Mimitin – a novel cytokine-regulated mitochondrial protein View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2009-03-31

AUTHORS

Paulina Wegrzyn, Stephen J Yarwood, Nathalie Fiegler, Monika Bzowska, Aleksander Koj, Danuta Mizgalska, Stanisław Malicki, Magdalena Pajak, Aneta Kasza, Neli Kachamakova-Trojanowska, Joanna Bereta, Jacek Jura, Jolanta Jura

ABSTRACT

BACKGROUND: The product of a novel cytokine-responsive gene discovered by differential display analysis in our earlier studies on HepG2 cells was identified as mimitin - a small mitochondrial protein. Since proinflammatory cytokines are known to affect components of the respiratory chain in mitochondria, and mimitin was reported as a possible chaperone for assembly of mitochondrial complex I, we looked for the effects of modulation of mimitin expression and for mimitin-binding partners. RESULTS: By blocking mimitin expression in HepG2 cells by siRNA we found that mimitin has no direct influence on caspase 3/7 activities implicated in apoptosis. However, when apoptosis was induced by TNF and cycloheximide, and mimitin expression blocked, the activities of these caspases were significantly increased. This was accompanied by a slight decrease in proliferation of HepG2 cells. Our observations suggest that mimitin may be involved in the control of apoptosis indirectly, through another protein, or proteins. Using the yeast two-hybrid system and coimmunoprecipitation we found MAP1S among proteins interacting with mimitin. MAP1S is a recently identified member of the microtubule-associated protein family and has been shown to interact with NADH dehydrogenase I and cytochrome oxidase I. Moreover, it was implicated in the process of mitochondrial aggregation and nuclear genome destruction. The expression of mimitin is stimulated more than 1.6-fold by IL-1 and by IL-6, with the maximum level of mimitin observed after 18-24 h exposure to these cytokines. We also found that the cytokine-induced signal leading to stimulation of mimitin synthesis utilizes the MAP kinase pathway. CONCLUSION: Mimitin is a mitochondrial protein upregulated by proinflammatory cytokines at the transcriptional and protein levels, with MAP kinases involved in IL-1-dependent induction. Mimitin interacts with a microtubular protein (MAP1S), and some changes of mimitin gene expression modulate activity of apoptotic caspases 3/7, suggesting that this protein may indirectly participate in apoptosis. More... »

PAGES

23-23

Identifiers

URI

http://scigraph.springernature.com/pub.10.1186/1471-2121-10-23

DOI

http://dx.doi.org/10.1186/1471-2121-10-23

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1016596190

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/19331698


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27 schema:description BACKGROUND: The product of a novel cytokine-responsive gene discovered by differential display analysis in our earlier studies on HepG2 cells was identified as mimitin - a small mitochondrial protein. Since proinflammatory cytokines are known to affect components of the respiratory chain in mitochondria, and mimitin was reported as a possible chaperone for assembly of mitochondrial complex I, we looked for the effects of modulation of mimitin expression and for mimitin-binding partners. RESULTS: By blocking mimitin expression in HepG2 cells by siRNA we found that mimitin has no direct influence on caspase 3/7 activities implicated in apoptosis. However, when apoptosis was induced by TNF and cycloheximide, and mimitin expression blocked, the activities of these caspases were significantly increased. This was accompanied by a slight decrease in proliferation of HepG2 cells. Our observations suggest that mimitin may be involved in the control of apoptosis indirectly, through another protein, or proteins. Using the yeast two-hybrid system and coimmunoprecipitation we found MAP1S among proteins interacting with mimitin. MAP1S is a recently identified member of the microtubule-associated protein family and has been shown to interact with NADH dehydrogenase I and cytochrome oxidase I. Moreover, it was implicated in the process of mitochondrial aggregation and nuclear genome destruction. The expression of mimitin is stimulated more than 1.6-fold by IL-1 and by IL-6, with the maximum level of mimitin observed after 18-24 h exposure to these cytokines. We also found that the cytokine-induced signal leading to stimulation of mimitin synthesis utilizes the MAP kinase pathway. CONCLUSION: Mimitin is a mitochondrial protein upregulated by proinflammatory cytokines at the transcriptional and protein levels, with MAP kinases involved in IL-1-dependent induction. Mimitin interacts with a microtubular protein (MAP1S), and some changes of mimitin gene expression modulate activity of apoptotic caspases 3/7, suggesting that this protein may indirectly participate in apoptosis.
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34 schema:keywords HepG2 cells
35 IL-1
36 IL-1-dependent induction
37 IL-6
38 MAP kinase
39 MAP kinase pathway
40 MAP1
41 NADH dehydrogenase I
42 TNF
43 activity
44 aggregation
45 analysis
46 apoptosis
47 apoptotic caspases 3/7
48 assembly
49 caspase 3/7 activity
50 caspase-3/7
51 caspases
52 cells
53 chain
54 changes
55 chaperones
56 coimmunoprecipitation
57 complex I
58 components
59 control
60 control of apoptosis
61 cycloheximide
62 cytochrome oxidase I.
63 cytokine-induced signals
64 cytokine-regulated mitochondrial protein
65 cytokine-responsive genes
66 cytokines
67 decrease
68 dehydrogenase I
69 destruction
70 differential display analysis
71 direct influence
72 display analysis
73 earlier studies
74 effect
75 effect of modulation
76 exposure
77 expression
78 expression modulate activity
79 expression of mimitin
80 family
81 gene expression modulate activity
82 genes
83 genome destruction
84 i.
85 induction
86 influence
87 kinase
88 kinase pathway
89 levels
90 maximum level
91 members
92 microtubular protein
93 microtubules
94 mimitin
95 mimitin expression
96 mimitin gene expression modulate activity
97 mimitin synthesis
98 mimitin-binding partners
99 mitochondria
100 mitochondrial aggregation
101 mitochondrial complex I
102 mitochondrial proteins
103 modulates activity
104 modulation
105 novel cytokine-regulated mitochondrial protein
106 novel cytokine-responsive gene
107 nuclear genome destruction
108 observations
109 oxidase I.
110 partners
111 pathway
112 possible chaperone
113 process
114 products
115 proinflammatory cytokines
116 proliferation
117 protein
118 protein family
119 protein levels
120 respiratory chain
121 siRNA
122 signals
123 slight decrease
124 small mitochondrial protein
125 stimulation
126 study
127 synthesis
128 system
129 two-hybrid system
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