Výsledky vyhledávání - "Adrian R. Pierotti"

Down-regulation of neprilysin (EC3.4.24.11) expression in vascular endothelial cells by laminar shear stress involves NADPH oxidase-dependent ROS production

Autor: Philip M. Cummins, Maria T. Killeen, Tony G. Walsh, Adrian R. Pierotti, Nicholas P. Tobin, Paul A. Fitzpatrick, Anthony F. Guinan, Ronan P. Murphy

Publikováno v: The International Journal of Biochemistry & Cell Biology. 41:2287-2294

Neprilysin (NEP, neutral endopeptidase, EC3.4.24.11), a zinc metallopeptidase expressed on the surface of endothelial cells, influences vascular homeostasis primarily through regulated inactivation of natriuretic peptides and bradykinin. Earlier in v

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b89bf3ff210aa562497204bc6139bd91
https://doi.org/10.1016/j.biocel.2009.05.011

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Gene expression of the dibasic-pair cleaving enzyme NRD convertase (N-arginine dibasic convertase) is differentially regulated in the GH3 pituitary and Mat-Lu prostate cell lines

Autor: Andrew Winter, Adrian R. Pierotti

Publikováno v: Biochemical Journal. 351:755-764

NRD convertase (N-arginine dibasic convertase, NRD-C) is a dibasic selective metalloprotease which cleaves on the N-terminal side of an arginine residue in a dibasic pair. Abundant in endocrine tissues, the highest levels are found in testis. The mec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::03f2412c0132779353392c4a3ca96d64
https://doi.org/10.1042/bj3510755

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Aminopeptidase-B in the rat testes: isolation, functional properties and cellular localization in the seminiferous tubules

Autor: Nicole Barré, Sandrine Cadel, Thierry Foulon, Dominique Segre´tain, Paul Cohen, Adrian R. Pierotti, Christophe Cre´minon

Publikováno v: Molecular and Cellular Endocrinology. 110:149-160

An aminopeptidase of the B-type, with an apparent M(r) 72,000 and pI = 4.9, was isolated from rat testes and characterized. The enzyme was able to remove only Arg and/or Lys residues from L-amino acid beta-naphthylamide derivatives and from the N-ter

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1ec51e5f14ca105b3f6f034c69608f5
https://doi.org/10.1016/0303-7207(95)03529-g

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Endopeptidase-24.15 in rat hypothalamic/pituitary/gonadal axis

Autor: James L. Roberts, Abraham Lasdun, Julia M. Ayala, Christopher J. Molineaux, Adrian R. Pierotti

Publikováno v: Molecular and Cellular Endocrinology. 76:95-103

Endopeptidase-24.15 (E.C. 3.4.24.15; EP-24.15) cleaves several substrates found in the hypothalamic/pituitary/gonadal axis, including gonadotropin-releasing hormone (GnRH) and the opioid peptides of the dynorphin family. We have examined the activity

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0024d9c4f6b6af4425d8ffeb5b87a791
https://doi.org/10.1016/0303-7207(91)90264-s

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Thimet oligopeptidase expression is differentially regulated in neuroendocrine and spermatid cell lines by transcription factor binding to SRY (sex-determining region Y), CAAT and CREB (cAMP-response-element-binding protein) promoter consensus sequences

Autor: Lesley S. Morrison, Adrian R. Pierotti

Publikováno v: The Biochemical journal. 376(Pt 1)

The zinc metalloprotease thimet oligopeptidase (EP24.15) is found predominantly in the neuroendocrine–gonadal axis where it is implicated in the processing of bioactive peptides, including GnRH (gonadotropin-releasing hormone), β-neoendorphin, α-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83cff2b785ab9bdd92504236d3762213
https://pubmed.ncbi.nlm.nih.gov/12911328

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Expression of the thimet oligopeptidase gene is regulated by positively and negatively acting elements

Autor: Adrian R. Pierotti, Suzan McCool

Publikováno v: DNA and cell biology. 19(12)

Thimet oligopeptidase (TOP) is a thiol-dependent metallopeptidase, which can cleave and thereby modulate the activity of many neuropeptides. The enzyme is active in many endocrine tissues, including testis, brain, and pituitary. In rat, the richest s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57e6c5f32d073405de9cfd0e390dfe2c
https://pubmed.ncbi.nlm.nih.gov/11177571

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Endopeptidase EC 3.4.24.15 presence in the rat median eminence and hypophysial portal blood and its modulation of the luteinizing hormone surge

Autor: A. Ian Smith, T. J. Wu, James L. Roberts, Adrian R. Pierotti, Marc J. Glucksman, W. John Sheward, Joan C. King, George Fink, Moshe Jakubowski

Publikováno v: Monash University

The endopeptidase EC 3.4.24.15 (EP24.15) is a zinc metalloendopeptidase that is widely distributed in a variety of tissues, including the testes, pituitary and the central nervous system. Among its numerous roles in metabolizing and processing biolog

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71ae2538c402fc98906f438c2883e53a
https://pubmed.ncbi.nlm.nih.gov/9419832

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N-arginine dibasic convertase, a metalloendopeptidase as a prototype of a class of processing enzymes

Autor: Annik Prat, Paul Cohen, Florence Gaudoux, Thierry Foulon, Adrian R. Pierotti, Anne-Marie Leseney, Valérie Chesneau

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America. 91(13)

N-Arg dibasic convertase is a metalloendopeptidase from rat brain cortex and testis that cleaves peptide substrates on the N terminus of Arg residues in dibasic stretches. By using both an oligonucleotide and antibodies to screen a rat testis cDNA li

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6a403a4c8f863d2c72ad4abb35f64db
https://pubmed.ncbi.nlm.nih.gov/8016118

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