Calumenin interacts with serum amyloid P component

Vorum, Henrik; Jacobsen, Christian; Honoré, Bent

doi:10.1016/s0014-5793(99)01734-2

Cited by 42 publications

(28 citation statements)

References 41 publications

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“…cytokines and growth factors in activated Schwann cells. In addition, CALU and RCN2 have been implicated in calciumdependent cell adhesion (55) and CALU in immunological defense (56). Whether these alternative functions of RCN2 and CALU are of importance for peripheral nerve regeneration remains to be established.…”

Section: Discussionmentioning

confidence: 99%

Proteomics of the Injured Rat Sciatic Nerve Reveals Protein Expression Dynamics During Regeneration

Jiménez

Stam

et al. 2005

Molecular & Cellular Proteomics

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Using proteomics, we investigated the temporal expression profiles of proteins in rat sciatic nerve after experimental crush. Extracts of sciatic nerves collected at 5, 10, and 35 days after injury were analyzed by two-dimensional gel electrophoresis and quantitative image analysis. Of the ϳ1,500 protein spots resolved on each gel, 121 showed significant regulation during at least one time point. Using cluster analysis, these proteins were grouped into two expression profiles of down-regulation and four of up-regulation. These profiles mainly reflected differences in cellular origins in addition to different functional roles. Mass spectrometric analysis identified 82 proteins pertaining to several functional classes, i.e. acute-phase proteins, antioxidant proteins, and proteins involved in protein synthesis/maturation/degradation, cytoskeletal (re)organization, and in lipid metabolism. Several proteins not previously implicated in nerve regeneration were identified, e.g. translationally controlled tumor protein, annexin A9/31, vitamin D-binding protein, ␣-crystallin B, ␣-synuclein, dimethylargininases, and reticulocalbin. Real-time PCR analysis of selected genes showed which were expressed in the nerve versus the dorsal root ganglion neurons. In conclusion, this study highlights the complexity and temporal aspect of the molecular process underlying nerve regeneration and points to the importance of glial and inflammatory determinants. Molecular & Cellular Proteomics 4:120 -132, 2005.Injury to a peripheral nerve induces cellular and molecular changes in the injured neurons and in the microenvironment of their axon stumps, which together support axonal regeneration (for a review see Refs. 1-3). During the first week after injury, Wallerian (anterograde) degeneration occurs whereby distal axons and their myelin sheaths are phagocytosed by invading macrophages (4). Schwann cells, deprived of axonal contact, play a key role in regulating macrophage recruitment (5, 6). Moreover, following injury, Schwann cells proliferate and migrate to provide a growth-permissive substrate onto which axons regenerate through the expression of cell adhesion molecules and growth factors (7-10). Thus, the molecular and cellular changes that underly peripheral nerve regeneration are complex and identification of proteins involved will contribute significantly to our understanding of neuroregeneration.To study the molecular mechanisms that govern regeneration of the sciatic nerve, global gene expression profiling of dorsal root ganglia (DRG) 1 and sciatic nerve has been employed recently. These studies revealed that the regenerationassociated genes can be categorized into several groups, including cytoskeletal proteins, neurotransmitter metabolizing enzymes, neuropeptides, growth factors, and signal transduction molecules in the DRG (11-14), as well as genes encoding proteins involved in inflammation, proliferation, and myelination in the nerve (15)(16)(17).Proteomic analysis of the protein expression pattern of the regenerating nerve is ...

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Section: Discussionmentioning

confidence: 99%

Proteomics of the Injured Rat Sciatic Nerve Reveals Protein Expression Dynamics During Regeneration

Jiménez

Stam

et al. 2005

Molecular & Cellular Proteomics

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“…60 It has, however, been shown to bind to serum amyloid P component, which is also released from platelets (Table 2). 61 Calumenin inhibits the activity of vitamin K-dependent ␥-carboxylation 62 responsible for the activation of coagulation factors and proteins such as matrix Gla protein (MGP). 63 Both calumenin and warfarin target the enzyme vitamin K epoxide reductase (VKOR), an integral membrane complex, which converts vitamin K to its hydroquinone form, a cofactor for the enzyme ␥-carboxylase, thus inhibiting the ␥-carboxylation.…”

Section: Characterization Of the Platelet Releasate 2101mentioning

confidence: 99%

Characterization of the proteins released from activated platelets leads to localization of novel platelet proteins in human atherosclerotic lesions

Coppinger

Cagney

Toomey

et al. 2004

Blood

722

540

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Proteins secreted by activated platelets can adhere to the vessel wall and promote the development of atherosclerosis and thrombosis. Despite this biologic significance, however, the complement of proteins comprising the platelet releasate is largely unknown. Using a proteomics approach, we have identified more than 300 proteins released by human platelets following thrombin activation. Many of the proteins identified were not previously attributed to platelets, including secretogranin III, a potential monocyte chemoattractant precursor; cyclophilin A, a vascular smooth muscle cell growth factor; calumenin, an inhibitor of the vitamin K epoxide reductase-warfarin interaction, as well as proteins of unknown function that map to expressed sequence tags. Secretogranin III, cyclophilin A, and calumenin were confirmed to localize in platelets and to be released upon activation. Furthermore, while absent in normal vasculature, they were identified in human atherosclerotic lesions. Therefore, these and other proteins released from platelets may contribute to atherosclerosis and to the thrombosis that complicates the disease. Moreover, as soluble extracellular proteins, they may prove suitable as novel therapeutic targets.

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“…Serum amyloid P component (SAP) was the first protein reported to interact with calumenin in Ca 2+ -dependent fashion (32). This interaction indicates that calumenin may participate in the immunological defense response and could be involved http://bmbreports.org BMB reports in amyloidosis that causes amyloid deposition in different types of tissues.…”

Section: Functional Role Of Calumenin In Non-muscle Cellsmentioning

confidence: 99%

Characterization of calumenin in mouse heart

Sahoo¹,

Kim²

2010

BMB Reports

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Calumenin interacts with serum amyloid P component

Abstract: We recently reported the identification of human calumenin, a novel Ca 2+ binding, transformation-sensitive and secreted protein [Vorum et al. (1998)

Cited by 42 publications

References 41 publications

Proteomics of the Injured Rat Sciatic Nerve Reveals Protein Expression Dynamics During Regeneration

Proteomics of the Injured Rat Sciatic Nerve Reveals Protein Expression Dynamics During Regeneration

Characterization of the proteins released from activated platelets leads to localization of novel platelet proteins in human atherosclerotic lesions

Characterization of calumenin in mouse heart

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