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- Institut für Anatomie und Zellbiologie (165) (remove)
Sonstige beteiligte Institutionen
- Naturalis Biodiversity Centre (2)
- Department of Biomedical Imaging, National Cerebral and Cardiovascular Research Center, Suita, Japan (1)
- Division of Medical Technology and Science, Department of Medical Physics and Engineering, Course of Health Science, Osaka University Graduate School of Medicine, Suita Japan (1)
- Institut for Molecular Biology and CMBI, Department of Genomics, Stem Cell Biology and Regenerative Medicine, Leopold-Franzens-University Innsbruck, Innsbruck, Austria (1)
- Johns Hopkins School of Medicine (1)
- Johns Hopkins School of Medicine, The Russell H Morgan Department of Radiology and Radiological Science, Baltimore, MD, USA (1)
The gene encoding the human homologue of the guinea pig uterine bombesm receptor [( 1992) Eur. J. Biochem. 208,405] was isolated from a genomic lambda library by the PCR/homology screening approach. The gene spans more than 4 kb and consists of 3 exons and 2 introns. The deduced amino acid sequence shows about 86% identity to that of guinea pig bombesin receptor. This subtype of bombesin receptor is expressed in the pregnant uterus and in two human tumour cell lines, T47D (ductal breast carcinoma) and A431 (epidermal carcinoma). PCR analysis of genomic DNA from human-mouse cell hybrids allows the cloned gene to be localized to the region q26q28 on chromosome X.
A cDNA encoding guinea-pig uterine substance P (SP) receptor has been isolated using the homology screening approach. Northern blot analysis reveals that the corresponding mRNA, of approx. 4.8 kb, is expressed in all tissues tested, but predominantly in the uteri of non-pregnant animals; during pregnancy its expression is reduced. The guinea-pig SP receptor was expressed in COS-7 cells and demonstrated relative Iigand affinity in the order: SP >> neurokinin A > neurokinin B.
The homology screening approach has been used to clone a new member of the guanine-nucleotidebinding-protein-coupled receptor superfamily from guinea pig uterus. The cloned cDNA encodes a 399-amino-acid protein and shows the highest amino acid similarity to members of the bombesin receptor family; 52% and 47% similarity to the gastrin-releasing-peptide (GRP) receptor and the neuromedin-B receptor, respectively. Bindingexperiments with the stably transfected LLC-PK<sub>1</sub> cell line expressing the new receptor protein confmned the bombesin-like nature of the cloned receptor. The relative order ofligand affinity, GRP = neuromedin C >> neuromedin B, suggests that the cloned cDNA represents the GRP subtype rather than the neuromedin-B subtype of bombesin receptors. Northern-blot analysis of mRNA species from several guinea-pig tissues showed that the mRNA for the new bombesin receptor subtype is expressed mainly in uteri of pregnant animals.
A recombinant plasmid was constructed containing the gene for bovine growth hormone joinea with the regulatory region and the region coding the signal sequence of the Escherichia coli alkaline phosphatase gene. In conditions of phosphorus starvation, which c~s derepression of alkaline phosphatase, expression was shown of the gene for bovine growth hormone, in addition to partial processing and secretion of protein into periplasm.
Results are presented of cloning cDNA of procine growth hormone, analysis of its primary structure, and creation of a construction capable of expression of this cDNA in Esqheriahia coti cells. It is shown that in the population of mRNA coding porcine growth hormone, heterogeneity is noted which is manifested not only at the level of the nucleotide sequence, but also is reflected in the amino acid sequence of the mature hormone.
Primary structure is determined of an insertion of a clone isolated from the library of hypophyseal cDNA of cattle by hybridization with a probe specific for prolactin. Analysis of nucleotide sequences showed that in the process of cloning, reorganization occurred in structure of preprolactin cDNA, including an inversion of the 5'-terminal and deletion of the central section of cDNA. Nevertheless, from structure of cDNA, nucleotide sequences can be deduced of extended 5'- and 3'-terminal sections of preprolactin mRNA in cattle with lengths of 257 and 551 nucleotide residues, respectively. When these sequences are compared to those established previously, some differences were found in primary structure. The most important of them is the presence of an additional codon which codes alanine at the position (-22) of the signal peptide. It is suggested that heterogeneity of preprolactin mRNA of cattle in the section coding the signal peptide is the result of alternative splicing, as was shown for preprolactin mRNA in rats.
Primary infection of HEp-2 cells with rubella virus resulted in non-cytophatic longterm persistent infection. During four years of persistence the virus was produced in sufficient quantities (up to 6 logs PFU/ml) and did not differ from the parental variant in its pathogenicity for BHK-21 or RK-13 cells, or hemagglutinating activity, but formed smaller plaques. Persistent virus preserved the original antigenicity as judged from reciprocal hemagglutination-inhibition or plaque reduction-neutralization tests with polyclonal antisera. Both original and persistent rubella viruses were thermoresistant (T 56° C) and sligthly temperature-sensitive. Clonal analysis revealed presence of ts-mutants among both original and persistent virus clones with different degrees of plating efficiency at 40°/34° C. RNA fingerprinting showed only minor changes in persistent rubella virus.
Structural peculiarities of the S'-end segments of genomic RNA were studied in F potato virus (F-PV) and white clover mosaic virus (WCMV). The methods of affinity chromatography on oligo(dT) cellulose and oligonucleotide mapping revealed a prolonged (up to 210 nucleotides) polyadenyl sequence at the 3'-end of F-PV RNA. A polyadenyl sequence is missing at the 3'end of WCMV RNA. A study of the translation products of WCMV and F-PV RNAs in a oe11-free protein-synthesizing system derived from rabbit reticulocytes showed that polypeptides electrophoretically comigrating with a structural protein of either virus were synthesized alongside high-molecular-weight polypeptides (M\(_r\)\(\approx\) 180-150 kdaltons).
Peptide and polypeptide hormones represent an extensive group of biologically active compounds of important significance for medicine and agriculture. In recent years genetic engineering methods have been used to create strains of microorganisms synthesizing eukaryotic proteins, including hormones and their precursors. The first stage of such developments is the isolation of DNA coding the des~red product. We have accomplished the cloning of the cDNA of a number of polypeptide and peptide hormones of the pituitary of man and domestic animals. The model gene of human calcitonin has also been synthesized and cloned. The obtained genes are being used to develop methods for the microbiological synthesis of human and animal-hormones.