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).

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.

cDNA Sequence and Deduced Amino Acid Sequence of a Fungal Stress Protein Induced inRhizopus nigricansby Steroids

1998 ◽  
Vol 250 (3) ◽  
pp. 664-667 ◽  
Author(s):  
Bronislava Črešnar ◽  
Andreja Plaper ◽  
Katja Breskvar ◽  
Tamara Hudnik-Plevnik
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Sequence ◽  
Stress Protein

scholarly journals Intracellular Retention of the Corticotrophin-releasing Hormone (CRH) Precursor Within COS-7 Cells

1998 ◽  
Vol 46 (10) ◽  
pp. 1193-1197 ◽  
Author(s):  
Marcelo J. Perone ◽  
Simon Windeatt ◽  
Ewan Morrison ◽  
Andy Shering ◽  
Peter Tomasec ◽  
...  
Keyword(s):  
Amino Acid ◽  
Golgi Apparatus ◽  
Amino Acid Sequence ◽  
Protein Secretion ◽  
Intracellular Trafficking ◽  
Secretory Pathway ◽  
Intracellular Localization ◽  
Primary Amino Acid Sequence ◽  
Releasing Hormone ◽  
Primary Amino

We investigated the intracellular localization of CRH in transiently transfected COS-7 cells expressing the full-length rat corticotropin-releasing hormone (CRH) precursor cDNA. CRH synthesized by transfected COS-7 cells is mainly stored intracellularly. In contrast, CHO-K1 cells expressing the same CRH precursor stored and released equal amounts of immunoreactive (IR)-CRH. Ultrastructural analysis revealed that CRH is stored in electron-dense aggregates in the RER of transiently transfected COS-7 cells and does not migrate into the Golgi apparatus. On the basis of the different intracellular localization, storage, and release of CRH in COS-7 and CHO-K1 cells, we hypothesize that the intracellular trafficking of CRH within the constitutive secretory pathway for protein secretion not only depends on its primary amino acid sequence but might also be influenced by intracellular conditions or factors.

scholarly journals cDNA Cloning and Partial Characterization of the DJ-1 Gene from Tribolium castaneum

Antioxidants ◽  
2021 ◽  
Vol 10 (12) ◽  
pp. 1970
Author(s):  
Shunya Sasaki ◽  
Maaya Nishiko ◽  
Takuma Sakamoto ◽  
Michael R. Kanost ◽  
Hiroko Tabunoki
Keyword(s):  
Oxidative Stress ◽  
Amino Acid ◽  
Tribolium Castaneum ◽  
Cdna Sequence ◽  
Developmental Stages ◽  
Red Flour Beetle ◽  
Genome Database ◽  
Antioxidant Function ◽  
Increased Sensitivity

The DJ-1 gene is highly conserved across a wide variety of organisms and it plays a role in anti-oxidative stress mechanisms in cells. The red flour beetle, Tribolium castaneum, is widely used as a model insect species because it is easy to evaluate gene function in this species using RNA interference (RNAi). The T. castaneum DJ-1 (TcDJ-1) sequence is annotated in the T. castaneum genome database; however, the function and characteristics of the TcDJ-1 gene have not been elucidated. Here, we investigated the cDNA sequence of TcDJ-1 and partially characterized its function. First, we examined the TcDJ-1 amino acid sequence and found that it was highly conserved with sequences from other species. TcDJ-1 mRNA expression was higher in the early pupal and adult developmental stages. We evaluated oxidant tolerance in TcDJ-1 knockdown adults using paraquat and found that adults with TcDJ-1 knockdown exhibited increased sensitivity to paraquat. Our findings show that TcDJ-1 has an antioxidant function, as observed for DJ-1 from other insects. Therefore, these results suggest that TcDJ-1 protects against oxidative stress during metamorphosis.

scholarly journals Biochemical characterization of a second family of human Ia molecules, HLA-DS, equivalent to murine I-A subregion molecules.

