogue receptor, GHS-R) and a variant form was detected in a variety of tissues collected from 3-week-old male broiler chickens possibly suggesting autocrine/paracrine effects. These results offer new information about the avian ghrelin and ghrelin receptor genes and the potential role that this system might play in regulating feed intake and energy balance in poultry.
Amino Acid Sequence↗
Recombinant fowlpox viruses coexpressing chicken type I IFN and Newcastle disease virus HN and F genes: influence of IFN on protective efficacy and humoral responses of chickens following in ovo or post-hatch administration of recombinant viruses.
We have constructed recombinant (r) fowl pox viruses (FPVs) coexpressing chicken type I interferon (IFN) and/or hemagglutinin-neuraminidase (HN) and fusion (F) proteins of Newcastle disease virus (NDV). We administered rFPVs and FPV into embryonated chicken eggs at 17 days of embryonation or in chickens after hatch. Administration of FPV or rFPVs did not influence hatchability and survival of hatched chicks. In ovo or after hatch vaccination of chickens with the recombinant viruses resulted in protection against challenge with virulent FPV and NDV. Chickens vaccinated with FPV or FPV-NDV recombinant had significantly lower body weight 2 weeks following vaccination. This loss in body weight was not detected in chickens receiving FPV-IFN and FPV-NDV-IFN recombinants. Chickens vaccinated with FPV coexpressing IFN and NDV genes produced less antibodies against NDV in comparison with chickens vaccinated with FPV expressing NDV genes.
Animals↗
Assessment of the cell-mediated immune response in chickens by detection of chicken interferon-gamma in response to mitogen and recall Newcastle disease viral antigen stimulation.
The potential of a capture enzyme-linked immunosorbent assay (ELISA) specific for chicken interferon-gamma (ChIFN-gamma) has been evaluated as a tool to assess cell-mediated immunity (CMI) in the chicken. In a first step, ChIFN-gamma production and cell proliferation of mitogen-activated chicken splenocytes have been compared. In general, for each of the stimulation conditions where significant proliferation was observed, production of ChIFN-gamma could be measured by ELISA. In our hands, the combination of ionomycin and phorbol-12-myristate 13-acetate or the use of recombinant chicken interleukin-2 gave the most satisfactory results. Then, the CMI response induced by live or killed Newcastle disease virus (NDV) vaccines has been evaluated sequentially by ex vivo antigen-specific ChIFN-gamma production and cell proliferation of splenocytes from immune chickens. The ex vivo data showed that both types of NDV vaccines are capable of stimulating CMI responses to NDV in chickens as measured by the ChIFN-gamma ELISA. However, most of the chickens vaccinated with the live vaccine produced ChIFN-gamma after antigen recall stimulation, from 2 to 4 weeks after vaccination, when only some chickens vaccinated with the inactivated vaccine showed a specific response 4 weeks after vaccination. No significant proliferative responses to either NDV vaccine were detectable during the 4 weeks of the study. From our results, it appears that antigen-specific ChIFN-gamma production can be used as a good indicator of actively acquired immunity to NDV and that the sensitivity range of the capture ELISA test is well adequate to measure ex vivo release of ChIFN-gamma.
Animals↗
Gene mapping in chicken-Chinese hamster somatic cell hybrids. Serum albumin and phosphoglucomutase-2 structural genes on chicken chromosome 6.
Chicken phosphoglucomutase (PGM-2), serum albumin, vitamin D binding protein (Gc) and phosphoribosyl pyrophosphate amidotransferase (PPAT) structural genes have been mapped to chicken chromosome 6 using chicken-Chinese hamster somatic cell hybrids containing this chromosome as the only chicken genetic material. Chicken PGM-2 activity was detected in the hybrids using cellogel electrophoresis and a substrate, ribose-1-phosphate (R-1-P), that allows the detection of PGM-1 activity in mice and PGM-2 activity in humans. Chicken albumin sequences were detected in the hybrids with the use of a labelled chicken serum albumin cloned cDNA. Classical studies have shown linkage of the serum albumin and Gc genes, and the Gc gene also can be localized to chicken chromosome 6. The PPAT gene was localized to this chromosome in previous studies using these hybrids. A homologous linkage group has been identified in mammals and, therefore, a chromosomal linkage group containing at least four genes--Gc, serum albumin, PPAT, and PGM-2--has been conserved over a period of 300 million years, throughout both avian and mammalian evolution.
Amidophosphoribosyltransferase↗
Chicken GnRH II-like peptides and a GnRH receptor selective for chicken GnRH II in amphibian sympathetic ganglia.
