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  • Processing  (2)
  • central nervous system  (1)
  • chromogranin  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Functional diversity of bioactive peptides in the nervous system itself: “How the brain may understand” (1989)
    Springer
    Bioscience reports 9 (1989), S. 693-700 
    Details
    ISSN: 1573-4935
    Keywords: central nervous system ; processing ; biological diversity ; peptide hormones
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The interactions involving cells of the nervous system are a complex form of intercellular communication. Biosynthesis of peptide hormones or active neuropeptides is generally through a precursor which provides increased product choices as a function of the processing pathway. Proteolytic processing as well as other molecular modification lead to a wide range of mature products which may vary in different tissues even though they are derived from the same precursor. Also the same neuropeptide may exhibit different bioactivities for different target cells. Finally, by means of collective packaging in secretory organelles, a cell may be able by synergism to further broaden its biologic effects. In these ways, what is seen as added complication in the CNS, may be from the point of view of the cell, a successful attempt to increase its survival ability to adapt and influence its bioenvironment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01114807
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The distinct gene expression of the pro-hormone convertases in the rat heart suggests potential substrates (1995)
    Springer
    Cell & tissue research 279 (1995), S. 539-549 
    Details
    ISSN: 1432-0878
    Keywords: Key words: In situ hybridization ; Immunohistochemistry ; Pro-hormone convertases ; Cardiovascular tissues ; Pro-atrial natriuretic factor ; Pro-endothelin ; Processing ; Rat (Sprague Dawley)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The present study examined the distribution of the pro-hormone convertases PC1, PC2, furin, PACE4 and PC5 in the rat heart. Northern blot analysis of RNA extracted from cardiac tissues showed high levels of furin and PACE4 mRNA in the atria and ventricles, while PC5 mRNA was found to be expressed at high levels in the dorsal aorta. Although undetectable by Northern blot analysis, both PC1 and PC2 mRNA were detected by in situ hybridization and immunohistochemistry in discrete regions of the intracardiac para-aortic ganglia. In situ hybridization studies also showed that furin mRNA was observed in all cardiac tissues and cells, consistent with the previously reported ubiquitous expression of this gene. PACE4 mRNA was highly abundant in both the atria and ventricular cardiomyocytes, with low to undetectable levels observed in blood vessels. Finally, PC5 transcripts were expressed in the endothelial cells lining coronary vessels and the valve leaflets of the heart. The present localization studies in the heart and cardiac blood vessels suggests potential roles for each convertase in the processing of various neuropeptides, hormones and growth factors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004410050313
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    The distinct gene expression of the pro-hormone convertases in the rat heart suggests potential substrates (1995)
    Springer
    Cell & tissue research 279 (1995), S. 539-549 
    Details
    ISSN: 1432-0878
    Keywords: In situ hybridization ; Immunohistochemistry ; Pro-hormone convertases ; Cardiovascular tissues ; Pro-atrial natriuretic factor ; Pro-endothelin ; Processing ; Rat (Sprague Dawley)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The present study examined the distribution of the pro-hormone convertases PC1, PC2, furin, PACE4 and PC5 in the rat heart. Northern blot analysis of RNA extracted from cardiac tissues showed high levels of furin and PACE4 mRNA in the atria and ventricles, while PC5 mRNA was found to be expressed at high levels in the dorsal aorta. Although undetectable by Northern blot analysis, both PC1 and PC2 mRNA were detected by in situ hybridization and immunohistochemistry in discrete regions of the intracardiac para-aortic ganglia. In situ hybridization studies also showed that furin mRNA was observed in all cardiac tissues and cells, consistent with the previously reported ubiquitous expression of this gene. PACE4 mRNA was highly abundant in both the atria and ventricular cardiomyocytes, with low to undetectable levels observed in blood vessels. Finally, PC5 transcripts were expressed in the endothelial cells lining coronary vessels and the valve leaflets of the heart. The present localization studies in the heart and cardiac blood vessels suggests potential roles for each convertase in the processing of various neuropeptides, hormones and growth factors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00318166
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Distribution and Regulation of Proconvertases PC1 and PC2 in Human Pituitary Adenomas (1999)
    Springer
    Pituitary 1 (1999), S. 187-195 
    Details
    ISSN: 1573-7403
    Keywords: pituitary ; proconvertase ; chromogranin ; pancreastatin ; in situ hybridization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Pituitary adenomas are members of the family of neuroendocrine cells and tumors which have secretory granules containing chromogranins/secretogranins and other proteins. Pituitary adenomas express the neuroendocrine specific proconvertases PC1 (also known as PC3) and PC2, which are important for the proteolytic processing of chromogranins/secretogranins molecules. We examined the distribution of PC1 and PC2 in primary cultures of 20 pituitary adenomas and analyzed the regulation of the proconvertase mRNAs and proteins by various secretagogues including hypothalamic hormones and phorbol ester to determine the role of PC1 and PC2 in CgA processing in pituitary adenomas. Although PC2 was present in all adenomas, there was a differential distribution of PC1 with PRL adenomas expressing lower levels of PC1 compared to other adenoma types by RT-PCR analysis, in situ hybridization and immunostaining. Treatment of primary cultures of pituitary adenomas with phorbol 12-myristrate 13-acetate (PMA) resulted in an increase in pancreastatin (PST) secretion in most pituitary adenomas and increased PC1 mRNA and protein expression in gonadotroph adenomas, but not in other types of adenomas. Analysis of a human pituitary adenoma cell line, immortalized by recombinant defective adenovirus (HP75), which expressed chromogranin A, FSH, PC1 and PC2 showed that PST was secreted by these immortalized cells. Treatment with TGFβ1 resulted in an increase in PST secretion and in PC1 mRNA and protein. These results indicate that a) there is a differential distribution of PC1 in human pituitary adenomas with PRL adenomas expressing very little PC1 mRNA and protein and b) that PC1 expression in gonadotropin hormone-producing adenomas is regulated by PMA and TGFβ1. These findings support the observation that chromogranin A is a substrate for the endoproteinase PC1 in human pituitary adenoma cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1009909232243
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    Paper (German National Licenses)
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