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Relevant bibliographies by topics / NRD convertase

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Academic literature on the topic 'NRD convertase'

Author: Grafiati

Published: 25 May 2024

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Journal articles on the topic "NRD convertase"

1

HOSPITAL, Véronique, Valérie CHESNEAU, Agnès BALOGH, Catherine JOULIE, Nabil G. SEIDAH, Paul COHEN, and Annik PRAT. "N-arginine dibasic convertase (nardilysin) isoforms are soluble dibasic-specific metalloendopeptidases that localize in the cytoplasm and at the cell surface." Biochemical Journal 349, no. 2 (July 10, 2000): 587–97. http://dx.doi.org/10.1042/bj3490587.

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N-arginine (R) dibasic (NRD) convertase (nardilysin; EC 3.4.24.61), a metalloendopeptidase of the M16 family, specifically cleaves peptide substrates at the N-terminus of arginines in dibasic motifs in vitro. In rat testis, the enzyme localizes within the cytoplasm of spermatids and associates with microtubules of the manchette and axoneme. NRD1 and NRD2 convertases, two NRD convertase isoforms, differ by the absence (isoform 1) or presence (isoform 2) of a 68-amino acid insertion close to the active site. In this study, we overexpressed both isoforms, either by vaccinia virus infection of BSC40 cells or transfection of COS-7 cells. The partially purified enzymes exhibit very similar biochemical and enzymic properties. Microsequencing revealed that NRD convertase is N-terminally processed. Results of immunocytofluorescence, immunoelectron microscopy and subcellular fractionation studies argue in favour of a primary cytosolic localization of both peptidases. Although the putative signal peptide did not direct NRD convertase into microsomes in an in vitro translation assay, biotinylation experiments clearly showed the presence of both isoforms at the cell surface. In conclusion, although most known processing events at pairs of basic residues are achieved by proprotein convertases within the secretory pathway, NRD convertase may fulfil a similar function in the cytoplasm and/or at the cell surface.

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2

HOSPITAL, Véronique, Annik PRAT, Catherine JOULIE, Dorra CHÉRIF, Robert DAY, and Paul COHEN. "Human and rat testis express two mRNA species encoding variants of NRD convertase, a metalloendopeptidase of the insulinase family." Biochemical Journal 327, no. 3 (November 1, 1997): 773–79. http://dx.doi.org/10.1042/bj3270773.

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Rat testis NRD convertase (EC 3.4.24.61) is a Zn2+-dependent endopeptidase that cleaves, in vitro, peptide substrates at the N-terminus of Arg residues in dibasic sites. This putative processing enzyme of the insulinase family of metallopeptidases exhibits a significant degree of similarity to insulinase and two yeast processing enzymes, Axl1 and Ste23. We report the cloning of two human testis cDNA species encoding isoforms of NRD convertase, hNRD1 and hNRD2. Whereas the hNRD1 transcript (3.7 kb) is equivalent to the previously characterized rat cDNA (rNRD1), hNRD2 and rNRD2 are 3.9 kb novel forms containing a nucleotide insertion encoding a 68-residue segment. This motif, which is inserted N-terminal of the Zn2+-binding site, HXXEH, is contained within the most conserved region among the insulinase family members. Analysis of the deduced primary sequences revealed 92% identity between rat and human orthologues. The human gene encoding NRD convertase was localized to chromosome 1p32.1-p32.2. Whereas NRD convertase is mostly expressed in testis and in 24 cell lines, low mRNA levels were detected in most of the 27 other tissues tested.

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3

Chesneau, V., A. Prat, D. Segretain, V. Hospital, A. Dupaix, T. Foulon, B. Jegou, and P. Cohen. "NRD convertase: a putative processing endoprotease associated with the axoneme and the manchette in late spermatids." Journal of Cell Science 109, no. 11 (November 1, 1996): 2737–45. http://dx.doi.org/10.1242/jcs.109.11.2737.

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N-arginine dibasic convertase is a novel metalloendopeptidase which selectively cleaves at the N terminus of arginine residues in paired basic amino acids. Although present in brain and several other tissues, NRD convertase is particularly abundant in testis, where its expression appeared to be restricted to germ cells. Low levels of both mRNA and its corresponding protein were detected early in spermatogenesis. However, a marked accumulation of the protein was observed during late steps (14 to 19) of spermiogenesis. By electron microscopy, the NRD convertase immunoreactivity was localized in the cytoplasm of elongating and elongated spermatids, with a noticeable concentration at the level of two microtubular structures, i.e. the manchette and the axoneme. These observations strongly support the hypothesis that NRD convertase is involved in processing events potentially associated with the morphological transformations occurring during spermiogenesis.

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4

Csuhai, Eva, Maria Aparecida Juliano, Luiz Juliano, and Louis B. Hersh. "Kinetic Analysis of Spermine Binding to NRD Convertase." Archives of Biochemistry and Biophysics 362, no. 2 (February 1999): 291–300. http://dx.doi.org/10.1006/abbi.1998.1029.

