Mediates adhesion of proximal tubule epithelial cells via integrins alpha3-beta1 and alphaV-beta3. This is a non catalytic peptidase C1 family protein.
Tubulointerstitial nephritis antigen (TIN-ag) is a novel basement membrane macromolecule that is involved in human antitubular-basement-membrane-mediated tubulointerstitial nephritis. The presence of antibodies to TIN-ag may result in an alteration of proximal tubule epithelial cell interaction with surrounding matrix and contribute to the pathogenesis of immune-mediated tubulointerstitial disease. To study the adhesive interactions between TIN-ag and proximal tubule epithelial cells and the macromolecules that mediate these interactions, an immortalized proximal tubular epithelial cell line from normal adult human kidney (HK-2) was used. Plastic-coated TIN-ag was able to promote adhesion of HK-2 cells in a concentration-dependent manner. the strength of the adhesive interaction was comparable to that of type IV collagen or laminin. to explore which members of the integrin family of cell surface receptors were involved in this interaction, we performed fluorescence activated cell sorting (FACS) analysis and adhesion-inhibition studies using monoclonal antibodies against various integrins. Both approaches suggested that integrins alpha 3 beta 1 and alpha 5 beta 3 are crucial for the adhesion of proximal tubule epithelial cells on TIN-ag, and that they are probably using independent domains of TIN-ag for their action. These data will help us to understand the interactions between proximal tubule epithelial cells and the underlying basement membrane, and will provide tubule clues to the pathogenesis of kidney tubular diseases at the molecular level.
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile.
Tubulointerstitial nephritis antigen (TIN-ag) is an extracellular matrix basement protein which was originally identified as a target antigen involved in anti-tubular basement membrane (TBM) antibody-mediated interstitial nephritis (TIN). Further investigations elucidated that TIN-ag plays a role in renal tubulogenesis and that TIN-ag is defected in hereditary tubulointerstitial disorder such as juvenile nephronophthisis. We previously isolated and characterized 54 kDa glycoprotein as TIN-ag. cDNA encoding rabbit and mouse TIN-ag has recently been identified. In the present study, the cDNA of the human homologue of TIN-ag was cloned and its nucleotide sequence was determined (Accession No. AB022277; the DDBJ nucleotide sequence database). Deduced amino acid sequence (476 aa) exhibited the presence of a signal peptide (1-18 aa), cysteine residues termed follistatin module, six potential glycosylation sites, and an ATP/GTP-binding site. Homology search revealed approximately 85% homology with both rabbit and mouse TIN-ag, and also some ( approximately 40%) similarity with C. elegans. Human TIN-ag contained a sequence similar to several classes of extracellular matrix molecules in amino terminal region and to cathepsin family of cysteine proteinases in the carboxyl terminal region. Northern blot analysis revealed exclusive expression of this molecule in human adult and fetal kidney tissues. Using a monoclonal antibody recognizing human TIN-ag, protein expression ( approximately 50 kDa) was identified in cultured COS-1 cells transfected with human TIN-ag cDNA. The human TIN-ag was mapped to chromosome 6p11.2-12 by fluorescence in situ hybridization. These results may provide further evidence for understanding TIN-ag molecule and clues for gene analysis of juvenile nephronophthisis.
Interacting selectively and non-covalently with a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
Tubulointerstitial nephritis antigen (TIN-ag) is an extracellular matrix basement protein which was originally identified as a target antigen involved in anti-tubular basement membrane (TBM) antibody-mediated interstitial nephritis (TIN). Further investigations elucidated that TIN-ag plays a role in renal tubulogenesis and that TIN-ag is defected in hereditary tubulointerstitial disorder such as juvenile nephronophthisis. We previously isolated and characterized 54 kDa glycoprotein as TIN-ag. cDNA encoding rabbit and mouse TIN-ag has recently been identified. In the present study, the cDNA of the human homologue of TIN-ag was cloned and its nucleotide sequence was determined (Accession No. AB022277; the DDBJ nucleotide sequence database). Deduced amino acid sequence (476 aa) exhibited the presence of a signal peptide (1-18 aa), cysteine residues termed follistatin module, six potential glycosylation sites, and an ATP/GTP-binding site. Homology search revealed approximately 85% homology with both rabbit and mouse TIN-ag, and also some ( approximately 40%) similarity with C. elegans. Human TIN-ag contained a sequence similar to several classes of extracellular matrix molecules in amino terminal region and to cathepsin family of cysteine proteinases in the carboxyl terminal region. Northern blot analysis revealed exclusive expression of this molecule in human adult and fetal kidney tissues. Using a monoclonal antibody recognizing human TIN-ag, protein expression ( approximately 50 kDa) was identified in cultured COS-1 cells transfected with human TIN-ag cDNA. The human TIN-ag was mapped to chromosome 6p11.2-12 by fluorescence in situ hybridization. These results may provide further evidence for understanding TIN-ag molecule and clues for gene analysis of juvenile nephronophthisis.
Combining with any modified low-density lipoprotein (LDL) or other polyanionic ligand and delivering the ligand into the cell via endocytosis. Ligands include acetylated and oxidized LDL, Gram-positive and Gram-negative bacteria, apoptotic cells, beta-amyloid fibrils, and advanced glycation end products (AGEs).
Tubulointerstitial nephritis antigen (TIN-ag) is a novel basement membrane macromolecule that is involved in human antitubular-basement-membrane-mediated tubulointerstitial nephritis. The presence of antibodies to TIN-ag may result in an alteration of proximal tubule epithelial cell interaction with surrounding matrix and contribute to the pathogenesis of immune-mediated tubulointerstitial disease. To study the adhesive interactions between TIN-ag and proximal tubule epithelial cells and the macromolecules that mediate these interactions, an immortalized proximal tubular epithelial cell line from normal adult human kidney (HK-2) was used. Plastic-coated TIN-ag was able to promote adhesion of HK-2 cells in a concentration-dependent manner. the strength of the adhesive interaction was comparable to that of type IV collagen or laminin. to explore which members of the integrin family of cell surface receptors were involved in this interaction, we performed fluorescence activated cell sorting (FACS) analysis and adhesion-inhibition studies using monoclonal antibodies against various integrins. Both approaches suggested that integrins alpha 3 beta 1 and alpha 5 beta 3 are crucial for the adhesion of proximal tubule epithelial cells on TIN-ag, and that they are probably using independent domains of TIN-ag for their action. These data will help us to understand the interactions between proximal tubule epithelial cells and the underlying basement membrane, and will provide tubule clues to the pathogenesis of kidney tubular diseases at the molecular level.
A reference proteome is a set of protein sequences derived from a complete proteome which constitutes a defined standard for a particular user community. Reference proteomes are manually defined according to a number of criteria. They cover the proteomes of well- studied model organisms and other proteomes of interest for biomedical and biotechnological research. Reference proteomes have been selected to provide broad coverage of the tree of life, and constitute a representative cross-section of the taxonomic diversity to be found within UniProtKB.
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