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01000caa a22002652 4500 |
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NLM115779310 |
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DE-627 |
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20250202222135.0 |
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231222s2001 xx ||||| 00| ||eng c |
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|a pubmed25n0386.xml
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|a (DE-627)NLM115779310
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|a (NLM)11683582
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Pelletier, M
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Modulation of interleukin-15-induced human neutrophil responses by the plant lectin Viscum album agglutinin-I
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| 264 |
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1 |
|c 2001
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| 336 |
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|a Text
|b txt
|2 rdacontent
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| 337 |
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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| 338 |
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|a Band
|b nc
|2 rdacarrier
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| 500 |
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|a Date Completed 07.12.2001
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| 500 |
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|a Date Revised 30.09.2009
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|a published: Print
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|a Citation Status MEDLINE
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| 520 |
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|a Copyright 2001 Academic Press.
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| 520 |
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|a The plant lectin Viscum album agglutinin-I (VAA-I) and the interleukin-15 (IL-15) cytokine are two molecules with potential therapeutic properties known to modulate neutrophil functions when used separately. This study was conducted in order to better understand the mode of action of VAA-I and to elucidate how VAA-I could modulate IL-15-induced neutrophil responses. We found that VAA-I cannot induce phosphorylation events in human neutrophils. However, it enhances phagocytosis by itself without altering IL-15-induced phagocytosis. VAA-I was found to reverse the ability of IL-15 to delay neutrophil apoptosis and this was correlated with an inhibition of IL-15-induced de novo protein synthesis. In addition, we also found that IL-15 cannot reverse or attenuate the caspase-induced gelsolin fragmentation observed during apoptosis as assessed by immunoblotting. We conclude that VAA-I can be used to modulate some, but not all, IL-15-induced neutrophil responses and that it acts independent of phosphorylation events
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| 650 |
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4 |
|a Journal Article
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| 650 |
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4 |
|a Research Support, Non-U.S. Gov't
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| 650 |
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7 |
|a Adjuvants, Immunologic
|2 NLM
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| 650 |
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7 |
|a Gelsolin
|2 NLM
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| 650 |
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7 |
|a Interleukin-15
|2 NLM
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| 650 |
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7 |
|a Interleukin-2
|2 NLM
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| 650 |
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7 |
|a Plant Preparations
|2 NLM
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| 650 |
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7 |
|a Plant Proteins
|2 NLM
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| 650 |
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7 |
|a Ribosome Inactivating Proteins, Type 2
|2 NLM
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| 650 |
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7 |
|a Toxins, Biological
|2 NLM
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| 650 |
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7 |
|a VAA-I protein, Viscum album
|2 NLM
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| 650 |
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7 |
|a ribosome inactivating protein, Viscum
|2 NLM
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| 650 |
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7 |
|a Ribosome Inactivating Proteins
|2 NLM
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| 650 |
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7 |
|a EC 3.2.2.22
|2 NLM
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| 700 |
1 |
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|a Lavastre, V
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Savoie, A
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Ratthé, C
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Saller, R
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Hostanska, K
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Girard, D
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Clinical immunology (Orlando, Fla.)
|d 1999
|g 101(2001), 2 vom: 01. Nov., Seite 229-36
|w (DE-627)NLM098196855
|x 1521-6616
|7 nnns
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| 773 |
1 |
8 |
|g volume:101
|g year:2001
|g number:2
|g day:01
|g month:11
|g pages:229-36
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| 912 |
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|a GBV_USEFLAG_A
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| 912 |
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|a SYSFLAG_A
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| 912 |
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|a GBV_NLM
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| 912 |
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|a GBV_ILN_11
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| 912 |
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|a GBV_ILN_24
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| 912 |
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|a GBV_ILN_350
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| 951 |
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|a AR
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| 952 |
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|d 101
|j 2001
|e 2
|b 01
|c 11
|h 229-36
|