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PubMed1991

Immunolocalization of steroidogenic cells in small follicles of the chicken ovary: anatomical arrangement and location of steroidogenic cells change during follicular development.

Previous anatomical and histochemical studies suggested that interstitial cells were the only steroidogenic cells in the theca layer of small follicles of the chicken ovary. However, the precise cellular site of steroid production in the small follicles is not certain. Therefore, our goal was to identify steroidogenic cells in small follicles (less than 10 mm in diameter) of the chicken ovary which have not entered the follicular hierarchy by localizing steroidogenic enzymes with immunocytochemistry. Polyclonal antisera used were anti-cholesterol side-chain-cleavage cytochrome P450 (P450scc), anti-17 alpha-hydroxylase cytochrome P450 (P450c17), and anti-aromatase cytochrome P450 (P450arom) for pregnenolone-, androgen-, and estrogen-producing cells, respectively. Ovaries were collected 2 hr after oviposition and embedded in Paraplast after fixation with 4% paraformaldehyde, 10% formaldehyde, or Bouin's solution. Tissues were sectioned (4-6 microns) and sections were mounted on poly-L-lysine coated slides. Sections were incubated overnight at room temperature with each specific antiserum raised in rabbits against cytochrome P450 steroidogenic enzymes or normal rabbit serum as a control and were immunostained with an avidin-biotin-peroxidase complex. Immunoreactivity for the P450 enzymes was absent in the granulosa layer but was present in the theca layer of the small follicles (less than 10 mm in diameter). Interstitial cells in the single theca layer of cortical follicles embedded in the ovarian cortex (less than 1 mm in diameter) contained P450scc and P450c17. Cells which contained P450arom, identified as aromatase cells, surrounded the interstitial cells in the theca layer.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed2004

A new single nucleotide polymorphism in the chicken pituitary-specific transcription factor (POU1F1) gene associated with growth rate.

The pituitary-specific transcription factor (POU1F1) is a protein which binds to and transactivates promoters of growth hormone (GH), prolactin (PRL) and thyroid-stimulating hormone chain (TSHB)-encoding genes. Ten chicken populations (n = 662), including six Chinese indigenous breeds, White Leghorn, paternal/maternal lines of brown egg layer and a paternal line of broiler, were used to detect single nucleotide polymorphisms in the pituitary-specific transcription factor gene (PIT1) by means of PCR-SSCP. A nucleotide transversion from adenine (A) to thymidine (T) at position 980 of the open reading frame of the PIT1 cDNA (GenBank accession no. AF029892) was identified. This nucleotide transversion results in an alteration of codon 299 from AAC to ATC, which leads to a change from asparagine (Asn) to isoleucine (Ile) in the POU domain of POU1F1. The distribution of allele and genotype frequencies differed significantly between meat-type chickens (higher frequencies of A and A/A) and layer-type chickens (P < 0.01). Another experimental population with growth records was used to evaluate the relationship between this polymorphism and growth rate. The results revealed a positive relationship between genotype A/A and body weight at 8 weeks of age, indicating that the SNP in PIT1 gene is a potential molecular marker for early growth rate in chicken.

Animals↗
PubMed1995

Contribution of oligosaccharide and polysaccharide digestion, and excreta losses of lactic acid and short chain fatty acids, to dietary metabolisable energy values in broiler chickens and adult cockerels.