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5

Psatha, Maria, Andrew Winter, and Adrian R. Pierotti. "Analysis of regulatory sequences in the NRD Convertase promoter." Biochemical Society Transactions 28, no. 3 (June 1, 2000): A83. http://dx.doi.org/10.1042/bst028a083b.

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6

WINTER, Andrew G., and Adrian R. PIEROTTI. "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." Biochemical Journal 351, no. 3 (October 24, 2000): 755–64. http://dx.doi.org/10.1042/bj3510755.

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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 mechanism whereby NRD-C expression is regulated at the transcriptional level has been examined by reporter-gene assay and electrophoretic-mobility-shift assays. Analysis of the rat and human promoters show that they are highly conserved, containing a number of motifs which may correspond to transcription-factor binding sites. The rat promoter has been cloned into a luciferase reporter vector and analysed in a number of cell lines. Full functionality of the promoter is observed with 5′ deletions to 411bp upstream of the transcriptional start site in spermatid, prostate and pituitary cell lines. Further deletion to 101bp causes a complete loss of activity in spermatid and prostate lines. By contrast, GH3 pituitary cells display no reduction in promoter activity with deletion to 101bp of upstream sequence. A number of transcription-factor binding sites have been identified by electrophoretic-mobility-shift assays in the region 411–101; however, no differences in binding between the cell lines were observed.

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7

Chesneau, V., A. R. Pierotti, A. Prat, F. Gaudoux, T. Foulon, and P. Cohen. "N-arginine dibasic convertase (NRD convertase): a newcomer to the family of processing endopeptidases. An overview." Biochimie 76, no. 3-4 (January 1994): 234–40. http://dx.doi.org/10.1016/0300-9084(94)90151-1.

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8

Psatha, M. I., J. A. Craft, and A. R. Pierotti. "Regulation of the expression of NRD-Convertase: a novel promoter element." Biochemical Society Transactions 29, no. 5 (October 1, 2001): A130. http://dx.doi.org/10.1042/bst029a130.

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9

Psatha, M. I., and A. R. Pierotti. "Identification of a putative cell type specific repressor activity within the NRD convertase gene promoter." Biochemical Society Transactions 30, no. 1 (February 1, 2002): A42. http://dx.doi.org/10.1042/bst030a042.

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10

Fumagalli, P., M. Accarino, A. Egeo, P. Scartezzini, G. Rappazzo, A. Pizzuti, V. Avvantaggiato, et al. "Human NRD Convertase: A Highly Conserved Metalloendopeptidase Expressed at Specific Sites during Development and in Adult Tissues." Genomics 47, no. 2 (January 1998): 238–45. http://dx.doi.org/10.1006/geno.1997.5078.

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More sources

Dissertations / Theses on the topic "NRD convertase"

1

Psatha, Maria Ioannou. "Functional characterisation of the NRD convertase gene promoter." Thesis, Glasgow Caledonian University, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.395792.

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2

Winter, Andrew Gavin. "Cloning, characterisation, and regulation of the NRD convertase gene." Thesis, Glasgow Caledonian University, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.267548.

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3

CHESNEAU, VALERIE. "La nrd convertase (ec 3. 4. 24. 61) : une nouvelle metalloprotease. isolement, caracterisation, clonage et distribution tissulaire." Paris 6, 1995. http://www.theses.fr/1995PA066287.

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La n-arginine dibasic convertase (nrd convertase, nardilysine, ec 3. 4. 24. 61) est une metalloendopeptidase clivant selectivement en amont de residus arginine inclus dans des paires d'acides amines basiques. Initialement mise en evidence dans des extraits de cerveau de rat, elle s'avere particulierement abondante dans le testicule. Deux isoformes de masses moleculaires 110 et 140 kda sont purifiees a partir de chacun de ces deux tissus. L'adn complementaire du messager de cette enzyme a ete isole. La sequence proteique deduite (133 kda) presente trois caracteristiques majeures: un peptide signal putatif d'adressage au reticulum endoplasmique, un domaine acide de 71 residus compose a 79% d'acides aspartiques et glutamiques, et le pentapeptide consensuel hxxeh implique dans la coordination de l'atome de zinc catalytique. Bien que les homologues les plus proches de la nardilysine soient l'insulysine (ec 3. 4. 99. 45) et la pitrilysine (ec 3. 4. 99. 44), la presence du motif hxxeh l'apparente egalement a plusieurs metallopeptidases de la famille m16. L'analyse comparative de ses 27 membres a permis de reveler un certain nombre de positions conservees, exclusivement associees a la presence du site de fixation du zinc. Une definition plus restrictive de cette famille a donc ete proposee. Dans le testicule, l'expression de la nardilysine est restreinte aux cellules de la lignee germinale et fortement regulee au cours de la spermatogenese. Detectee des le stade spermatocyte primaire, la proteine voit sa synthese s'accroitre de maniere spectaculaire lors des phases finales de la spermiogenese. De plus, la nrd convertase s'accumule au niveau des deux structures microtubulaires de la spermatide allongee: l'axoneme et la manchette, etablie de maniere transitoire au cours de la metamorphose cellulaire. Le profil d'expression de la nardilysine au cours de la spermatogenese et sa localisation subcellulaire dans la spermatide agee suggerent fortement qu'elle pourrait participer aux evenements biochimiques associes au processus d'elongation cellulaire. Cependant, cette endopeptidase est, d'evidence, egalement secretee par la cellule germinale. L'hypothese d'une proteine bifonctionnelle semble s'imposer. Sa specificite de clivage, associee a son transit par la voie de secretion, en fait egalement un excellent candidat au role d'endoprotease de maturation prohormonale