Amphibia, like most vertebrate species, have two forms of GnRH, namely [Arg8]GnRH (mammalian GnRH) and [His5,Trp7,Tyr8] GnRH (chicken GnRH II). The differential distribution of the two peptides in the amphibian brain suggests that they may play different roles. Mammalian GnRH, which is found predominantly in the hypothalamus, is most likely the prime regulator of gonadotropin release, while chicken GnRH II, which occurs predominantly in the midbrain and hindbrain, may play a neuromodulatory role. In amphibian sympathetic ganglia, GnRH has been demonstrated to be a neurotransmitter where its release from the presynaptic nerve terminals reversibly inhibits M current, a time- and voltage-dependent potassium current. The occurrence of GnRH in sympathetic ganglia extracts from two amphibian species was investigated. Chicken GnRH II-like immunoreactivity was detected in extracts of bullfrog (Rana catesbeiana) and platanna (Xenopus laevis) sympathetic ganglia after high performance liquid chromatography. Under the chromatographic conditions used, a second unknown peptide co-eluted with synthetic mammalian GnRH, but showed no cross-reactivity with specific mammalian GnRH antisera. To test the possibility of the presence of a chicken GnRH II receptor in sympathetic ganglion neurones, competition binding of membranes extracted from the sympathetic ganglia of the two amphibian species was investigated with 125I-labelled GnRH agonists. The binding of 125-I-[His5,D-Arg6,Trp7,Tyr8]GnRH (a chicken GnRH II agonist) to membranes from the sympathetic ganglia of both amphibian species was specific and had a higher affinity than chicken GnRH II, mammalian GnRH and a mammalian GnRH agonist [D-Ala6,NMe-Leu7,Pro9-NHEt]GnRH. These findings suggest that endogenous chicken GnRH II may play a role in synaptic transmission in the sympathetic ganglia via a receptor specific for chicken GnRH II.
Amphibians↗
Molecular cloning of the chicken growth hormone receptor complementary deoxyribonucleic acid: mutation of the gene in sex-linked dwarf chickens.
A novel complementary DNA (cDNA) encoding the chicken GH receptor was isolated from a chicken liver cDNA library, using polymerase chain reaction with primers derived from highly conserved sequences of the mammalian GH receptor. The nucleotide sequence predicts a mature protein of 592 amino acids and a 16 amino acid signal peptide that are partially homologous to the sequence reported for the rabbit (53%), rat (58%), and human (50%) GH receptors. Despite this low level of homology, a number of structural features of the GH receptor are conserved, including 7 cysteine residues in the extracellular domain and 5 in the intracellular region. Three transcripts of approximately 4.7, 4.0, and 1.0 kilobases are present on Northern blots of total RNA prepared from the livers of 35-week-old male chickens. Expression of the GH receptor was also detected in a wide range of tissues. The chicken GH receptor cDNA was then used as a probe in Southern and Northern blot analyses of DNA and RNA prepared from livers of sex-linked dwarf chickens, which have undetectable levels of hepatic GH-binding activity, in addition to other endocrine abnormalities. A restriction fragment length polymorphism was found in DNA, and an aberrantly-sized transcript was found in hepatic RNA of the dwarf chicken. These results indicate that a mutation in the GH receptor gene is responsible for the phenotype of the sex-linked dwarf chicken. This type of dwarfism resembles Laron-type dwarfism in humans, where a defect in the GH receptor gene has recently been identified. These receptor-deficient chickens should serve as a unique model system for studying the role of the GH receptor in growth and development.
Amino Acid Sequence↗
Effect of serum from chickens treated with clenbuterol on myosin accumulation, beta-adrenergic receptor population, and cyclic AMP synthesis in embryonic chicken skeletal muscle cell cultures.
Broiler chickens at 35 d of age were fed 1 ppm clenbuterol for 14 d. This level of dietary clenbuterol led to 5-7% increases in the weights of leg and breast muscle tissue. At the end of the 14-d period, serum was prepared from both control and clenbuterol-treated chickens, and was then employed as a component of cell culture media at a final concentration of 20% (v/v). Muscle cell cultures were prepared from both the leg and the breast muscle groups of 12-d chick embryos. Treatment groups included control chicken serum to which 10 nM, 50 nM, and 1 microM clenbuterol had been added, as well as cells grown in media containing 10% horse serum. Cultures were subjected to each treatment for 3 d, beginning on the seventh d in culture. Neither the percent fusion nor the number of nuclei in myotubes was significantly affected by any of the treatments. The quantity of myosin heavy chains (MHCs) was not increased by serum from clenbuterol-treated chickens in either breast or leg muscle cultures; however, the MHC quantity was 50-150% higher in cultures grown in control chicken serum to which 10 and 50 nM clenbuterol had also been added. The beta-adrenergic receptor (betaAR) population was 4000-7000 betaARs per cell in cultures grown in chicken serum, with leg muscle cultures having approximately 25-30% more receptors than breast muscle cultures. Receptor population was not significantly affected by the presence of clenbuterol or by the presence of serum from clenbuterol-treated chickens. In contrast, the betaAR population in leg and breast muscle cultures grown in the presence of 10% horse serum was 16,000-18,000 betaARs per cell. Basal concentration of cyclic adenosine 3':5'monophosphate (cAMP) was not significantly affected by the treatments. When cultures grown in chicken serum were stimulated for 10 min with 1 microM isoproterenol, limited increases of 12-20% in cAMP concentration above the basal levels were observed. However, when cultures grown in the presence of horse serum were stimulated with 1 microM isoproterenol, cAMP concentration was stimulated 5- to 9-fold above the basal levels. Thus, not only did cells grown in horse serum have a higher betaAR population, but also each receptor had a higher capacity for cAMP synthesis following isoproterenol stimulation. Finally, the hypothesis that clenbuterol exerts its action on muscle protein content by changes in cAMP concentration was tested. No correlation was apparent between basal cAMP concentration and MHC content.
