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alpha1-Antitrypsin inhibits Moraxella catarrhalis MID protein-induced tonsillar B cell proliferation and IL-6 release.

Hadzic, Radinka LU ; Nita, Izabela LU ; Tassidis, Helena LU ; Riesbeck, Kristian LU ; Gjörloff Wingren, Anette LU and Janciauskiene, Sabina LU (2006) In Immunology Letters 102(2). p.141-147
Abstract
alpha 1-Antitrypsin (AAT) is a major circulating and tissues inhibitor of serine proteinases implicated in the regulation of inflammation and host defence. There is now increasing evidence that AAT may also exhibit anti-inflammatory activities independent of its protease inhibitor function. This study was undertaken to investigate the effects of native (inhibitory) and polymerized (non-inhibitory) forms of AAT on MID (Moraxella IgD binding protein)-induced human tonsillar B cell activation in vitro. We found that 0.5 mu g/ml MID induces B cell proliferation and stimulates IL-6 release (p < 0.001) relative to non-stimulated controls. Both native and polymerized AAT (0.5 mg/ml) inhibited MID-stimulated B cell proliferation in a similar... (More)
alpha 1-Antitrypsin (AAT) is a major circulating and tissues inhibitor of serine proteinases implicated in the regulation of inflammation and host defence. There is now increasing evidence that AAT may also exhibit anti-inflammatory activities independent of its protease inhibitor function. This study was undertaken to investigate the effects of native (inhibitory) and polymerized (non-inhibitory) forms of AAT on MID (Moraxella IgD binding protein)-induced human tonsillar B cell activation in vitro. We found that 0.5 mu g/ml MID induces B cell proliferation and stimulates IL-6 release (p < 0.001) relative to non-stimulated controls. Both native and polymerized AAT (0.5 mg/ml) inhibited MID-stimulated B cell proliferation in a similar manner (by 70%, p < 0.001), whereas MID-induced IL-6 release was more strongly suppressed by polymefized (9.9-fold, p < 0.001) as compared to native AAT (2.8-fold, p < 0.01). Electrophoretic analysis of cell culture media did not indicate any interaction between AAT and MID, and flow cytometry data showed no competition for the same receptor. The effects of AATs were observed whether added together with MID or 2 h after MID-addition to cell cultures. Thus, our data demonstrate that AAT inhibits MID-induced B cell activation in vitro that is unrelated to its protease inhibitory activity and is not dependent on MID binding to the cell surface. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
MID, inflammation, B cells, alpha 1-antitrypsin, tonsils
in
Immunology Letters
volume
102
issue
2
pages
141 - 147
publisher
Elsevier
external identifiers
  • wos:000235324300003
  • pmid:16214222
  • scopus:30144440693
ISSN
0165-2478
DOI
10.1016/j.imlet.2005.08.006
language
English
LU publication?
yes
id
c6990b98-a290-4ea3-98a2-012379ff1085 (old id 144750)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=16214222&dopt=Abstract
date added to LUP
2007-07-23 13:08:34
date last changed
2018-07-01 03:25:35
@article{c6990b98-a290-4ea3-98a2-012379ff1085,
  abstract     = {alpha 1-Antitrypsin (AAT) is a major circulating and tissues inhibitor of serine proteinases implicated in the regulation of inflammation and host defence. There is now increasing evidence that AAT may also exhibit anti-inflammatory activities independent of its protease inhibitor function. This study was undertaken to investigate the effects of native (inhibitory) and polymerized (non-inhibitory) forms of AAT on MID (Moraxella IgD binding protein)-induced human tonsillar B cell activation in vitro. We found that 0.5 mu g/ml MID induces B cell proliferation and stimulates IL-6 release (p &lt; 0.001) relative to non-stimulated controls. Both native and polymerized AAT (0.5 mg/ml) inhibited MID-stimulated B cell proliferation in a similar manner (by 70%, p &lt; 0.001), whereas MID-induced IL-6 release was more strongly suppressed by polymefized (9.9-fold, p &lt; 0.001) as compared to native AAT (2.8-fold, p &lt; 0.01). Electrophoretic analysis of cell culture media did not indicate any interaction between AAT and MID, and flow cytometry data showed no competition for the same receptor. The effects of AATs were observed whether added together with MID or 2 h after MID-addition to cell cultures. Thus, our data demonstrate that AAT inhibits MID-induced B cell activation in vitro that is unrelated to its protease inhibitory activity and is not dependent on MID binding to the cell surface.},
  author       = {Hadzic, Radinka and Nita, Izabela and Tassidis, Helena and Riesbeck, Kristian and Gjörloff Wingren, Anette and Janciauskiene, Sabina},
  issn         = {0165-2478},
  keyword      = {MID,inflammation,B cells,alpha 1-antitrypsin,tonsils},
  language     = {eng},
  number       = {2},
  pages        = {141--147},
  publisher    = {Elsevier},
  series       = {Immunology Letters},
  title        = {alpha1-Antitrypsin inhibits Moraxella catarrhalis MID protein-induced tonsillar B cell proliferation and IL-6 release.},
  url          = {http://dx.doi.org/10.1016/j.imlet.2005.08.006},
  volume       = {102},
  year         = {2006},
}