Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.5.1.12 (biotinidase)
392 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Migration of hematopoietic precursor cells to the thymus is shown to depend upon a novel molecule called Vanin-1 expressed by perivascular thymic stromal cells. An anti-Vanin-1 antibody blocks the binding of pro-T cells to thymic sections in vitro, the in vivo accumulation of bone marrow cells around cortical thymic vessels, and long-term thymic regeneration. Thus, it interferes with the entry, and not the differentiation, of hematopoietic precursor cells. The Vanin-1 gene codes for a GPI-anchored 70 kDa protein that shows homology only with human biotinidase. Transfection of thymic stromal cells with the Vanin-1 cDNA enhances thymocyte adhesion in vitro. These data suggest that Vanin-1 regulates late adhesion steps of thymus homing under physiological, noninflammatory conditions.
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PMID:Vanin-1, a novel GPI-linked perivascular molecule involved in thymus homing. 893 67

We report here the identification of two distinct human cDNAs, called VNN1 and VNN2, related to the recently described mouse Vanin-1 molecule involved in lymphocyte migration (M. Aurrand-Lions et al., 1996, Immunity 5: 391-405). Tissue distribution of the expression of these two human Vanin-like genes is differential. Since Vanin-1 shares significant homologies with human biotinidase (BTD), we describe here a new family of related genes including at least four members: mouse Vanin-1, VNN1, VNN2, and BTD. We have mapped the murine locus encompassing the Vanin-1 gene on mouse chromosome 10 in position A2B1. The two human Vanin-like genes are closely linked, since they were found on the same YAC clone and colocalized on human chromosome 6q23-q24 known to contain several genetic alterations linked to the progression of metastatic human cancers.
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PMID:Two human genes related to murine vanin-1 are located on the long arm of human chromosome 6. 979 Jul 69

We report here a novel glycosylphosphatidyl-inositol (GPI)-anchored glycoprotein on human leukocytes. Treatment of neutrophils with a mAb (3H9) to this molecule sequentially up-regulates and down-regulates beta2 integrin-dependent adhesion of these cells as well as their transendothelial migration in vitro. In addition, this mAb simultaneously modulates the avidity of beta2 integrin for its ligand, iC3b, with kinetics similar to those observed in 3H9 modulation of neutrophil adherence. This mAb also induces beta2 integrin-dependent cytoskeletal remodeling. This novel GPI-anchored protein (GPI-80) is highly homologous with Vanin-1, a recently reported GPI-anchored protein that is expressed on perivascular thymic stromal cells and is involved in thymus homing in mice. The finding that both GPI-80 and Vanin-1 are 40% homologous with human biotinidase suggests the existence of a biotinidase superfamily of molecules that may be involved in the regulation of leukocyte trafficking.
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PMID:A novel glycosylphosphatidyl inositol-anchored protein on human leukocytes: a possible role for regulation of neutrophil adherence and migration. 1020 59

Pantetheinase is an amidohydrolase involved in the dissimilative pathway of CoA, allowing the turnover of the pantothenate moiety. We have determined the N-terminal sequence as well as the sequences of a number of tryptic and chymotryptic peptides of the protein isolated from pig kidney. These sequence stretches were used as probes to search in the SwissProt database and significant similarities were found with a GPI-anchored protein (mouse vanin-1, with a suggested role in lymphocyte migration), with two putative proteins encoded by human cDNAs (VNN1 and VNN2) and with human biotinidase. On the basis of sequence similarity, we propose that vanin-1 and VNN1 should be identified as pantetheinase.
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PMID:Is pantetheinase the actual identity of mouse and human vanin-1 proteins? 1056 87