Neutrophil gelatinase-associated lipocalin
From Proteopedia
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== Function == | == Function == | ||
| - | '''Neutrophil gelatinase-associated lipocalin''' (NGAL) or '''lipocalin-2''' is involved in innate immunity by sequestering bacterial iron and thus preventing bacterial growth<ref>PMID:10475571</ref>. | + | '''Neutrophil gelatinase-associated lipocalin''' (NGAL) or '''lipocalin-2''' is involved in innate immunity by sequestering bacterial iron and thus preventing bacterial growth<ref>PMID:10475571</ref>. '''Lipocalin-1''' (Lcn1) or '''Tear lipocalin''' is a major protein in tears which binds diverse set of lipophilic molecules <ref>PMID:21791187</ref>. |
== Relevance == | == Relevance == | ||
| - | NGAL is secreted in high levels into the blood following acute kidney injury and thus can be used as a biomarker for it<ref>PMID:20921623</ref>. | + | NGAL is secreted in high levels into the blood following acute kidney injury and thus can be used as a biomarker for it<ref>PMID:20921623</ref>. Lcn1 functions in tears includes their viscosity and it serves as biomarker for dry eyes. |
== Structural highlights == | == Structural highlights == | ||
Revision as of 10:32, 11 May 2016
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3D structures of neutrophil gelatinase-associated lipocalin
Updated on 11-May-2016
References
- ↑ Friedl A, Stoesz SP, Buckley P, Gould MN. Neutrophil gelatinase-associated lipocalin in normal and neoplastic human tissues. Cell type-specific pattern of expression. Histochem J. 1999 Jul;31(7):433-41. PMID:10475571
- ↑ Dartt DA. Tear lipocalin: structure and function. Ocul Surf. 2011 Jul;9(3):126-38. PMID:21791187
- ↑ Viau A, El Karoui K, Laouari D, Burtin M, Nguyen C, Mori K, Pillebout E, Berger T, Mak TW, Knebelmann B, Friedlander G, Barasch J, Terzi F. Lipocalin 2 is essential for chronic kidney disease progression in mice and humans. J Clin Invest. 2010 Nov;120(11):4065-76. doi: 10.1172/JCI42004. PMID:20921623 doi:http://dx.doi.org/10.1172/JCI42004
- ↑ Holmes MA, Paulsene W, Jide X, Ratledge C, Strong RK. Siderocalin (Lcn 2) also binds carboxymycobactins, potentially defending against mycobacterial infections through iron sequestration. Structure. 2005 Jan;13(1):29-41. PMID:15642259 doi:10.1016/j.str.2004.10.009
