Human testis specifically expresses a homologue of the rodent T lymphocytes RT6 mRNA

Lévy, Isabelle; Wu, Yuan-Qing; Roëckel, Nathalie; Bulle, Frédérique; Pawlak, André; Siegrist, Sylvie; Mattéi, Marie Geneviève; Guellaën, Georges

doi:10.1016/0014-5793(96)00183-4

Cited by 22 publications

(11 citation statements)

References 28 publications

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“…Among the monoARTs are bacterial products (e.g., cholera toxin), which are responsible for the clinical syndrome in disease (13). A family of mammalian ARTs that are secreted or localized on the cell surface through glycosylphosphatidylinositol anchors (14)(15)(16)(17)(18)(19) are expressed preferentially on epithelial and inflammatory cells such as lymphocytes and neutrophils (17,20). Substrates of the five known mammalian ARTs (ART-1-5) include proteins that are involved in critical cellular events (e.g., lymphocyte activation, neutrophil chemotaxis) (21)(22)(23).…”

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confidence: 99%

ADP ribosylation of human neutrophil peptide-1 regulates its biological properties

Paone

Wada

Stevens

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

116

108

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In human airways, epithelial cells lining the lumen and intraluminal cells (e.g., polymorphonuclear cells) participate in the innate immune response. These cells secrete or express on their surfaces arginine-specific ADP ribosyltransferases. Defensins, antimicrobial proteins secreted by immune cells, are arginine-rich, leading us to hypothesize that ADP ribosylation could modify their biological activities. We found that an arginine-specific ADP ribosyltransferase-1 present on airway epithelial cells modifies Arg-14 of ␣ defensin-1. ADP-ribosylated defensin-1 had decreased antimicrobial and cytotoxic activities but still stimulated T cell chemotaxis and IL-8 release from A549 cells. Further, ADP-ribosylated defensin-1 inhibited cytotoxic and antimicrobial activities of unmodified defensin-1. We identified ADP-ribosylated defensin-1 in bronchoalveolar lavage fluid from smokers but not from nonsmokers, confirming its existence in vivo. Thus, airway mono-ADP-ribosyltransferases could have an important regulatory role in the innate immune response through modification of ␣ defensin-1 and perhaps other basic molecules, with alteration of their biological properties. In the human airway, epithelial cells, in concert with intraluminal cells (e.g., macrophages), contribute to the innate immune response. Activation of airway epithelial cells releases proinflammatory mediators and chemotaxins, leading to the recruitment of inflammatory cells (e.g., neutrophils) (1, 2). Activated neutrophils, in turn, release azurophilic granules that contain human neutrophil peptides (HNP), small cationic peptides ranging in size from 29-33 aa (3). HNPs are characterized by a high arginine content and contain three pairs of disulfidelinked cysteines (4). They have a broad spectrum of antimicrobial and cytotoxic activities and play an important role in the innate immune response against both Gram-positive and -negative bacteria, fungi, and certain enveloped viruses (5-8). High HNP levels have been found in airway secretions of patients with inflammatory lung diseases (9-11).A family of eukaryotic and prokaryotic mono-ADP ribosyltransferases (ARTs) catalyze the transfer of ADP ribose from NAD ϩ to arginine residues in proteins (12). Among the monoARTs are bacterial products (e.g., cholera toxin), which are responsible for the clinical syndrome in disease (13). A family of mammalian ARTs that are secreted or localized on the cell surface through glycosylphosphatidylinositol anchors (14-19) are expressed preferentially on epithelial and inflammatory cells such as lymphocytes and neutrophils (17,20). Substrates of the five known mammalian ARTs (ART-1-5) include proteins that are involved in critical cellular events (e.g., lymphocyte activation, neutrophil chemotaxis) (21-23). Two of these transferases, ART-1 and -5, specifically modify arginine residues in proteins. The finding of ARTs on airway epithelial and inflammatory cells prompted us to evaluate potential substrates for ADP ribosylation in the airway (24). Because of the high arginine c...

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mentioning

confidence: 99%

ADP ribosylation of human neutrophil peptide-1 regulates its biological properties

Paone

Wada

Stevens

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

116

108

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“…Poly(A) + RNA from dierent human tumor tissues were analysed by Northern blot as previously described (Levy et al, 1996).…”

Section: Northern and Southern Blot Analysismentioning

confidence: 99%

hH-Rev107, a class II tumor suppressor gene, is expressed by post-meiotic testicular germ cells and CIS cells but not by human testicular germ cell tumors

et al. 2001

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By systematic analysis of a human testis library, we have isolated the hH-Rev107-3 cDNA, identical to hHRev107-1 cDNA, which was previously described as a class II tumor suppressor gene. In this study, two transcripts (1 and 0.8 kb) were detected by Northern blot in all human tissues, excepted in thymus. The strongest expression was found in testis, skeletal muscle and heart. These two mRNA are probably transcribed from only one gene that we mapped to the q12-q13 region of the chromosome 11. In human testis, hH-Rev107 gene expression was localized, by in situ hybridization, within the round spermatids. To investigate a possible role for hH-Rev107 protein in testicular malignant growth, we examined the expression of this gene in germ cell tumors. A strong hH-Rev107 gene expression was observed in normal testis as well as in samples with preinvasive carcinoma in situ but was completely absent in overt tumors, both seminomas and non-seminomas. By in situ hybridization, CIS was found hH-Rev107 positive and tumor negative. A semi-quantitative assessment of hHRev107 mRNA level in testicular germ cell tumors, by RT ± PCR, exhibited a ninefold decrease in the gene expression. No gross structural aberrations of hHRev107 gene were detected in these human primary tumors. The results suggest that down-regulation of hHRev107 may be associated with invasive progression of testicular germ cell tumors. Oncogene (2001) 20, 5155 ± 5163.

