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A Protocol for the Production of KLRG1 Tetramer
Killer cell lectin-like receptor G1 (KLRG1) is a type II transmembrane glycoprotein inhibitory receptor belonging to the C type lectin-like superfamily. KLRG1 exists both as a monomer and as a disulfide-linked homodimer. This well-conserved receptor is found on the most mature and recently activated...
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Formato: | Texto |
Lenguaje: | English |
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MyJove Corporation
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2848686/ https://www.ncbi.nlm.nih.gov/pubmed/20068548 http://dx.doi.org/10.3791/1701 |
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author | Terrizzi, Stephanie C. Banh, Cindy Brossay, Laurent |
author_facet | Terrizzi, Stephanie C. Banh, Cindy Brossay, Laurent |
author_sort | Terrizzi, Stephanie C. |
collection | PubMed |
description | Killer cell lectin-like receptor G1 (KLRG1) is a type II transmembrane glycoprotein inhibitory receptor belonging to the C type lectin-like superfamily. KLRG1 exists both as a monomer and as a disulfide-linked homodimer. This well-conserved receptor is found on the most mature and recently activated NK cells as well as on a subset of effector/memory T cells. Using KLRG1 tetramer as well as other methods, E-, N-, and R-cadherins were identified as KLRG1 ligands. These Ca(2+)-dependent cell-cell adhesion molecules comprises of an extracellular domain containing five cadherin repeats responsible for cell-cell interactions, a transmembrane domain and a cytoplasmic domain that is linked to the actin cytoskeleton. Generation of the KLRG1 tetramer was essential to the identification of the KLRG1 ligands. KLRG1 tetramer is also a unique tool to elucidate the roles cadherin and KLRG1 play in regulating the immune response and tissue integrity. |
format | Text |
id | pubmed-2848686 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | MyJove Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-28486862012-01-12 A Protocol for the Production of KLRG1 Tetramer Terrizzi, Stephanie C. Banh, Cindy Brossay, Laurent J Vis Exp Microbiology Killer cell lectin-like receptor G1 (KLRG1) is a type II transmembrane glycoprotein inhibitory receptor belonging to the C type lectin-like superfamily. KLRG1 exists both as a monomer and as a disulfide-linked homodimer. This well-conserved receptor is found on the most mature and recently activated NK cells as well as on a subset of effector/memory T cells. Using KLRG1 tetramer as well as other methods, E-, N-, and R-cadherins were identified as KLRG1 ligands. These Ca(2+)-dependent cell-cell adhesion molecules comprises of an extracellular domain containing five cadherin repeats responsible for cell-cell interactions, a transmembrane domain and a cytoplasmic domain that is linked to the actin cytoskeleton. Generation of the KLRG1 tetramer was essential to the identification of the KLRG1 ligands. KLRG1 tetramer is also a unique tool to elucidate the roles cadherin and KLRG1 play in regulating the immune response and tissue integrity. MyJove Corporation 2010-01-12 /pmc/articles/PMC2848686/ /pubmed/20068548 http://dx.doi.org/10.3791/1701 Text en Copyright © 2010, Journal of Visualized Experiments http://creativecommons.org/licenses/by/2.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Microbiology Terrizzi, Stephanie C. Banh, Cindy Brossay, Laurent A Protocol for the Production of KLRG1 Tetramer |
title | A Protocol for the Production of KLRG1 Tetramer |
title_full | A Protocol for the Production of KLRG1 Tetramer |
title_fullStr | A Protocol for the Production of KLRG1 Tetramer |
title_full_unstemmed | A Protocol for the Production of KLRG1 Tetramer |
title_short | A Protocol for the Production of KLRG1 Tetramer |
title_sort | protocol for the production of klrg1 tetramer |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2848686/ https://www.ncbi.nlm.nih.gov/pubmed/20068548 http://dx.doi.org/10.3791/1701 |
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