1. Two experiments were conducted, using both adult cockerels from a layer strain and 3-week-old broiler chickens. In the first experiment, one of the 2 diets investigated was composed mainly of maize and soyabean meals, the other one containing the latter ingredients diluted with 475 g/kg mature pea seeds. For these 2 diets, the apparent metabolisable energy values corrected to 0 nitrogen retention (AMEn) were derived, together with the apparent digestibilities of nitrogen, amino acids, total lipids, starch, individual oligosaccharides, and non-starch polysaccharides (NSP). Excretions of lactic acid and short chain fatty acids (SCFA) were also determined. 2. In the first experiment, the mean apparent digestibilities of starch, lipids, total amino acids, NSP, sucrose and alpha-galacto-oligosaccharides in adult cockerels were 0.946, 0.785, 0.835, 0.045, 0.99 and 0.99, respectively. In broiler chickens, they were 0.938, 0.675, 0.830, -0.016, 0.988 and 0.867, respectively. The bird type effects were significant (P < 0.05) for the digestibilities of starch, lipids, NSP (for the maize-soyabean meal diet, only) and alpha-galacto-oligosaccharides. Broiler chickens excreted a mean of 11.032 g organic acids/kg diet against 4.190 in adult cockerels (P < 0.001). These digestibility measurements enabled the contribution made by each dietary component to the AMEn value of the diets to be calculated. AMEn values were lower in broiler chickens than in adult cockerels, with on average 0.8 MJ/kg dry matter difference resulting from bird type. This difference was accounted for by differences between bird types in energy supplied by lipids (34.0%), starch (7.5%), alpha-galacto-oligosaccharides (8.7%), NSP (14.2%), and in energy losses from lactic acid excretion (16.4% of the difference in AMEn between bird types). 3. In the second experiment 2 diets were studied, consisting of a basal and the basal diluted with 30 g/kg lactose (a fermentable sugar in chickens) and 12 g/kg of a water-soluble gel-forming component containing 50% polygalacturonic acids. Lactose digestibilities reached 0.928 and 0.712 in adult cockerels and chickens, respectively. The digestibilities of the water-soluble polygalacturonic acids were similar in cockerels and broiler chickens, with a mean value of 0.672. Figures similar to those of the first experiment were found in the comparison between cockerels and broiler chickens, for the AMEn values of diets, the digestibilities of starch and lipids and the excretion of lactic acid. Broiler chickens excreted 4.580 g lactic acid/kg dry food intake, compared with 0.740 g in the adult.(ABSTRACT TRUNCATED AT 400 WORDS)

Aging↗
PubMed1983

Interspecies comparison of muscle gangliosides by two-dimensional thin-layer chromatography.

Skeletal muscle gangliosides prepared from ten species of animals (human, monkey, bovine, hog, dog, cat, rabbit, guinea pig, mouse, and chicken) were studied by two-dimensional thin-layer chromatography. Densitometric quantification of spots on the chromatograms was carried out with an image analysis system equipped with a computer system. In about thirty-five resorcinol-positive spots, sixteen components could be identified by comparison with authentic standards we had previously obtained. GM3 ganglioside was found as a major component in all examined animals, but there were remarkable species variations in the minor gangliosides. In bovine and hog muscle gangliosides, more than fifteen minor components were detected owing to the presence of N-glycolyl neuraminic acid species. In contrast to this, muscle gangliosides of human, dog, cat, rabbit, and chicken showed relatively simple patterns because of the absence or the small amounts of N-glycolyl type gangliosides. The presence of lactosamine containing gangliosides was characteristic of muscle gangliosides of the examined species.

Animals↗
PubMed1996

Distribution of neurotensin-containing neurons in the central nervous system of the pigeon and the chicken.

Neurotensin is widely located in neurons of the central and peripheral nervous systems among mammalian species. To obtain a comparative evaluation, we examined the distribution of neurotensin-containing cell bodies and fibers in the central nervous system of the pigeon and the chicken. The pattern of localization of neurotensin immunoreactivity was similar in the two species. Abundant accumulations of neurotensin-containing cell bodies were found in the dorsolateral corticoid area, the piriform cortex, the parahippocampal area, the medial part of the frontal neostriatum, the lateral part of the caudal neostriatum, nucleus accumbens, the bed nucleus of the stria terminalis, ventral paleostriatum, the preoptic area, the ventromedial hypothalamic nucleus, the inferior hypothalamic nucleus, the infundibular hypothalamic nucleus, and the mammillary nuclei. Extremely dense networks of neurotensin-containing fibers were found in the pallial commissure, the lateral septal nucleus, the preoptic area, the periventricular gray around the third ventricle, the dorsalis hypothalamic area, the hypothalamic nuclei, the parabrachial nucleus, the locus ceruleus, and the dorsal vagal complex. Major differences of immunoreactivity between the two species were as follows. 1) The chicken neurohypophysis contained an extremely large accumulation of immunoreactive fibers, but there were few in the median eminence. The reverse was found in the pigeon. 2) The optic tectum in the pigeon contained immunoreactive cells and fibers in layers 2 and 4, but no immunoreactivity was seen in the chicken optic tectum. 3) The cerebellar cortex in the pigeon contained a small number of immunoreactive fibers, whereas that in the chicken did not. 4) The pigeon spinal cord contained immunoreactive neurons in the subependymal layer, but the chicken spinal cord did not. Our observations suggest the presence of a very wide network of neurotensin-containing neurons in the avian brain and spinal cord, which is also the case in mammals.