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“…The hydropathy profiles of the amino-and carboxyl-terminal sequences of ART3 and ART4 demonstrate hydrophobic signal sequences consistent with the possibility that ART3 and ART4, like ART1, may be GPI-linked. The ART3 gene was localized to chromosome 4q13-q21 (42), and ART4 is on chromosome 12q13.2-q13.3 (43). On Northern analysis, a 1.8-kb band in poly(A) ϩ RNA from human testis and skeletal muscle and a weaker 1.6-kb band in poly(A) ϩ RNA from heart hybridized with an ART3 cDNA probe (42).…”

Section: Mammalian Adp-ribosyltransferasesmentioning

confidence: 99%

“…ART3 and ART4 -ART3 and ART4 were recently cloned from human testis (42) and spleen (43), respectively. The deduced amino acid sequences of ART3 and ART4 possess several regions of sequence similarity with ART1 and are 14 and 31% identical, respectively, to ART1.…”

Section: Mammalian Adp-ribosyltransferasesmentioning

confidence: 99%

“…The ART3 gene was localized to chromosome 4q13-q21 (42), and ART4 is on chromosome 12q13.2-q13.3 (43). On Northern analysis, a 1.8-kb band in poly(A) ϩ RNA from human testis and skeletal muscle and a weaker 1.6-kb band in poly(A) ϩ RNA from heart hybridized with an ART3 cDNA probe (42). An ART4 probe hybridized with 1.4-, 2.4-, and 5.5-kb bands in poly(A) ϩ RNA from spleen, ovary, and intestine (43).…”

Section: Mammalian Adp-ribosyltransferasesmentioning

confidence: 99%

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Glycosylphosphatidylinositol-anchored and Secretory Isoforms of Mono-ADP-ribosyltransferases

Okazaki

Moss

1998

Journal of Biological Chemistry

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Mono-ADP-ribosylation, a post-translational modification of proteins in which the ADP-ribose moiety of NAD is transferred to an acceptor amino acid, occurs in viruses, bacteria, and eukaryotic cells (1). The reaction is distinct from that catalyzed by poly(ADPribose) polymerase, a nuclear protein involved in DNA repair, cell differentiation, and the maintenance of chromatin structure (2). Among mono-ADP-ribosyltransferases, the bacterial toxins, cholera toxin, pertussis toxin, diphtheria toxin, and Pseudomonas aeruginosa exotoxin A are the best characterized in molecular structure, function, and substrate specificity (reviewed in Ref. 1). Mono-ADP-ribosyltransferases from mammalian and avian cells have been cloned and characterized, and specific target proteins have been identified (3,4). In lymphocytes, a glycosylphosphatidylinositol (GPI) 1 -anchored transferase appears to be involved in immune modulation, whereas other isoforms in lymphocytes (5) and chicken heterophil granules (6) are membrane-associated but appear to be processed for secretion. Further, ADP-ribosyltransferases have been purified from brain, and data from several independent laboratories demonstrate that ADP-ribosylation is involved in neuronal function (7,8). Deduced amino acid sequences of the vertebrate ADP-ribosyltransferases have similarities to those of viral and bacterial toxin transferases (9, 10) in regions that form, in part, an active site cleft, consistent with a common mechanism of NAD binding and ADP-ribose transfer (9).The majority of the eukaryotic enzymes are arginine-specific transferases. ADP-ribosylation of arginine appears to be a reversible process; free arginine can be regenerated in ADP-ribosylated proteins by ADP-ribosylarginine hydrolases (1). ADP-ribosylarginine hydrolase activity was detected in the soluble fraction of turkey erythrocytes, cultured mouse cells, and rat skeletal muscle with deduced amino acid sequences known for rat, mouse, and human brain ADP-ribosylarginine hydrolases (11,12).ADP-ribosylation of cysteine was reported in bovine erythrocytes (13), and an NAD:cysteine ADP-ribosyltransferase that modified G␣ i was purified from human erythrocyte and platelet membranes (14). Consistent with this, ADP-ribosylcysteine linkages were detected in rat liver plasma membranes (15). ADP-ribosylation of cysteine can, however, occur nonenzymatically via the reaction of ADP-ribose, generated from NAD by NAD glycohydrolases, with cysteine to form an ADP-ribosylthiazolidine, a linkage distinct from the thioglycoside formed by pertussis toxin (PT)-catalyzed ADP-ribosylation of a cysteine in the heterotrimeric guanine nucleotide-binding (G) proteins (16). Nonenzymatic ADP-ribosylation of cysteine in proteins, however, yielded a product with the same chemical sensitivity as the linkage formed by PT (17). Based on these data, the ADP-ribose-cysteine produced by the human erythrocyte enzyme may have been generated nonenzymatically from free ADP-ribose. Because nitric oxide (NO) induced the noncovalent binding of the ent...

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Human testis specifically expresses a homologue of the rodent T lymphocytes RT6 mRNA

Cited by 22 publications

References 28 publications

ADP ribosylation of human neutrophil peptide-1 regulates its biological properties

ADP ribosylation of human neutrophil peptide-1 regulates its biological properties

hH-Rev107, a class II tumor suppressor gene, is expressed by post-meiotic testicular germ cells and CIS cells but not by human testicular germ cell tumors

Glycosylphosphatidylinositol-anchored and Secretory Isoforms of Mono-ADP-ribosyltransferases

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