The neuromuscular spindles in the adult chicken

1967 ◽  
Vol 67 (4) ◽  
pp. 595-608 ◽  
Author(s):  
Antonieta Rebollo ◽  
Griselda De Anda
1967 ◽  
Vol 67 (3) ◽  
pp. 437-451 ◽  
Author(s):  
Griselda de Anda ◽  
María Antonieta Rebollo

1969 ◽  
Vol 129 (3) ◽  
pp. 459-467 ◽  
Author(s):  
Norman W. Nisbet ◽  
Morten Simonsen ◽  
Marek Zaleski

Graft-vs.-host (GVH) reactions were performed in chicken embryos by intravenous injection of adult chicken blood dilutions, and the result was scored by weighing the spleens as well as by karyological identification of host and donor metaphases. From the frequency of detectable signs of GVH reaction when low doses of donor cells were injected into hosts containing one foreign allele of the B locus it is concluded that 1–2% must be a minimum estimate for the frequency of antigen-sensitive cells of a given specificity in this system. It is not found possible to reconcile the findings with the strictest form of clonal selection which postulates a single receptor specificity per clone of antigen-sensitive cells.


1992 ◽  
Vol 135 (3) ◽  
pp. 459-468 ◽  
Author(s):  
K. L. Hull ◽  
R. A. Fraser ◽  
S. Harvey

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


1991 ◽  
Vol 11 (9) ◽  
pp. 4690-4697 ◽  
Author(s):  
J G Glauber ◽  
N J Wandersee ◽  
J A Little ◽  
G D Ginder

A stable transfection assay was used to test the mechanism by which embryonic globin gene transcription is stimulated in adult erythroid cells exposed to butyric acid and its analogs. To test the appropriate expression and inducibility of chicken globin genes in murine erythroleukemia (MEL) cells, an adult chicken beta-globin gene construct was stably transfected. The chicken beta-globin gene was found to be coregulated with the endogenous adult mouse alpha-globin gene following induction of erythroid differentiation of the transfected MEL cells by incubation with either 2% dimethyl sulfoxide (DMSO) or 1 mM sodium butyrate (NaB). In contrast, a stably transfected embryonic chicken beta-type globin gene, rho, was downregulated during DMSO-induced MEL cell differentiation. However, incubation with NaB, which induces MEL cell differentiation, or alpha-amino butyrate, which does not induce differentiation of MEL cells, resulted in markedly increased levels of transcription from the stably transfected rho gene. Analysis of histone modification showed that induction of rho gene expression was not correlated with increased bulk histone acetylation. A region of 5'-flanking sequence extending from -569 to -725 bp upstream of the rho gene cap site was found to be required for both downregulation of rho gene expression during DMSO-induced differentiation and upregulation by treatment with NaB or alpha-amino butyrate. These data are support for a novel mechanism by which butyrate compounds can alter cellular gene expression through specific DNA sequences. The results reported here are also evidence that 5'-flanking sequences are involved in the suppression of embryonic globin gene expression in terminally differentiated adult erythroid cells.


1987 ◽  
Vol 14 (1) ◽  
pp. 49-61 ◽  
Author(s):  
Roger K.R. Thompson ◽  
Mark Liebreich

2011 ◽  
Vol 14 (3) ◽  
pp. 218-223 ◽  
Author(s):  
Martine Sinico ◽  
Guillaume Bassez ◽  
Claudine Touboul ◽  
Helene Cavé ◽  
Armand Vergnaud ◽  
...  

1982 ◽  
Vol 92 (1) ◽  
pp. 23-27 ◽  
Author(s):  
E C Beyer ◽  
S H Barondes

Two lactose-binding lectins from chicken tissues, chicken-lactose-lectin-1 (CLL-1) and chicken-lactose-lectin-11 (CLL-11) were quantified with a radioimmunoassay in extracts of a number of developing and adult chicken tissues. Both lectins could be measured in the same extract without separation, because they showed not significant immunological cross-reactivity. Many embryonic and adult tissues, including brain, heart, intestine, kidney, liver, lung, muscle, pancreas, and spleen, contained one or both lectins, although their concentrations differed markedly. For example, embryonic muscle, the richest source of CLL-1 contained only traces of CLL-11 whereas embryonic kidney, a very rich source of CLL-11 contained substantial CLL-1. In both muscle and kidney, lectin levels in adulthood were much lower than in the embryonic state. In contrast, CLL-1 in liver and CLL-11 in intestine were 10-fold to 30-fold more concentrated in the adult than in the 15-d embryo. CLL-1 and CLL-11 from several tissues were purified by affinity chromatography and their identity in the various tissues was confirmed by polyacrylamide gel electrophoresis, isoelectric focusing, and peptide mapping. The results suggest that these lectins might have different functions in the many developing and adult tissues in which they are found.


Development ◽  
1970 ◽  
Vol 24 (1) ◽  
pp. 13-20
Author(s):  
C. E. Grossi ◽  
P. Carinci ◽  
L. Manzoli-Guidotti

By means of immunochemical techniques, the protein components of the water-soluble fraction (WSF) of the egg yolk have been examined in the unincubated egg and during incubation. Anti-ovalbumin and anti-total adult chicken serum antisera have been employed. Ovalbumin can be detected in the unincubated WSF as well as during incubation; its concentration seems to increase during incubation. In the WSF of the unincubated egg, six proteins immunologically related to adult serum proteins can be detected. They correspond to α-livetin, α1-globulin, β-livetin, ovotransferrin (conalbumin) and γ-livetin (two components). β-Livetin disappears after the 14th day of incubation while the other components can be demonstrated till hatching. The findings are discussed in relation to the data available in the literature. The findings are discussed in relation to the data available in the literature.


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