Anatomy, Artistic↗
PubMed2001

Activin A and gonadotropin regulation of follicle-stimulating hormone and luteinizing hormone receptor messenger RNA in avian granulosa cells.

Activin A regulation of the expression of mRNA for the LH receptor, FSH receptor, and the inhibin alpha subunit as well as the effect of activin A on the secretion of progesterone were investigated in chicken granulosa cell cultures. Granulosa layers were isolated from the F(1) and F(3) + F(4) follicles from five hens, pooled according to size, dispersed, and cultured for 48 h. In experiment 1 (n = 3 replications), granulosa cells were cultured with or without highly purified ovine (o) FSH at 50 ng/ml and in the presence of 0, 10, or 50 ng/ml of recombinant chicken activin A. Experiment 2 (n = 4 replications) followed the same protocol as experiment 1, except that oFSH was replaced with oLH. Results from these experiments showed that addition of activin A to the granulosa cell cultures had no effect on the expression of mRNA for the inhibin alpha subunit or the FSH receptor, but it did affect the expression of mRNA for the LH receptor. Treatment of F(3) + F(4) granulosa cells with LH stimulated the expression of mRNA for the LH receptor; however, when LH was combined with either dose of activin A, this induction was prevented. The highest dose of activin A with or without LH resulted in decreased expression of the LH receptor compared to the untreated controls in the F(3) + F(4) cell cultures. Progesterone secretion by the granulosa cells from both follicle sizes was not altered by activin A. In experiment 3 (n = 3 replications), the effect of activin A on the growth of granulosa cells was examined with the following treatments: 0, 10, or 50 ng/ml of activin A; 50 ng/ml of either oLH or oFSH; and oLH or oFSH combined with 10 ng/ml of activin A. The highest dose of activin reduced the rate of granulosa cell proliferation in both follicle types. Growth of F(1) and F(3) + F(4) granulosa cells was stimulated by the addition of either gonadotropin, and the presence of 10 ng/ml of activin A with either gonadotropin did not alter this proliferation, except for the LH-treated F(3) + F(4) granulosa cells, in which the increase in proliferation was prevented. The results suggest that activin A could act as a local factor that regulates follicular maturation by preventing excessive or untimely LH receptor expression.

Activins↗
PubMed1997

Activin receptor mRNA expression by neurons of the avian ciliary ganglion.

Previous studies have suggested that activin may serve as a neurodifferentiation factor regulating somatostatin expression in neurons of the avian ciliary ganglion (CG). As one aspect of examining the role of activin in CG development, we inquired whether any of the known activin receptors are expressed by developing CG neurons in vivo. In addition, we examined whether activin A mRNA is expressed in the choroid layer and iris of the chicken eye. Oligonucleotide primers were designed for the chicken activin receptor type IIA (cActR-IIA), type IIB (cActR-IIB), and activin A. In reverse-transcription-polymerase chain reaction (rtPCR), an appropriately sized product was amplified from CG cDNA using primers to the cActR-IIA but not the cActR-IIB. Sequencing confirmed the identity of the PCR product as a fragment of the cActR-IIA. It thus appears that mRNA for the type IIA but not the type IIB activin receptor is expressed in the chicken CG. An antisense strand digoxigenin-labeled riboprobe complimentary to a 358-bp portion of the cActR-IIA kinase region hybridized to cells within cryostat sections of embryonic CG. From E6.5-E18, hybridization of this probe appears to be specific for cells with a neuronal morphology. Using rtPCR with activin A-specific primers we detected activin mRNA in the choroid layer of E14 and E19 eyes, and from the iris at E14. Our results are consistent with a role for activin as a neurodifferentiation factor in vivo, and imply that within the CG, the cActR-IIA is specifically expressed by neurons, and that activin A is expressed in the targets of these neurons.

Activin Receptors↗
PubMed2004

A new paradigm for corneal wound healing research: the white leghorn chicken (Gallus gallus domesticus).

