Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Structure and Regulation of the Melanin-Concentrating Hormone Gene (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 680 (1993), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1993.tb19678.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Neuropeptide-E-1 Antagonizes the Action of Melanin-Concentrating Hormone on Stress-Induced Release of Adrenocorticotropin in the Rat (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neuroendocrinology 7 (1995), S. 0 
    Details
    ISSN: 1365-2826
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The physiological role of melanin-concentrating hormone (MCH) in mammals is still very elusive, but this peptide might participate in the central control of the hypothalamopituitary adrenal (HPA) axis during adaptation to stress. Cloning and sequencing of the rat MCH (rMCH) cDNA revealed the existence of additional peptides encoded into the MCH precursor. Among these peptides, neuropeptide (N) glutamic acid (E) isoleucine (I) arnide (NEI) is co-processed and secreted with MCH in rat hypothalamus. In the present work we examined: (1) The pattern of rMCH mRNA expression during the light and dark conditions in the rat hypothalamus and (2) The effect of intracerebroventricular (ICV) injections of rMCH and NEI in the control of basal or ether stress-modified release of corticotropin (ACTH), prolactin (PRL) and growth hormone (GH) secretion in vivo in light-on and light-off conditions. Our data indicate that rMCH mRNA levels do not change during the light-on period, but increase after the onset of darkness. Either alone or co-administered, rMCH and NEI do not modify basal secretion of GH and PRL at any time tested nor do they alter ether stress-induced changes in these two hormonal secretions. At the end of the light on period corresponding to the peak of the circadian rhythm in ACTH, administration of rMCH but not NEI leads to a decrease in ACTH levels while MCH is not effective during the light off period of the cycle (i.e. when basal ACTH levels are already low). Using a moderate ether induced stress, ACTH levels are only stimulated during the dark phase of the cycle. rMCH (63 or 210 nmoles) prevents the rise in ACTH release while NEI alone does not modify the stress response. Co-administration of both peptides before stress results in an abolition of the rMCH induced inhibition of ACTH plasma levels. Taken together, these data indicate that rMCH may act as a central corticotropin inhibitory factor involved in the circadian rhythmicity of plasma ACTH levels and that NEI antagonizes its action.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2826.1995.tb00761.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Analysis of the expression of two genes of Dictyostelium discoideum which code for developmentally regulated cysteine proteinases (1986)
    Springer
    Molecular genetics and genomics 203 (1986), S. 333-340 
    Details
    ISSN: 1617-4623
    Keywords: Dictyostelium ; Cysteine proteinases ; Development ; Regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We analysed the expression of two genes encoding two different cysteine proteinases which show a high degree of homology and are regulated differentially during Dictyostelium discoideum development. While absent from growing vegetative cells, the two specific messengers RNAs appear at an early stage of development but accumulate in the polysomes at different later stages of development. The message coding for cysteine proteinase I reaches its maximum level after the aggregative period while cysteine proteinase II mRNA reaches its maximum during the culmination stage. At these times they represent 1% and 0.7%, respectively, of cellular mRNA and belong to the most abundant class of mRNAs. No accumulation of the two messages elsewhere than in the polyribosomes was observed in the cytoplasm of the cells, whatever the stage of development analysed. Results of analysis of the nuclear levels of RNA complementary to the two genes are in agreement with the relative transcription rates determined by in vitro transcription of nuclei isolated at different stages. The combined results of these measurements demonstrate that the expression of the cysteine proteinase I and II genes is mainly under transcriptional control. However, the difference between the RNA synthetic rate in the nucleus and the accumulation of the mRNA in the cytoplasm, indicates an additional post-transcriptional regulation for the cysteine proteinase II gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00333976
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Structural analysis of a developmentally regulated sequence encoding for a cysteine proteinase in Dictyostelium discoideum (1986)
    Springer
    Molecular genetics and genomics 203 (1986), S. 324-332 
    Details
    ISSN: 1617-4623
    Keywords: Dictyostelium ; Cysteine proteinase ; Gene sequencing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A developmentally regulated DNA sequence was isolated from a Dictyostelium discoideum genomic library by cross hybridization with a cDNA clone of cysteine proteinase I. The genomic fragment represents a different but related gene, designated cysteine proteinase II. This sequence is unique in the genome and it hybridizes to a polyA+ RNA of 1.5 kb length, which is produced after the aggregation period. From the determination of polarity of transcription and from the nucleotide sequence, it was shown that the isolated fragment representing about a third of the gene includes its 3′ end. The open reading frame ends with a termination codon TAA and is not interrupted by intervening sequences. The flanking untranslated sequence beyond the 3′ terminus is very A+T rich (91%) and includes a sequence, ATTAAA, known to be important in polyA addition. A striking homology in the corresponding amino acid sequence was found not only with cysteine proteinase I of Dictyostelium discoideum but also with other known cysteine proteases from plants and from mammals. The strongest homology is observed especially around the cysteine at the active site identified in some of these enzymes. Interestingly the organization of cysteine proteinase I and II of Dictyostelium discoideum differs considerably. The C terminal region of the latter corresponds to the N terminal one of the former.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00333975
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...