Localization of mRNA for the β-subunit of placental hCG by in situ hybridization

1988 ◽  
Vol 119 (1) ◽  
pp. 69-74 ◽  
Author(s):  
Mariann Wide ◽  
Håkan Persson ◽  
Örjan Lundkvist ◽  
Leif Wide
Keyword(s):  
In Situ Hybridization ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Background Noise ◽  
Placental Tissue ◽  
Β Subunit ◽  
Chorionic Villi ◽  
Cellular Origin ◽  
Β Hcg

Abstract. The cellular origin of placental hCG is not yet completely established. Depending on the method used, the syncytium, cytotrophoblast or both types of tissue have been claimed to synthesize hCG. In the present study in situ hybridization was used on sections of chorionic villi in order to detect expression of the gene for the β-subunit of hCG (β-hCG). Placental tissue was obtained from the 8th to the 11th weeks of pregnancy, when the concentration of hCG is high. A cDNA clone, encoding the entire amino acid sequence of β-hCG, was used as a probe. Hybrids of β-hCG cDNA/mRNA were found only over the syncytiotrophoblast. Background noise was extremely low and no signals above that were detected in the cytotrophoblast cells. It is concluded that at this stage of pregnancy the gene for β-hCG is activated in the syncytial parts of chorionic villi and not in the cytotrophoblast.

scholarly journals Drosophila laminin: sequence of B2 subunit and expression of all three subunits during embryogenesis.

1989 ◽  
Vol 109 (5) ◽  
pp. 2441-2453 ◽  
Author(s):  
D J Montell ◽  
C S Goodman
Keyword(s):  
Nervous System ◽  
In Situ Hybridization ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Sequence ◽  
Drosophila Embryogenesis ◽  
Substrate Adhesion ◽  
Genes Encoding ◽  
Developing Nervous System

In a previous study, we described the cloning of the genes encoding the three subunits of Drosophila laminin, a substrate adhesion molecule, and the cDNA sequence of the B1 subunit (Montell and Goodman, 1988). This analysis revealed the similarity of Drosophila laminin with the mouse and human complexes in subunit composition, domain structure, and amino acid sequence. In this paper, we report the deduced amino acid sequence of the B2 subunit. We then describe the expression and tissue distribution of the three subunits of laminin during Drosophila embryogenesis using both in situ hybridization and immunolocalization techniques, with particular emphasis on its expression in and around the developing nervous system.

A simple in situ cyanogen bromide cleavage method to obtain internal amino acid sequence of proteins electroblotted to polyvinyldifluoride membranes

1988 ◽  
Vol 155 (3) ◽  
pp. 1353-1359 ◽  
Author(s):  
Mitchell G. Scott ◽  
Daniel L. Crimmins ◽  
David W. McCourt ◽  
Jeffrey J. Tarrand ◽  
Margaret C. Eyerman ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Internal Amino Acid Sequence ◽  
Cleavage Method

scholarly journals Tissue Expression of the S100 Protein Family-related MRP8 Gene in Human Chorionic Villi by in situ Hybridization Techniques

1999 ◽  
Vol 76 (2-3) ◽  
pp. 123-129 ◽  
Author(s):  
Noriaki SATO ◽  
Kazuhiro ISONO ◽  
Isamu ISHIWATA ◽  
Mitsuo NAKAI ◽  
Koji KAMI
Keyword(s):  
In Situ Hybridization ◽  
S100 Protein ◽  
Tissue Expression ◽  
Protein Family ◽  
Chorionic Villi

scholarly journals Nephrocystin

2000 ◽  
Vol 11 (2) ◽  
pp. 270-282
Author(s):  
EDGAR OTTO ◽  
ANDREAS KISPERT ◽  
SILVIA SCHÄTZLE ◽  
BIRGIT LESCHER ◽  
CORNELIA RENSING ◽  
...  
Keyword(s):  
Amino Acid ◽  
Caenorhabditis Elegans ◽  
Amino Acid Sequence ◽  
Protein Interaction ◽  
Tissue Expression ◽  
Sequence Conservation ◽  
Cystic Kidney ◽  
Protein Protein Interaction ◽  
Amino Acid Sequence Conservation

Juvenile nephronophthisis, an autosomal recessive cystic kidney disease, is the primary genetic cause for chronic renal failure in children. The gene (NPHP 1) for nephronophthisis type 1 has recently been identified. Its gene product, nephrocystin, is a novel protein of unknown function, which contains a src-homology 3 domain. To study tissue expression and analyze amino acid sequence conservation of nephrocystin, the full-length murine Nphp 1 cDNA sequence was obtained and Northern and in situ hybridization analyses were performed for extensive expression studies. The results demonstrate widespread but relatively weak NPHP 1 expression in the human adult. In the adult mouse there is strong expression in testis. This expression occurs specifically in cell stages of the first meiotic division and thereafter. In situ hybridization to whole mouse embryos demonstrated widespread and uniform expression at all developmental stages. Amino acid sequence conservation studies in human, mouse, and Caenorhabditis elegans show that in nephrocystin the src-homology 3 domain is embedded in a novel context of other putative domains of protein-protein interaction, such as coiled-coil and E-rich domains. It is concluded that for multiple putative protein-protein interaction domains of nephrocystin, sequence conservation dates back at least to Caenorhabditis elegans. The previously described discrepancy between widespread tissue expression and the restriction of symptoms to the kidney has now been confirmed by an in-depth expression study.

scholarly journals Cloning and hypothalamic distribution of the chicken thyrotropin-releasing hormone precursor cDNA

2005 ◽  
Vol 186 (2) ◽  
pp. 387-396 ◽  
Author(s):  
Kristien Vandenborne ◽  
Simon A Roelens ◽  
Veerle M Darras ◽  
Eduard R Kühn ◽  
Serge Van der Geyten
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Sequence ◽  
Chicken Genome ◽  
Amino Acid Sequence Homology ◽  
Tertiary Structures ◽  
Genome Database ◽  
Releasing Hormone ◽  
Translation Start

In this paper we report the cloning of the chicken preprothyrotropin-releasing hormone (TRH) cDNA and the study of its hypothalamic distribution. Chicken pre-proTRH contains five exact copies of the TRH progenitor sequence (Glu-His-Pro-Gly) of which only four are flanked by pairs of basic amino acids. In addition, the amino acid sequence contains three sequences that resemble the TRH progenitor sequence but seem to have lost their TRH-coding function during vertebrate evolution. The amino acid sequence homology of preproTRH between different species is very low. Nevertheless, when the tertiary structures are compared using hydrophobicity plots, the resemblance between chicken and rat prepro-TRH is striking. The cloning results also showed that the chicken preproTRH sequence includes neither a rat peptide spacer 4 (Ps4) nor a Ps5 connecting peptide. Comparison of the cDNA sequence with the chicken genome database revealed the presence of two introns, one in the 5′ untranslated region, and another downstream from the translation start site. This means that the gene structure of chicken preproTRH resembles the gene stucture of this precursor in mammals. Based on the cDNA sequence, digoxigenin-labelled probes were produced to study the distribution of preproTRH in the chicken brain. By means of in situ hybridization, preproTRH mRNA was detected in the chicken paraventricular nucleus (PVN) and in the lateral hypothalamus (LHy).

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