PURPOSE: To evaluate the chicken cornea as a model for corneal wound healing research. METHODS: We conducted studies on normal chicken corneas and on corneas following mechanical debridement and photorefractive keratectomy (PRK). RESULTS: The chicken cornea possesses six distinct layers that resemble the layers of the human cornea, including a substantial Bowman's layer measuring 5.2 +/- 0.3 microm thick. Reepithelialization time was 44.8 +/- 1.1 hours with a sliding rate of 75.3 +/- 3.2 microm/hour following mechanical debridement and 54.4 +/- 2.8 hours with a sliding rate of 63.3 +/- 3.2 microm/hour for PRK-treated corneas. Biomicroscopic haze post-PRK peaked at 4-6 weeks and regressed until 20 weeks post-PRK. Histologic and clinical observations of wound healing strongly paralleled that noted in humans. CONCLUSION: The chicken cornea's morphology and wound healing response render it a useful model for corneal wound healing investigations.

Animals↗
PubMed1988

Differential developmental expression of cellular yes and cellular src proteins in cerebellum.

To identify the specific areas of the brain that express c-yes and c-src proteins, we examined chicken brains dissected from two-week-old birds using an immune complex kinase assay and an immune blot analysis. Highest levels of both proto-oncogene proteins were found in the cerebellum, whereas other parts of the brain, including telencephalon, diencephalon, mesencephalon and spinal cord, showed three- to six-times lower levels. Relatively low levels of the two proteins were detected in pineal body and pituitary. When the cerebellum was further dissected into three layers, molecular, granular and fibrous, both the c-yes and c-src proteins were found to be concentrated in the molecular layer and, to a lesser degree, also in the granular layer. In cerebellum and in chicken embryo fibroblasts the c-yes protein was predominantly associated with the membrane fraction, and in chicken embryo fibroblasts c-yes was labeled with radioactive myristic acid. Adult cerebellum showed a two- to three-fold increase in the c-yes protein level over that detected in embryonal cerebellum. Conversely, c-src expression in the embryonic cerebellum was relatively high and it was diminished in the adult cerebellum. Differential developmental expression of c-yes and c-src proteins in cerebellum suggests that these proteins fulfill different functions or different aspects of the same function.

Age Factors↗
PubMed1985

An interspecies comparison of gangliosides and neutral glycolipids in adrenal glands.

Gangliosides and neutral glycolipids of adrenal glands of mouse, rat, guinea pig, rabbit, cat, pig, cow, monkey, and chicken were analyzed by thin layer chromatography (TLC). The major gangliosides common to all species had lactosylceramide in their core structure. GM3 containing N-acetylneuraminic acid (NeuAc) was the major ganglioside in rat, guinea pig, rabbit, and cat, whereas GM3 containing N-glycolylneuraminic acid (NeuGc) was the major one in mouse, cow, and monkey. GD3 was also detected in all species except mouse and GD3(NeuAc)2 was the major in pig adrenal gland. GM4(NeuAc) was detected in the adrenal glands of guinea pig and chicken but not in those of the other species. In the neutral glycolipid fractions, galactosylceramide, glucosylceramide, lactosylceramide, globotriaosylceramide and globotetraosylceramide were detected and the proportions of these glycolipids varied among the species. Guinea pig and chicken adrenal glands contained large amounts of galactosylceramide, this being consistent with the presence of GM4 in these two species. Globopentaosylceramide was detected in mouse, guinea pig, cat, and chicken by the TLC-immunostaining procedure.

Adrenal Glands↗
PubMed2005

Breed-dependent susceptibility to acute sound exposure in young chickens.

Commercially available chickens fall into two categories: egg layers and broilers. Durham et al. (Hear. Res. 166 (2002) 82-95) showed that despite similar noisy living environments, cochleae of most adult broilers show extensive damage, while cochleae of adult egg layers are largely normal. This finding suggests that egg layers and broilers differ in their susceptibility to noise damage. Here, we evaluate breed differences in susceptibility to acoustic trauma. Young egg layers and broilers (10-17 weeks) were exposed to a 1500Hz pure tone (120dB SPL; 24h) and killed 24 or 72h later. Cochleae were prepared for scanning electron microscopy and photomicrographs of the cochlear surface were used to determine location and severity of damage. Cochleae were grouped based upon damage severity (moderate or severe). While location and area of damage were similar between both breeds at each recovery time, cochlear damage at 72h was more extensive than at 24h. We found no quantitative breed differences within either damage category or recovery time. However, more egg layers (25/27) than broilers (16/32) displayed severely damaged cochleae. Our findings conflict with those reported by Durham et al. (2002). Our results identify a breed-dependent difference in susceptibility to acute sound exposure, with young egg layers displaying increased sensitivity.

