Ask about this productRelated genes to: TINAG Blocking Peptide
- Gene:
- TINAG NIH gene
- Name:
- tubulointerstitial nephritis antigen
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 6p12.1
- Locus Type:
- gene with protein product
- Date approved:
- 2001-04-05
- Date modifiied:
- 2015-09-08
- Gene:
- TINAGL1 NIH gene
- Name:
- tubulointerstitial nephritis antigen like 1
- Previous symbol:
- LCN7
- Synonyms:
- P3ECSL, LIECG3, ARG1, TINAGRP
- Chromosome:
- 1p35.2
- Locus Type:
- gene with protein product
- Date approved:
- 2002-08-29
- Date modifiied:
- 2016-10-05
Related products to: TINAG Blocking Peptide
Related articles to: TINAG Blocking Peptide
- Secreted wingless-interacting protein (Swim) is the ortholog gene of the mammalian Tubulointerstitial Nephritis Antigen like 1 (TINAGL1), also known as lipocalin-7 (LCN7), or adrenocortical zonation factor 1 (AZ-1). Swim and TINAGL1 proteins share a significant homology, including the somatomedin B and the predictive inactive C1 cysteine peptidase domains. In mammals, both TINAGL1 and its closely related homolog TINAG have been identified in basement membranes, where they may function as modulators of integrin-mediated adhesion. In , Swim was initially identified in the eggshell matrix and was subsequently detected in the culture medium of S2 cells. Further biochemical analysis indicated that Swim binds to wingless (wg) in a lipid-dependent manner. This observation, together with RNAi-knockdown studies, suggested that Swim is an essential cofactor of wg-signalling. However, recent elegant genetic studies ruled out the possibility that Swim is required alone to facilitate wg-signalling in , because flies without Swim are viable and fertile. Here, we use the UAS/Gal4 expression system together with confocal imaging to analyze the localization of a chimeric Swim-GFP in the developing embryo. Our data fully support the notion that Swim is an extracellular matrix component that is secreted upon ectopic expression and preferentially associates with the basement membranes of various organs and with the specialized tendon matrix at the muscle attachment sites (MAS). Interestingly, the accumulation of Swim at the MAS does not require integrins. In conclusion, Swim is an extracellular matrix component, and Swim may exhibit overlapping functions in concert with other undefined components. - Source: PubMed
Kaltezioti ValeriaVakaloglou Katerina MCharonis Aristidis SZervas Christos G - A human cDNA of 2166 bp encoding a novel cathepsin B-related protein was isolated and characterized. The amino acid sequence of the predicted protein of 467 aa was 46% identical with that of human tubulointerstitial nephritis antigen (TIN-ag), and therefore, the protein was tentatively designated as the TIN-ag-related protein (TIN-ag-RP). The amino acid sequence of TIN-ag-RP is composed of a 21 aa long signal sequence, a 181 aa long N-terminal domain containing two epidermal growth factor-like domains, a follistatin motif, and a 265 aa long cathepsin B-like domain. Interestingly, a serine residue has replaced the active site cysteine residue in the cathepsin B-like domain, resulting in a proteolytically inactive protein. Evolutionary analysis revealed that a distinct family of "TIN-ag-like" proteins had evolved in vertebrates. Northern blot analysis revealed a single TIN-ag-RP transcript of 2.4 kb in various tissues with the highest transcript levels detected in aorta, heart, placenta, skeletal muscle, kidney, and a colorectal adenocarcinoma cell line. Using a polyclonal anti-TIN-ag-RP antibody, TIN-ag-RP expression was predominantly seen in vascular smooth muscle (VSM) cells, but also in cardiac and skeletal muscle cells as well as in kidney. Interestingly, uterine smooth muscle cells completely lacked TIN-ag-RP expression, implying a regulated gene expression. Localization studies in HeLa cells stably transfected with TIN-ag-RP cDNA showed that TIN-ag-RP is glycosylated and actively secreted, a finding in line with its proposed function as a structural or regulatory protein similar to TIN-ag. - Source: PubMed
Wex TLipyansky ABrömme N CWex HGuan X QBrömme D