scholarly journals Localization of an endogenous lectin in chicken liver, intestine, and pancreas.

1979 ◽  
Vol 82 (2) ◽  
pp. 565-571 ◽  
Author(s):  
E C Beyer ◽  
K T Tokuyasu ◽  
S H Barondes
Keyword(s):  
Goblet Cells ◽  
Chicken Liver ◽  
Embryonic Chick ◽  
Adult Chicken ◽  
Pancreatic Acini ◽  
Adult Muscle ◽  
Endogenous Lectin ◽  
Liver Sinusoids ◽  
Different Tissues ◽  
In Cells

Extracts of adult chicken liver, pancreas, and intestine contain high levels of a lectin which appears to be identical to one previously purified from embryonic chick muscle. This lectin is virtually absent from adult muscle, but is highly concentrated in cells lining liver sinusoids, intestinal goblet cells, and the extracellular spaces surrounding pancreatic acini. These findings suggest that the lectin may play different roles in different tissues and at different times in the life of a chicken.

Expression of the growth hormone receptor gene in chicken pituitary glands

1992 ◽  
Vol 135 (3) ◽  
pp. 459-468 ◽  
Author(s):  
K. L. Hull ◽  
R. A. Fraser ◽  
S. Harvey
Keyword(s):  
Growth Hormone Receptor ◽  
Receptor Gene ◽  
Cell Types ◽  
Chicken Liver ◽  
Adult Chicken ◽  
Oligonucleotide Primers ◽  
Receptor Mrna ◽  
Gh Receptor ◽  
Pituitary Glands ◽  
Growth Hormone Receptor Gene

ABSTRACT Although GH has no direct effect on GH release from chicken pituitary glands, GH receptor mRNA similar to that in the rabbit liver was identified by Northern blot analysis in extracts of adult chicken pituitaries. Complementary (c) DNA, reverse transcribed from chicken pituitary RNA, was amplified by the polymerase chain reaction (PCR) in the presence of 3′- and 5′-oligonucleotide primers coding for the extracellular domain of the chicken liver GH receptor and was found to contain an electrophoretically separable fragment of 500 bp, identical in size to that in chicken liver. Digestion of this pituitary cDNA with NcoI produced expected moities of 350 and 150 bp. Amplification of chicken pituitary cDNA in the presence of oligonucleotide primers for the intracellular sequence of the chicken liver GH receptor produced an electrophoretically separable fragment of approximately 800 bp, similar to that in chicken liver. This fragment was cut into expected moieties of 530 and 275 bp after digestion with EcoRI. These PCR fragments were identified in extracts of the pituitary caudal lobe, in which somatotrophs are confined and account for the majority of endocrine cell types, and in the cephalic lobe, in which somatotrophs are lacking. Translation of the GH receptor mRNA in the pituitary gland was indicated by the qualitative demonstration of radio-labelled GH-binding sites in plasma membrane preparations, in pituitary cytosol and in nuclear membranes. These results provide evidence for the expression and translation of the GH receptor gene in pituitary tissue, in which GH receptors appear to be widely distributed within cells and in different cell types. GH may therefore have paracrine, autocrine or intracrine effects on pituitary function. Journal of Endocrinology (1992) 135, 459–468

Ribosome Crystals in Necrotizing Cells from the Posterior Necrotic Zone of the Developing Chick Limb

1972 ◽  
Vol 11 (2) ◽  
pp. 403-414
Author(s):  
N. K. MOTTET ◽  
S. P. HAMMAR
Keyword(s):  
Electron Micrographs ◽  
Protein Crystals ◽  
Embryonic Chick ◽  
3 Dimensional ◽  
Surface Lattice ◽  
Plane Group ◽  
High Doses ◽  
In Cells

Ribosome and ‘protein crystals" were observed in electron micrographs of degenerating cells from the posterior necrotic zone (PNZ) of developing chick limbs, stages 22 through 24. Ribosome crystals were made up of basic units of 4 ribosomes arranged in a square tetramer. They were monomorphic with the surface lattice being of the p4 plane group. The 1-ribosome-thick sheets of crystals were often seen stacked upon one another forming a 3-dimensional P422 configuration. The percentage of crystallized ribosomes within degenerating PNZ cells is nearly directly proportional to the degree of degeneration of the cell. Crystals identical to this have been observed in numerous types of embryonic chick cells subjected to hypothermia. The ‘protein crystals’ were composed of straight filamentous structures separated by a distance of 20-30 nm. They were always closely associated with the ribosome crystals. These crystals are similar to those seen in cells treated with high doses of vinblastine and vincristine. The pathogenesis of the ribosome and protein crystals occurring in degenerating PNZ cells is unknown. They are not associated in any way with hypothermia or vinblastine-vincristine treatment.

scholarly journals Expression of intermediate filament-associated proteins paranemin and synemin in chicken development.

