Bates Elizabeth E M, Fridman Wolf H, Mueller Chris G F
The ADAMDEC1 (decysin) gene structure: evolution by duplication in a metalloprotease gene cluster on chromosome 8p12 Article de journal
Dans: Immunogenetics, vol. 54, no. 2, p. 96–105, 2002, ISSN: 0093-7711.
Résumé | Liens | BibTeX | Étiquettes: ADAM Proteins, Amino Acid Sequence, Animals, Base Sequence, Chromosomes, Evolution, Gene Dosage, Gene Duplication, Genetic, Human, Humans, Inbred BALB C, Macaca mulatta, Membrane Glycoproteins, Metalloendopeptidases, Mice, Molecular, Molecular Sequence Data, Multigene Family, Pair 8, Promoter Regions, Sequence Alignment, Team-Mueller
@article{bates_adamdec1_2002,
title = {The ADAMDEC1 (decysin) gene structure: evolution by duplication in a metalloprotease gene cluster on chromosome 8p12},
author = {Elizabeth E M Bates and Wolf H Fridman and Chris G F Mueller},
doi = {10.1007/s00251-002-0430-3},
issn = {0093-7711},
year = {2002},
date = {2002-05-01},
journal = {Immunogenetics},
volume = {54},
number = {2},
pages = {96--105},
abstract = {Members of the ADAM superfamily of metalloprotease genes are involved in a number of biological processes, including fertilization, neurogenesis, muscle development, and the immune response. These proteins have been classified into several groups. The prototypic ADAM family is comprised of a pro-domain, a metalloprotease domain, a disintegrin domain, a cysteine-rich region, a transmembrane domain, and a variable cytoplasmic tail. We recently identified a novel member of this superfamily, ADAMDEC1 (decysin). Due to the partial lack of a disintegrin domain and the total lack of a cysteine-rich domain, this protein has been placed in a novel subclass of the ADAM gene family. We have investigated the gene structure of the human and mouse ADAMDEC1 and have revealed a metalloprotease gene cluster on human Chromosome 8p12 comprising ADAMDEC1, ADAM7, and ADAM28. Our results suggest that ADAMDEC1 has arisen by partial gene duplication from an ancestral gene at this locus and has acquired a novel function. ADAMDEC1 is expressed in the immune system, by dendritic cells and macrophages. The relatedness of ADAMDEC1, ADAM7, and ADAM28 suggests that these proteases share a similar function.},
keywords = {ADAM Proteins, Amino Acid Sequence, Animals, Base Sequence, Chromosomes, Evolution, Gene Dosage, Gene Duplication, Genetic, Human, Humans, Inbred BALB C, Macaca mulatta, Membrane Glycoproteins, Metalloendopeptidases, Mice, Molecular, Molecular Sequence Data, Multigene Family, Pair 8, Promoter Regions, Sequence Alignment, Team-Mueller},
pubstate = {published},
tppubtype = {article}
}
Mueller C G, Cremer I, Paulet P E, Niida S, Maeda N, Lebeque S, Fridman W H, Sautès-Fridman C
Mannose receptor ligand-positive cells express the metalloprotease decysin in the B cell follicle Article de journal
Dans: Journal of Immunology (Baltimore, Md.: 1950), vol. 167, no. 9, p. 5052–5060, 2001, ISSN: 0022-1767.
Résumé | Liens | BibTeX | Étiquettes: ADAM Proteins, Amino Acid Sequence, Animals, B-Lymphocytes, C-Type, Cell Surface, Cloning, Dendritic Cells, Follicular, Germinal Center, Humans, Inbred BALB C, Lectins, ligands, Macrophage Colony-Stimulating Factor, Macrophages, Mannose-Binding Lectins, Metalloendopeptidases, Mice, Molecular, Molecular Sequence Data, Receptors, SPLEEN, Team-Mueller
@article{mueller_mannose_2001,
title = {Mannose receptor ligand-positive cells express the metalloprotease decysin in the B cell follicle},
author = {C G Mueller and I Cremer and P E Paulet and S Niida and N Maeda and S Lebeque and W H Fridman and C Sautès-Fridman},
doi = {10.4049/jimmunol.167.9.5052},
issn = {0022-1767},
year = {2001},
date = {2001-11-01},
journal = {Journal of Immunology (Baltimore, Md.: 1950)},
volume = {167},
number = {9},
pages = {5052--5060},
abstract = {Decysin, a gene encoding a disintegrin metalloprotease, is transcribed in human dendritic cells (DC) and germinal centers (GC). We have cloned its murine homologue and show that it is processed by the endoprotease furin before secretion of the catalytic domain. We have defined the cell types that express decysin in mouse spleen in the course of an immune response to T cell-dependent Ags. Like in humans, decysin is transcribed by activated CD11c(+) DC that enter the T cell zone from the marginal zone (MZ). In the GC, decysin is expressed by follicular DC and tingible body macrophages. In addition, a MZ cell population expresses decysin and appears to migrate into the B cell follicle. The majority of these follicle-homing cells express the mannose receptor ligand, a marker for the macrophage-like MZ metallophils. The follicle-homing cells are M-CSF dependent, as they are absent in op/op mice that lack functional M-CSF. This suggests that mannose receptor ligand(+) MZ metallophils differentiate into cells that migrate from the MZ into the B cell follicle. Decysin represents the first marker for this previously unrecognized cell population of the mouse spleen, which may represent a precursor for GCDC and may be specialized in the transport of unprocessed Ag from the MZ into developing GC.},
keywords = {ADAM Proteins, Amino Acid Sequence, Animals, B-Lymphocytes, C-Type, Cell Surface, Cloning, Dendritic Cells, Follicular, Germinal Center, Humans, Inbred BALB C, Lectins, ligands, Macrophage Colony-Stimulating Factor, Macrophages, Mannose-Binding Lectins, Metalloendopeptidases, Mice, Molecular, Molecular Sequence Data, Receptors, SPLEEN, Team-Mueller},
pubstate = {published},
tppubtype = {article}
}