Animals↗
Isolation of chicken anaemia virus from broiler chickens.
Chicken anaemia virus (CAV) infection was demonstrated, by both serology and virus isolation, in 1- to 6-week-old broiler chickens originated from various parent flocks in Hungary. Total losses in the broiler flocks were estimated at 7 to 8% and about 25% of the chickens failed to reach target body mass by the 7th week of life. The clinical signs, postmortem lesions and histopathological changes of the affected chickens were similar to those of naturally occurring CAV-induced infectious anaemia of young chickens. In MDCC-MSB1 cell cultures, a chloroform-resistant virus smaller than 50 nm in diameter, resistant to heating at 70 degrees C for 30 min, and antigenically very closely related to the Cux-1 strain of CAV was isolated from the liver of naturally diseased broilers. This virus isolate was designated the Bia strain of CAV. Inoculation of susceptible 1-day-old SPF chicks with a CAV-positive liver extract from naturally diseased broilers caused pathological changes characteristic of CAV infection, namely impaired growth, severe anaemia with atrophy of the bone marrow, marked atrophy of the lymphoid organs and petechial haemorrhages throughout the body. A quite similar pathological syndrome was also induced by inoculation of 1-day-old SPF chicks with the MDCC-MSB1 cell-culture-propagated new Bia strain of CAV. The CAV was successfully reisolated from the livers of experimentally inoculated birds, and antibodies to the reference Cux-1 strain of CAV were also demonstrated by the indirect immunofluorescence test in sera of naturally diseased and experimentally inoculated chickens. No antibodies were found against infectious bursal disease virus, reticuloendotheliosis virus, Marek's disease herpesvirus as well as avian adenoviruses and reoviruses. The reported disease of young broiler chickens was associated with natural infection of a new isolate of CAV. On the basis of its physicochemical, antigenic and pathogenic characteristics, this virus is similar to other strains of CAV isolated from chickens in other countries.
Anemia↗
Evolution of intestinal apolipoprotein B mRNA editing. Chicken apolipoprotein B mRNA is not edited, but chicken enterocytes contain in vitro editing enhancement factor(s).
Mammalian intestinal apolipoprotein B (apoB) messenger RNA (mRNA) undergoes posttranscriptional editing, changing codon 2153 from CAA in apoB100 mRNA to an in-frame translational stop codon (UAA) in apoB48 mRNA. By contrast, chicken intestinal apoB cDNA contains a CAA codon at the corresponding site and apoB mRNA from chicken enterocytes, kidney, and liver is unedited. The cDNA sequence of chicken apoB spanning the edited base is divergent from mammalian apoB cDNA sequence, with 70% homology over the conserved 29-nucleotide sequence (6662-6690) flanking codon 2153. Efficient in vitro editing of both human and rat, but not chicken, synthetic apoB RNA was achieved using rat enterocyte S-100 extracts. By contrast, chicken enterocyte S-100 extracts failed to edit chicken, rat, or human synthetic apoB RNA. Mixing experiments, however, revealed that chicken enterocyte S-100 extracts enhance the in vitro editing activity of rat, pig, and human enterocyte S-100 extracts upon homologous RNAs. The editing enhancement activity of chicken enterocyte S-100 extracts is tissue-specific, heat-sensitive, substrate-saturable, and sensitive to proteinase K, but resistant to micrococcal nuclease. The activity was partially purified by Q-Sepharose chromatography and has an average molecular mass of 49 kDa when analyzed by gel filtration chromatography. We conclude that the evolutionary adaptation of intestinal apoB mRNA editing requires both a requisite RNA motif and tissue-specific factors which mediate the site-specific modification.
Animals↗