1983 ◽  
Vol 97 (6) ◽  
pp. 1860-1874 ◽  
Author(s):  
M G Price ◽  
E Lazarides
Keyword(s):  
Smooth Muscle ◽  
Intermediate Filament ◽  
Muscle Cells ◽  
Myocardial Cells ◽  
Adult Chicken ◽  
Intermediate Filament Proteins ◽  
Adult Muscle ◽  
Associated Proteins ◽  
Visceral Smooth Muscle ◽  
Chicken Development

The expression of two intermediate filament-associated proteins, paranemin (280,000 mol wt) and synemin (230,000 mol wt), was investigated with respect to the expression of two core intermediate filament proteins, desmin and vimentin, in various embryonic and adult chicken muscle and nonmuscle cells. All developing muscle cells, regardless of their type, simultaneously express desmin, vimentin, paranemin, and synemin. However, a difference is observed in the expression of paranemin in adult muscle. This protein is removed during differentiation of both fast and slow skeletal muscle, visceral smooth muscle, and the smooth muscle of muscular arteries, but remains in mature myocardial cells, cardiac conducting fibers, and the smooth muscle cells of elastic arteries. Some of these cells express vimentin, others desmin, and still others a mixture of the two. On the other hand, synemin is expressed in all the above types of adult muscle cells except myocardial cells. Adult myocardial cells also lack vimentin, and its presence is gradually reduced after hatching. Since in adult striated muscle all expressed intermediate filament proteins are found predominantly in association with the peripheries of myofibrillar Z discs, these results suggest that a change in the composition of skeletal and cardiac muscle Z discs occurs during chicken development and maturation. Erythrocytes that express synemin and vimentin do not express paranemin, while both embryonic and adult Schwann cells co-express paranemin and vimentin, but not synemin. Endothelial cells of muscular vessels express paranemin, while those of elastic vessels do not, and neither contains synemin. Paranemin and synemin are not expressed in neurons, epithelial, and most glial cells, suggesting that these two polypeptides are expressed only in conjunction with desmin or vimentin. These results suggest that the composition of intermediate filaments changes during chicken development, not only with respect to their core subunit proteins but also with respect to two associated polypeptides, particularly in muscle cells.

Identification of microRNAs from different tissues of chicken embryo and adult chicken

FEBS Letters ◽  
2006 ◽  
Vol 580 (15) ◽  
pp. 3610-3616 ◽  
Author(s):  
Hongtao Xu ◽  
Xiaobo Wang ◽  
Zhenglin Du ◽  
Ning Li
Keyword(s):  
Chicken Embryo ◽  
Adult Chicken ◽  
Different Tissues

scholarly journals Detection of desmin-containing intermediate filaments in cultured muscle and nonmuscle cells by immunoelectron microscopy.

1983 ◽  
Vol 96 (2) ◽  
pp. 401-408 ◽  
Author(s):  
W Ip ◽  
S I Danto ◽  
D A Fischman
Keyword(s):  
Intermediate Filaments ◽  
Polyacrylamide Gel Electrophoresis ◽  
Heart Cell ◽  
Embryonic Chick ◽  
Adult Chicken ◽  
Nonmuscle Cells ◽  
Chick Heart ◽  
Embryonic Chick Heart ◽  
Triton X ◽  
Fibroblastic Cells

Antibodies raised against chicken gizzard smooth muscle desmin were shown to be specific by immunofluorescence cytochemistry and immunoautoradiography after two-dimensional polyacrylamide gel electrophoresis. Embryonic chick heart cell cultures (permeabilized with Triton X-100) and enucleated adult chicken erythrocyte ghosts (Granger, B. L., E. A. Rapasky, and E. Lazarides, 1982, J. Cell Biol. 92:299-312) were then used for immunoelectronmicroscopic localization of desmin. As expected, all intermediate filaments (IF) of the cardiac myocytes were labeled heavily and uniformly with the desmin antibodies. No periodicity or helicity was detectable along the labeled IF. Of interest was the intermittent but clear labeling of the IF of the nonmuscle, fibroblastic cells in the identical cultures. These antibodies did not bind vimentin from embryonic chick heart homogenates; furthermore, they did not label IF of avian erythrocytes known to contain vimentin but not desmin. We conclude that IF of cardiac fibroblastic cells contain low, but significant, concentrations of desmin and that this protein probably forms a copolymer with vimentin in these cells.

scholarly journals Troponin in embryonic chick skeletal muscle cells in vitro. An immunoelectron microscope study.

