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• W2054248001 abstract "Almost 10 years have passed since the first cDNA clone for a vasopressin (VP) gene product was obtained. Since then many new genomic and transcribed sequences have been analysed for members of the VP/oxytocin (OT) gene family. However, knowledge of the way in which the expression of these genes is regulated at the molecular level in physiology as well as in pathology remains sadly elusive. In order to summarize the present state of knowledge concerning these genes, the workshop ‘Molecular Biology of Vasopressin and Oxytocin Genes’ was held on June 6th/7th 1991 in Utrecht in the Netherlands, bringing together researchers from all over the world to discuss both the problems and results in what appears to be a system with model character not only in regard to the physiology of neurosecretion but also in terms of novel molecular mechanisms which are implicated in the expression of the genes. The programme was opened by setting an evolutionary perspective. Urano (Tokyo) and Morley (Edinburgh) described a variety of vasotocin and isotocin genes from teleost fish and amphibia. These genes are equivalent to the mammalian VP and OT lines, respectively, but demonstrate that the initial gene duplication giving rise to OT and VP evidently occurred very early in, if not before vertebrate evolution. This point is supported by the fact that in molluscs both VPand OT-related peptides are found. Van Kesteren (Amsterdam) showed that in the pondsnail Lymnaea stagnalis a VP-related peptide is present, which has a similar prohormone organization as vasotocin in lower vertebrates. Fish are important, however, in that they demonstrate that gene duplication is not an isolated event but has‘ evidently been repeated throughout evolution, such that in salmonids at least three independent duplications are evident. The first ancestral duplication gave rise to the two main vasotocin and isotocin lines. Each of these duplicated again during the salmonid tetraploidization to provide the vasotocin I and I1 genes and the isotocin I and 11 genes, and finally evidence was reported suggesting a further division into vasotocin I and I’ and vasotocin 11 and 11’ genes. These results are important for several reasons. First, they are critical for understanding how in mammals the VP/OT gene locus, where both genes are closely linked on the Same chromosome, separated only by a few kilobases of sequence, may have arisen. Second, gene duplication is obviously a prerequisite for the gene conversion events which are seen at the gene and peptide levels and account for the high degree of sequence conservation in the neurophysin-encoding regions of the genes. It is interesting to observe that in all species so far analysed at the DNA level the neurophysin moiety is extremely highly conserved. As a word of caution, however, Morley (Edinburgh) pointed out that in some cases probes derived from one of the duplicated genes had diverged so much, even within the nonapeptidc-encoding region, that they would not cross-hybridize between family members even within the same species. This is an important point to recall when considering the possibility of other mammalian members of this gene family. This session was closed by a report of an avian vasotocin cDNA sequence by Ivell (Hamburg) where, although the tripartite coding domains are conserved (hormone-neurophysinglycopeptide), the cleavage signal separating the neurophysin and glycopeptide moieties is absent. Nevertheless, avian vasotocin physiology is very similar to that in mammals, with osmotic stimuli being able t o upregulate the vasotocin gene, as shown by Miihlbauer (Celle). This would imply either that neurophysin or the glycopeptide are not involved in this physiology, or that whatever function these polypeptides may have it is not hampered by a failure to cleave these moieties. The possibility that mammals might possess other members of this gene family besides OT and VP was addressed by Rosenbaum (Portland, Oregon). A chance observation led to the antigen of a tumour marker monoclonal antibody being identified as related to the VP-neurophysin precursor. This tumour marker, however, was an integral membrane protein of ca. 43 kd, was encoded by an mRNA of ca. 1,000 nucleotides, and was expressed in carcinomas of the lung, breast and colon and in the pituitary gland. Preliminary amino-acid sequence as well as epitope analysis indicate that VP, neurophysin and glycopeptide moieties are all present, but that internally the amino-acid sequence diverges. It will be extremely interesting to see whether or not this product derives by alternative splicing from the known VP gene, or whether it represents the first hard evidence for a second VP gene in mammals. Evidence for the latter possibility was presented by Lopes da Silva (Utrecht) from a hybridization study of human genomic DNA where, a t low stringency, EcoRI digests suggested additional related genes in the human genome. Support for the existence of an unidentified VP/OT-like peptide in the thymus was provided by Geenan (Liitge). Using a panel of OT, VP and neurophysin antibodies led to the observation that a thymic epitope reacting with some VP and OT antibodies differed from the known nonapeptides. The classical scheme of neurosecretion could not be applied to the thymic neurohypophysial-related peptide(s). Rather, a cryptocrine model of cell-to-cell signalling between thymic epithelial/nurse cells and immature thymocytes (pre-T cells) has been proposed. A second VP gene in mammals would be convenient also to explain the presence of normal VP peptide levels in peripheral tissues of the Brattleboro rat. However, although various groups have tried to approach this question no success has been reported. Hypothalamic expression of VP in this mutant rat is suppressed" @default.
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• W2054248001 date "1991-12-01" @default.
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• W2054248001 title "The Molecular Biology of Vasopressin and Oxytocin Genes" @default.
• W2054248001 doi "https://doi.org/10.1111/j.1365-2826.1991.tb00321.x" @default.
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