The Calgranulins, Members of the S-100 Protein Family: Structural Features, Expression, and Possible Function

Longbottom, David; Heyningen, Veronica van

doi:10.1007/978-3-642-76150-8_12

Cited by 2 publications

(2 citation statements)

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“…Isoforms a, b, c of MRP-14 recognized by the polyclonal antibody anti-MRP8 were found to correspond to the different proteins reacting with the monoclonal antibody 5.5 used in the work of Edgeworth et al (1989). This mAb 5.5 recognized one isoform of MRP-8, whereas our anti-MRP8 reacted with about four variants suggesting post-translational modifications, since MRP-8 is the product of a single gene, as is the case for MRP-14 (Longbottom and Van Heyningen, 1991). This difference in the observed number of isoforms could be explained by the western blotting detection system.…”

Section: Discussionmentioning

confidence: 69%

“…This mAb 5.5 recognized one isoform of MRP-8, whereas our anti-MRP8 reacted with about four variants suggesting post-translational modifications, since MRP-8 is the product of a single gene, as is the case for MRP-14 (Longbottom and Van Heyningen, 1991). This difference in the observed number of isoforms could be explained by the western blotting detection system.…”

Section: Discussionmentioning

confidence: 72%

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Phosphorylation of Myeloid‐Related Proteins MRP‐14 and MRP‐8 During Human Neutrophil Activation

Guignard

Mauël²,

Markert

1996

European Journal of Biochemistry

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The myeloid-related proteins MRP-14 and MRP-8 and also p6, three calcium-binding proteins of the SlOO family, translocate to the membrane during human neutrophil activation with stimuli known to require extracellular calcium for activity. When phorbol 12-myristate 13-acetate (PMA, an extracellular calcium-independent stimulus) is used, no translocation is observed. To characterize further the mechanisms involved in their translocation, phosphorylation of these proteins was studied.Three isoforms of MRP-14 were markedly phosphorylated in the membrane and in the cytosol upon activation with extracellular calcium-dependent stimuli, such as opsonized zymosan, the calcium ionophore A23187, N-formylmethionylleucylphenylalanine in the presence of cytochalasin B and arachidonic acid, or upon extracellular calcium-independent stimulation (PMA). In no case were p6 and a fourth, more basic isoform of MRP-14, phosphorylated. In PMA-activated cells, a phosphorylated acidic isoform of MRP-8 was detected in the cytosol only. However, phosphorylated MRP-8 represented only a small fraction of total MRP-8. Cgp 41251, an inhibitor of protein kinase C (PKC), completely inhibited the phosphorylation of MRP-8, and decreased cytosolic MRP-14 phosphorylation. To test whether phosphorylated MRP-8 could translocate, A231 87, which induces translocation of the three SlOO proteins, was added after PMA activation. This resulted in translocation of 18 % 2 5 % of phosphorylated MRP-14 and 19 % 2 1 % of only nonphosphorylated MRP-8. However, upon inhibition of PKC, translocation of MRP-14 and MRP-8 was increased up to 38% 1-7% and 34% 2 3% respectively. This suggests a putative role of phosphorylation and/or of PKC in the modulation of MRP-14 and MRP-8 translocation to the membrane.

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Section: Discussionmentioning

confidence: 69%

Section: Discussionmentioning

confidence: 72%

Phosphorylation of Myeloid‐Related Proteins MRP‐14 and MRP‐8 During Human Neutrophil Activation

Guignard

Mauël²,

Markert

1996

European Journal of Biochemistry

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The calcium‐binding proteins MRP8 and MRP14 form a membrane‐associated heterodimer in a subset of monocytes/macrophages present in acute but absent in chronic inflammatory lesions

et al. 1992

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Monocytes/macrophages expressing an epitope recognized by a monoclonal antibody 27E10 are present in acute but are absent in chronic inflammatory disorders. This report shows that the 27E10 antigen is formed by noncovalent association of the two Ca(2+)-binding proteins MRP8 and MRP14 which belong to the S100 protein family. Identification has been confirmed immunochemically, by matrix-assisted UV-laser desorption/ionization spectrometry and by partial amino acid sequencing. Surface expression of the MRP8/MRP14 complex on a subset of monocytes is reported for the first time and shown to be up-regulated in a Ca(2+)-dependent manner. The 27E10 surface-positive monocytes isolated by cell separation techniques release high amounts of tumor necrosis factor-alpha and interleukin-1 beta in contrast to their 27E10 surface-negative counterparts thus emphasizing their role in inflammation.

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The Calgranulins, Members of the S-100 Protein Family: Structural Features, Expression, and Possible Function

Cited by 2 publications

References 147 publications

Phosphorylation of Myeloid‐Related Proteins MRP‐14 and MRP‐8 During Human Neutrophil Activation

Phosphorylation of Myeloid‐Related Proteins MRP‐14 and MRP‐8 During Human Neutrophil Activation

The calcium‐binding proteins MRP8 and MRP14 form a membrane‐associated heterodimer in a subset of monocytes/macrophages present in acute but absent in chronic inflammatory lesions

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