Animals↗
PubMedDate not supplied

Prevalence of antibodies to infectious bursal disease virus serotypes I and II in 75 Ohio chicken flocks.

Serum samples from 75 Ohio layer flocks were tested for antibodies to infectious bursal disease virus (IBDV) serotypes I and II using a virus-neutralization test. Infectious bursal disease had been diagnosed in three of the 75 flocks. Antibody titers to serotype I were detected in 77% of the flocks, and antibody titers to serotype II were detected in 47% of the flocks. Of the eight flocks known to have been vaccinated using a serotype I IBDV vaccine, all had antibody titers to serotype I, and four had antibody titers to serotype II. Eleven of 17 known unvaccinated flocks had antibodies to serotype I, and seven had antibodies to serotype II.

Animals↗
PubMed2001

Competitive exclusion against Salmonella gallinarum of Salmonella enteritidis infected chickens.

To evaluate the degree of competitive exclusion against Salmonella gallinarum(S. gallinarum) of Salmonella enteritidis(S. enteritidis) infected chickens, fifty-six, 4-week old Hyline layer suspected of S. enteritidis infection were challenged with S. gallinarum. All chickens were tested for S. enteritidis isolation using cloacal swabs and serum plate agglutination test using S. enteritidis Ag. before challenge and classified into four groups(SE isolated, SE nonisolated, SE seropositive and SE seronegative). None of the SE isolated and the SE seropositive groups died after challenge and the average weight gains were 245.5g and 254.6g, respectively. But in the SE nonisolated and the SE seronegative groups, mortality was 18.2% and 20.6% and the average weight gains were 150.1g and 111.2g. The incidence of reisolation of S. gallinarum of the SE isolated and the SE seropositive groups were 41.7% and 47.6% from liver, 33.3% and 47.6% from spleen and 8.3% and 14.3% from cecum, respectively, and the SE nonisolated and the SE seronegative group were 63.6% and 64.7% from liver, 84.1% and 88.2% from spleen and 47.7% and 52.9% from cecum. The serological response of the SE isolated and the SE seropositive groups hardly changed from 75.0 and 81.8% before challenge to 75.0 and 85.7% after. But, the other two groups were found to be significantly higher after challenge and increased from 0 and 18.2% to 100%. Consequently, S. enteritidis preinfected chickens were found to be significant different in terms of mortality, weight gain, reisolation of S. gallinarum and serological response compared to noninfected chickens. Moreover, our study shows that S. enteritidis infected chickens appear strong competitive exclusion against the colonization of S. gallinarum.

Animals↗
PubMed1992

Contractile proteins in the hyaline cells of the chicken cochlea.

Hyaline cells are a single layer of epithelial cells found at the inferior edge of the sensory epithelium in the chick cochlea. They rest directly above a specialized region of the basilar membrane at a point where it connects to the fibrocartilaginous skeleton of the cochlear duct. The basal cytoplasm of the hyaline cells contains a bundle of linearly aligned actin filaments that resemble stress fibers in their organization. The actin filaments are anchored in the basal plasma membranes of the cells, which are, in turn, associated with the underlying basal lamina and the extracellular matrix of the basilar membrane. We have used a combination of transmission electron microscopy, differential-interference-contrast and epifluorescence light microscopy, and confocal laser scanning microscopy to study the composition and organization of these actin bundles within the hyaline cells. The bundles are arranged into triangular wedges that are oriented radially across the basilar membrane. Each cell contains one or two actin wedges. Adjacent cells can have them aligned in opposite directions so that in a whole-mount surface preparation they appear as interdigitations. Immunofluorescent staining of the hyaline cells has shown that smooth muscle myosin and alpha-actinin are co-localized to the actin bundles. Smooth muscle myosin is also found throughout the cytoplasm of the cells. The fact that hyaline cells in the chick cochlea are contacted by efferent nerve fibers suggests that these cells may regulate tension on the basilar membrane via the specialized bundle of actin filaments.

Animals↗