1979 ◽  
Vol 81 (1) ◽  
pp. 59-66 ◽  
Author(s):  
T Obinata ◽  
Y Shimada ◽  
R Matsuda
Keyword(s):  
Skeletal Muscle ◽  
Troponin T ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Regulatory Proteins ◽  
Embryonic Chick ◽  
Thin Filaments ◽  
Adult Chicken ◽  
Chicken Muscles

The fine structurel distribution of troponin on thin filaments in developing myofibrils was investigated by the use of immunoelectron microscopy. Embryonic chick skeletal muscle cells grown in vitro were treated with antibodies against each of the troponin components (troponin T, I, and C) from adult chicken muscles. Each antibody was distributed along the thin filaments with a period of 38 nm. It is concluded that these newly synthesized regulatory proteins are assembled at their characteristic position from the initial phases of myofibrillogenesis.

scholarly journals Comet assay study of the genotoxic effect of T-2 and HT-2 toxins in chicken hepatocytes

2019 ◽  
Vol 70 (4) ◽  
pp. 330-335
Author(s):  
Rubina Tu¨nde Szabó ◽  
Mária Kovács-Weber ◽  
Márta Erdélyi ◽  
Krisztián Balogh ◽  
Natasa Fazekas ◽  
...  
Keyword(s):  
Dna Damage ◽  
Comet Assay ◽  
Broiler Chickens ◽  
Treated Group ◽  
Chicken Liver ◽  
Control Group ◽  
Visual Evaluation ◽  
Method Of Evaluation ◽  
Different Tissues ◽  
Primary Dna Damage

Background and aims The aim of this study was to verify that the comet assay can be used to investigate the DNA damaging effects of T-2 and HT-2 toxins in the liver of broiler chickens. The comet assay is a favorable genotoxic analysis because it is cheap, simple, and can be used in many organisms and different tissues. Materials and methods Male broiler chickens were fed with T-2/HT-2 toxins-contaminated diet for 14 days. The comet assay was successfully adapted to chicken liver cells, and the DNA damage was determined by a decrease in the comet parameter (DNA % in the tail) in the experimental groups. Results The method of evaluation was found to be critical because DNA damage could not be detected exactly using the CometScore software, due to inaccurate separation of head and comet. However, this problem can be solved by visual evaluation. Conclusion In the case of the visual evaluation, each toxin-treated group differed significantly from the control group, indicating that the assay can be useful for the assessment of primary DNA damage caused by T-2/HT-2 toxins.

scholarly journals Changes in the nuclear polyamine content of chick erythrocytes during embryonic development

1979 ◽  
Vol 184 (3) ◽  
pp. 607-612 ◽  
Author(s):  
M H Goyns
Keyword(s):  
Embryonic Development ◽  
Metabolic Activity ◽  
Embryonic Chick ◽  
Polyamine Content ◽  
In Cells

The polyamine content of the circulating erythrocyte population in the embryonic chick was studied during its development. Total cellular polyamine content fell dramatically between 5 and 7 days of development, paralleling the decrease in metabolic activity exhibited by these cells. Nuclei were isolated from the erythrocytes by a non-aqueous technique, which not only eliminated the polyamine loss that occurred with aqueous isolation, but also prevented redistribution of the polyamines from the cytoplasm. Nuclear spermidine and spermine contents decreased markedly between 5 and 6 days of development from 31 to 10 pmol/microgram of DNA and from 33 to 18 pmol/microgram of DNA respectively. Thereafter the spermine content remained constant, but the spermidine content continued to decline. Good correlations between spermidine and RNA contents were observed in both cells and nuclei, and similarly between spermine and RNA contents in cells, but no such correlation was observed between spermine and RNA in nuclei.

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