The Fatty Acid-Binding Heterocomplex FA-p34 Formed by S100A8 and S100A9 Is the Major Fatty Acid Carrier in Neutrophils and Translocates from the Cytosol to the Membrane upon Stimulation

Roulin, Karen; Hagens, Gerry; Hotz, Raymonde; Saurat, Jean‐Hilaire; Veerkamp, J.H.; Siegenthaler, Georges

doi:10.1006/excr.1998.4382

Cited by 32 publications

(25 citation statements)

References 27 publications

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“…Although the homozygous deletion of MRP-8 results in embryonic lethality (26) (28). MRP-8/14 further appears to modulate calcium-coupled arachidonic acid signaling by binding to arachidonic acid in a calcium-dependent manner (29,30) and by facilitating translocation of arachidonic acid to the cytoskeleton (31,32). Intracellular MRP-8/14 also modulates cytoskeletal reorganization by promoting polymerization of microtubules (6).…”

Section: Discussionmentioning

confidence: 99%

Myeloid-related protein-14 regulates deep vein thrombosis

et al. 2017

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Section: Discussionmentioning

confidence: 99%

Myeloid-related protein-14 regulates deep vein thrombosis

et al. 2017

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“…Experiments with leukocytes isolated from Mrp14 -/-mice have demonstrated aberrant calcium signaling and blunted calcium responses following chemokine stimulation (34). MRP-8/14 further appears to modulate calcium-coupled arachidonic acid signaling by binding to arachidonic acid in a calcium-dependent manner (35,36) and by facilitating translocation of arachidonic acid to the cytoskeleton (37,38). Intracellular MRP-8/14 also modulates cytoskeletal reorganization by promoting polymerization of microtubules (6).…”

Section: Discussionmentioning

confidence: 99%

Platelet-derived S100 family member myeloid-related protein-14 regulates thrombosis

et al. 2014

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Expression of the gene encoding the S100 calcium-modulated protein family member MRP-14 (also known as S100A9) is elevated in platelets from patients presenting with acute myocardial infarction (MI) compared with those from patients with stable coronary artery disease; however, a causal role for MRP-14 in acute coronary syndromes has not been established. Here, using multiple models of vascular injury, we found that time to arterial thrombotic occlusion was markedly prolonged in Mrp14 -/-mice. We observed that MRP-14 and MRP-8/ MRP-14 heterodimers (S100A8/A9) are expressed in and secreted by platelets from WT mice and that thrombus formation was reduced in whole blood from Mrp14 -/-mice. Infusion of WT platelets, purified MRP-14, or purified MRP-8/MRP-14 heterodimers into Mrp14 -/-mice decreased the time to carotid artery occlusion after injury, indicating that platelet-derived MRP-14 directly regulates thrombosis. In contrast, infusion of purified MRP-14 into mice deficient for both MRP-14 and CD36 failed to reduce carotid occlusion times, indicating that CD36 is required for MRP-14-dependent thrombosis. Our data identify a molecular pathway of thrombosis that involves platelet MRP-14 and CD36 and suggest that targeting MRP-14 has potential for treating atherothrombotic disorders, including MI and stroke.

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“…This complex has been shown to inhibit the activity of casein kinase I and II [12]. Recent studies suggest that MRP8/P14 complex is the major fatty acid (FA) carrier in human neutrophils [13].…”

Section: Discussionmentioning

confidence: 99%

Expression of MRP14 gene is frequently down-regulated in Chinese human esophageal cancer

Wang

Cai

et al. 2004

Cell Res

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Migration inhibitory factor-related protein 14 (MRP14) is one of calcium-binding proteins, referred as S100A9. The heterodimeric molecule formed by MRP14 with its partner MRP8 (S100A8) is the major fatty acid carrier in neutrophils. The MRP8/14 complex has been also implicated in the intracellular transport of arachidonic acid and its precursors in keratinocytes. We show here the involvement of MRP14 in human esophageal cancer. In an initial study, mRNA differential display -reverse transcription polymerase chain reaction (DD-PCR) was performed with two esophageal carcinomas, one esophageal adenocarcinoma and matched normal adjacent mucosa. DD-PCR with the arbitrary primer OPA3 showed that one cDNA band was highly expressed in normal tissues, but disappeared or substantially decreased in tumor counterparts. It was later identified to be the 3'-end of migration inhibitory factor-related protein 14 (MRP14). Northern blotting, RT-PCR and Western blotting corroborated the down-regulation of MRP14 in 58/64 squamous cell carcinomas and 2/2 adenocarcinomas as compared with adjacent normal epithelia of the esophagus. MRP14 was undetectable in 3/3 esophageal-carcinoma cell lines. Immunochemistry demonstrated that expression of MRP14 was restricted to normal esophageal epithelia. No mutation was found in the genomic DNA of the MRP14 gene by PCR and directed DNA sequencing. Our finding suggested that the reduction of MRP14 expression is a frequent event in Chinese human esophageal cancer.

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The Fatty Acid-Binding Heterocomplex FA-p34 Formed by S100A8 and S100A9 Is the Major Fatty Acid Carrier in Neutrophils and Translocates from the Cytosol to the Membrane upon Stimulation

Cited by 32 publications

References 27 publications

Myeloid-related protein-14 regulates deep vein thrombosis

Myeloid-related protein-14 regulates deep vein thrombosis

Platelet-derived S100 family member myeloid-related protein-14 regulates thrombosis

Expression of MRP14 gene is frequently down-regulated in Chinese human esophageal cancer

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