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4

HOSPITAL, VERONIQUE. "Mise en evidence de deux arn messagers pour la nrd convertase. Caracterisation et localisation subcellulaire des enzymes recombinantes correspondantes." Paris 6, 1999. http://www.theses.fr/1999PA066571.

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In vitro, la n-arginine (r) dibasic (d) convertase (nrd convertase ; ec 3. 4. 24. 61 ; 140 kda), metalloendopeptidase de la famille m16 purifiee a partir du testicule de rat, clive selectivement en amont de residus arginine inclus dans des paires d'acides amines basiques. L'adnc isole code pour une proteine qui se caracterise par un peptide signal putatif d'adressage au re, par un domaine acide de 71 residus et le motif hxxeh. Son profil d'expression au cours de la spermatogenese et sa localisation au niveau de deux structures microtubulaires de la spermatide agee (l'axoneme et la manchette), suggerent fortement qu'elle pourrait participer au processus d'elongation cellulaire. Elle est egalement secretee par la cellule germinale et par les cellules el4, lignee cellulaire d'origine lymphocytaire. Le travail presente dans ce manuscrit rapporte : (i) le clonage de l'adnc de l'enzyme humaine et l'identification de deux especes moleculaires, le premier transcrit, hnrd1, est equivalent a celui precedemment caracterise chez le rat alors que le second, hnrd2, se distingue par une insertion de 204 nucleotides. Ce dernier, bien que moins represente dans le testicule de rat, a egalement ete caracterise. La proteine correspondante, nrd2 convertase, presente donc un segment additionnel de 68 residus positionne entre le domaine acide et le motif hxxeh. Les structures primaires des proteines humaines et de rat sont fortement conservees (92% identite). (ii) la distribution tissulaire et cellulaire des transcrits nrd analysee par northern blot, bien que le testicule soit le site principal de leur expression, ils sont largement exprimes, et l'expression de la nrd2 convertase n'est pas restreinte a ce tissu. (iii) l'analyse comparee des proprietes biochimiques et enzymatiques des deux isoformes surexprimees ainsi que leur localisation subcellulaire. Similaires et comparables a l'enzyme purifiee du testicule de rat, les deux isoformes ne se sont distinguees que par leur stabilite relative. Bien que leur specificite de clivage evoque celle d'enzymes de la voie de secretion, elles sont principalement localisees dans le cytoplasme des cellules qui les surexpriment. La nrd convertase semble donc etre une endopeptidase cytoplasmique. Les mecanismes conduisant a sa secretion ainsi que ses substrats in vivo restent a determiner.

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5

Sawaya, Jean-Pierre. "Les Sept Nations du Canada : traditions d'alliance dans le Nord-Est, XVIIIe-XIXe siècles." Master's thesis, Université Laval, 1994. http://hdl.handle.net/20.500.11794/28435.

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Books on the topic "NRD convertase"

1

Canetti, Regine. Sister of Zion: A life story. Springfield, NJ: Gefen Publishing House Ltd., 2015.

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2

Chryssides, George D. Conversion. Edited by James R. Lewis and Inga Tøllefsen. Oxford University Press, 2016. http://dx.doi.org/10.1093/oxfordhb/9780190466176.013.2.

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The chapter explores explanations for conversion to new religious movements (NRMs). Rather than sudden episodic conversion, joining an NRM can be attributed to self-discovery, following a schism, or pursuing a special interest within a religious organisation. There are definite patterns of conversion in NRMs, and notably a disproportion of Jews who join. It is argued that key factors include availability for the requisite lifestyle, and the gaining of “compensators” that the NRM offers. A further factor is offering religious experience and a forum in which to discuss it. The author explores the role of the Internet in conversion, arguing that it accounts the rise of “invented religions”, but otherwise has limited bearing on gaining new members. Finally, the religions themselves undergo change as new converts espouse them.

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3

(Foreword), Bernard Palmer, and L. W. Elford (Introduction), eds. The Bushman and the Spirits. Horizon Books Publishers, 1999.

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