Molecular cloning of the human kidney differentiation antigen gp160: human aminopeptidase A.

Nanus, David M.; Engelstein, Dov; Gastl, Guenther; Gluck, Lisa; Vidal, Matt J.; Morrison, Mark E.; Finstad, Connie L.; Bander, Neil H.; Albino, Anthony P.

doi:10.1073/pnas.90.15.7069

Cited by 104 publications

(80 citation statements)

References 34 publications

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“…Aminopeptidase A is an ectopeptidase member of the peptidase family m1 proposed to play a role in the progression of cervical neoplasms (Fujimura et al, 2000). Interestingly, its expression in tissue culture correlates with resistance of renal carcinoma cells to the antiproliferative e ects of alpha-interferon (Nanus et al, 1993). Aminopeptidase A shows a 54% identity to aminopeptidase N, a gene recently found to promote invasion and to be expressed on proliferating endothelial cells undergoing angiogenesis (Pasqualini et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

Identification of novel hypoxia dependent and independent target genes of the von Hippel-Lindau (VHL) tumour suppressor by mRNA differential expression profiling

et al. 2000

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The von Hippel-Lindau tumour suppressor gene (VHL) targets hypoxia inducible factor (HIF)-a subunits for ubiquitin dependent proteolysis. To better understand the role of this and other putative pathways of gene regulation in VHL function we subjected mRNA from VHL defective renal carcinoma cells and transfectants re-expressing a wild type VHL allele to di erential expression pro®ling, and analysed VHL target genes for oxygen regulated expression. Among a group of newly identi®ed VHL target genes the majority but not all were regulated by oxygen, indicating that whilst dysregulation of the HIF system makes a dominant contribution to alterations in transcription, VHL has other in¯uences on patterns of gene expression. Genes newly de®ned as targets of the VHL/hypoxia pathway (conditionally downregulated by VHL in normoxic cells) include aminopeptidase A, collagen type V, alpha 1, cyclin G2, DEC1/Stra13, endothelin 1, low density lipoprotein receptor-related protein 1, MIC2/CD99, and transglutaminase 2. These genes have a variety of functions relevant to tumour biology. However, not all are connected with the promotion of tumour growth, some being pro-apoptotic or growth inhibitory. We postulate that co-ordinate regulation as part of the HIF pathway may explain this paradox, and that evolution of antiapoptotic pathways may be required for tumour growth under VHL-dysregulation. Our results indicate that it will be necessary to consider the e ects of abnormal activity in integral regulatory pathways, as well as the e ects of individual genes to understand the role of abnormal patterns of gene expression in cancer. Oncogene (2000) 19, 6297 ± 6305.

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Section: Discussionmentioning

confidence: 99%

Identification of novel hypoxia dependent and independent target genes of the von Hippel-Lindau (VHL) tumour suppressor by mRNA differential expression profiling

et al. 2000

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“…extracellular domain (1)(2)(3) and is capable of cleaving N-terminal dipeptides with either L-proline or L-alanine at the penultimate position (2). CD26 activity is dependent on cell type and the microenvironment, factors that can influence its multiple biological roles (reviewed in Refs.…”

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confidence: 99%

Caveolin-1 Triggers T-cell Activation via CD26 in Association with CARMA1

Ohnuma

Uchiyama

Yamochi

et al. 2007

Journal of Biological Chemistry

119

111

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CD26 is a widely distributed 110-kDa cell surface glycoprotein with an important role in T-cell costimulation. We demonstrated previously that CD26 binds to caveolin-1 in antigen-presenting cells, and following exogenous CD26 stimulation, Tollip and IRAK-1 disengage from caveolin-1 in antigen-presenting cells. IRAK-1 is then subsequently phosphorylated to up-regulate CD86 expression, resulting in subsequent T-cell proliferation. However, it is unclear whether caveolin-1 is a costimulatory ligand for CD26 in T-cells. Using soluble caveolin-1-Fc fusion protein, we now show that caveolin-1 is the costimulatory ligand for CD26, and that ligation of CD26 by caveolin-1 induces T-cell proliferation and NF-B activation in a T-cell receptor/ CD3-dependent manner. We also demonstrated that the cytoplasmic tail of CD26 interacts with CARMA1 in T-cells, resulting in signaling events that lead to NF-B activation. Ligation of CD26 by caveolin-1 recruits a complex consisting of CD26, CARMA1, Bcl10, and IB kinase to lipid rafts. Taken together, our findings provide novel insights into the regulation of T-cell costimulation via the CD26 molecule.

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“…Gluzincin aminopeptidases share the consensus HEXXH(X) 18 E zinc-binding motif essential for enzymatic activity (10). This growing family of mammalian zinccontaining aminopeptidase includes membrane-bound (P-LAP, aminopeptidase A, aminopeptidase N, and thyrotropin-releasing hormone degrading enzyme) (3,4,6,11,12), cytosolic (puromycin-sensitive aminopeptidase (PSA) and leukotriene A 4 hydrolase) (13,14), secretory (aminopeptidase B) (15), and ER resident (A-LAP/ERAP1) (9,16) proteins. Mutational analyses revealed that essential amino acid residues are well conserved among members of the family (17)(18)(19)(20).…”

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confidence: 99%

Human Leukocyte-derived Arginine Aminopeptidase

Tanioka

Hattori

Masuda

et al. 2003

Journal of Biological Chemistry

178

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In this study we report the cloning and characterization of a novel human aminopeptidase, which we designate leukocyte-derived arginine aminopeptidase (L-RAP). The sequence encodes a 960-amino acid protein with significant homology to placental leucine aminopeptidase and adipocyte-derived leucine aminopeptidase. The predicted L-RAP contains the HEXXH(X) 18 E zinc-binding motif, which is characteristic of the M1 family of zinc metallopeptidases. Phylogenetic analysis indicates that L-RAP forms a distinct subfamily with placental leucine aminopeptidase and adipocyte-derived leucine aminopeptidase in the M1 family. Immunocytochemical analysis indicates that L-RAP is located in the lumenal side of the endoplasmic reticulum. Among various synthetic substrates tested, L-RAP revealed a preference for arginine, establishing that the enzyme is a novel arginine aminopeptidase with restricted substrate specificity. In addition to natural hormones such as angiotensin III and kallidin, L-RAP cleaved various N-terminal extended precursors to major histocompatibility complex class I-presented antigenic peptides. Like other proteins involved in antigen presentation, L-RAP is induced by interferon-␥. These results indicate that L-RAP is a novel aminopeptidase that can trim the N-terminal extended precursors to antigenic peptides in the endoplasmic reticulum.

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Molecular cloning of the human kidney differentiation antigen gp160: human aminopeptidase A.

Cited by 104 publications

References 34 publications

Identification of novel hypoxia dependent and independent target genes of the von Hippel-Lindau (VHL) tumour suppressor by mRNA differential expression profiling

Identification of novel hypoxia dependent and independent target genes of the von Hippel-Lindau (VHL) tumour suppressor by mRNA differential expression profiling

Caveolin-1 Triggers T-cell Activation via CD26 in Association with CARMA1

Human Leukocyte-derived Arginine Aminopeptidase

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