1982 ◽  
Vol 156 (2) ◽  
pp. 550-566 ◽  
Author(s):  
S M Goyert ◽  
J E Shively ◽  
J Silver
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Sequence Identity ◽  
Biochemical Characterization ◽  
Amino Acid Sequence Homology ◽  
Molecular Weights ◽  
Hla Dr ◽  
D Region ◽  
Polypeptide Chains

In mice, two families of structurally distinct Ia molecules, one designated I-A and the other I-E, have been identified and characterized. The HLA-DR molecules represent one family of human Ia molecules equivalent to the murine I-E molecules on the basis of amino acid sequence homology. We describe the isolation and biochemical characterization of a second family of human Ia molecules, designated HLA-DS for second D-region locus, equivalent to the murine I-A molecules. The human HLA-DS molecules consist of two polypeptide chains, DS alpha (37,000 mol wt) and DS beta (29,000 mol wt), with 73% amino acid sequence identity to the murine I-A molecules. Furthermore, the HLA-DS molecules are closely linked genetically to HLA-DR molecules, a situation analogous to that observed in mice. The similarity in molecular weights of the DR and DS molecules might explain why others have failed to identify the latter in man.

scholarly journals The amino acid sequence of a glutamic acid-rich protein from bovine retina as deduced from the cDNA sequence.

1991 ◽  
Vol 88 (8) ◽  
pp. 3116-3119 ◽  
Author(s):  
Y. Sugimoto ◽  
K. Yatsunami ◽  
M. Tsujimoto ◽  
H. G. Khorana ◽  
A. Ichikawa
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Glutamic Acid ◽  
Cdna Sequence ◽  
Bovine Retina

scholarly journals Cloning of glycoprotein IIIa cDNA from human erythroleukemia cells and localization of the gene to chromosome 17

Blood ◽  
1988 ◽  
Vol 72 (2) ◽  
pp. 593-600 ◽  
Author(s):  
JP Rosa ◽  
PF Bray ◽  
O Gayet ◽  
GI Johnston ◽  
RG Cook ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Sequence ◽  
Chromosome 17 ◽  
Coding Region ◽  
Membrane Glycoproteins ◽  
Cdna Sequences ◽  
Hel Cells ◽  
Adhesive Proteins

Abstract Platelet aggregation requires the binding of adhesive proteins such as fibrinogen to the heterodimer of membrane glycoproteins IIb (GPIIb) and IIIa (GPIIIa). Human erythroleukemia (HEL) cells synthesize both GPIIb and GPIIIa. Using poly(A+) RNA purified from HEL cells, we constructed a cDNA library in the lambda gt10 phage vector. This library was screened with a 38mer oligonucleotide derived from a platelet GPIIIa peptide, and three overlapping cDNAs were isolated. The three inserts encompassed 3.5 kilobases (kb), including the entire coding region of mature GPIIIa (2,286 basepairs, bp) and 1.3 kb of 3′ untranslated sequence. All 222 residues determined directly from platelet GPIIIa tryptic peptides exactly matched the HEL cell-deduced amino acid sequence. The HEL cell sequence matched a previously reported endothelial cell cDNA sequence except for eight nucleotides. Five of these nucleotide differences were silent changes consistent with genetic polymorphisms. The other three differences resulted in changes in the deduced amino acid sequence of GPIIIa; reexamination of the endothelial cell cDNA sequence in these three areas revealed that it is actually identical to the HEL cell sequence. The virtual identity of the endothelial and HEL cell cDNA sequences provides direct evidence that GPIIIa is a subunit common to cell-adhesion receptors present in more than one cell type. We localized the gene for GPIIIa to chromosome 17, the same chromosome to which we had previously mapped the gene for GPIIb.

scholarly journals Amino acid sequence of flounder growth hormone deduced from a cDNA sequence

1988 ◽  
Vol 16 (21) ◽  
pp. 10362-10362 ◽  
Author(s):  
Hiroshi Momota ◽  
Ryo Kosugi ◽  
Hideo Ohgai ◽  
Akihiko Hara ◽  
Hiroko Ishioka
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Sequence
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