FABP1

(redirected from L-FABP)
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FABP1

A gene on chromosome 2p11 that encodes a hepatic fatty acid-binding protein that binds long-chain fatty acids, other hydrophobic ligands and bile acids; it may be involved in intracellular lipid transport.
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References in periodicals archive ?
Urinary KIM-1, NGAL and L-FABP for the diagnosis of AKI in patients with acute coronary syndrome or heart failure undergoing coronary angiography.
Although several molecules such as NGAL, KIM-1, IL-18, L-FABP, IL-6, [alpha]/I GST, NAG, IGFBP7, and TIMP-2 have been reported to have a role in the diagnosis of AKI, none has been put into clinical use due to their specific deficiencies and problems particularly concerning their measurement method.1,3,8 Therefore, there is an ongoing search for a sensitive, specific, reliable, easy-to-measure, and cost-effective marker for the early diagnosis of AKI.
Additionally, urinary levels of L-FABP in patients with microalbuminuria were significantly higher than in those with normoalbuminuria [18, 47, 51].
The L-FABP test results are positive both within the tumor and in the surrounding liver parenchyma.
(11) The most promising urinary AKI biomarkers include NGAL, (IL)-18, L-FABP, cystatin C, and KIM-1, but comparison of the AUCs of these biomarkers with clinical and/or routine biochemical outcome parameters reveals that none of these biomarkers has a clear advantage beyond the traditional approach in clinical decision making in patients with AKI.
These molecules have ranged from constitutive proteins released by the damaged kidney (e.g., [alpha] and [pi] glutathione S-transferases, L-FABP) to molecules upregulated in response to injury (e.g., KIM-1 and NGAL) or nonrenal tissue products that are filtered, reabsorbed, or secreted by the kidney (e.g., cystatin C).
However, an isoform specific to the liver called L-FABP exists.
Recombinant liver fatty acid binding protein (L-FABP) and sterol carrier protein-2 (SCP-2) were prepared as described [34, 35].
The expression plasmid for human L-FABP was developed internally and is available from the Plasmid Repository (http://plasmid.med.harvard.edu/PLASMID/) under the plasmid identification codes HsCD00073511.
The relative mRNA abundance of SGLT1, CaBP-D28k, and PepT1 in duodenum and L-FABP in jejunum of broilers is shown in Figure 2.
With a sandwich ELISA method recently developed by Biovendor Laboratory Medicine, Inc., we found that the assay is highly specific for human A-FABP, with no detectable cross-reactivity with other types of FABPs [heart-type FABP (H-FABP), liver-type FABP (L-FABP), or keratinocyte FABP (EFABP)], leptin, adiponectin, resistin, tumor necrosis factor-[alpha], C-reactive protein, or interleukin-6.