Abstract:
:To compare the responses of individual neutrophils to chemoattractants, migration pathway data were obtained using TAXIScan, an optically accessible/horizontal apparatus in which a concentration gradient is established reproducibly for a given stimulus. The observed linear-mode trajectory pattern of neutrophils toward N-formyl-methionyl-leucyl-phenylalanine (fMLP) or Interleukin (IL)-8/CXCL8 was distinguished from random migration patterns toward leukotriene (LT) B4 or platelet activating factor (PAF). The median values of velocity and directionality calculated for individual cells toward fMLP and IL-8 were both relatively similar and high, whereas the values toward LTB4 and PAF were widely dispersed over a lower range of directionality and from low to high ranges of velocity. The different patterns between the groups may be explained by unique morphology with single polarity toward fMLP and IL-8, and unstable morphology with multiple polarities toward LTB4 and PAF. Unique morphologies toward fMLP and IL-8 were not affected by coexisting LTB4 or PAF. On the other hand, the addition of suboptimum concentrations of fMLP or IL-8 to LTB4 or PAF induced a nearly maximum chemotactic response in most cells. These data suggest that exogenous formyl peptides and endogenous chemokines augment neutrophil accumulation at inflammation sites, whereas lipid mediators may play a role in supporting activation of the inflammatory cells for recruitment.
journal_name
J Immunol Methodsjournal_title
Journal of immunological methodsauthors
Yamauchi A,Degawa-Yamauchi M,Kuribayashi F,Kanegasaki S,Tsuchiya Tdoi
10.1016/j.jim.2013.12.005subject
Has Abstractpub_date
2014-02-01 00:00:00pages
59-70eissn
0022-1759issn
1872-7905pii
S0022-1759(13)00369-4journal_volume
404pub_type
杂志文章abstract::A mild procedure for the purification of rabbit Fab' antibodies is described. A small column of normal goat IgG-Sepharose 4B (3 cm x 5mm) was saturated with F(ab')2 prepared from rabbit anti-goat IgG, and anti-goat IgG Fab was eluted from the column by splitting the disulfide bond in the hinge of the F(ab')2 molecule ...
journal_title:Journal of immunological methods
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journal_title:Journal of immunological methods
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journal_title:Journal of immunological methods
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journal_title:Journal of immunological methods
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journal_title:Journal of immunological methods
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journal_title:Journal of immunological methods
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journal_title:Journal of immunological methods
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更新日期:1981-01-01 00:00:00
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journal_title:Journal of immunological methods
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journal_title:Journal of immunological methods
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journal_title:Journal of immunological methods
pub_type: 杂志文章
doi:10.1016/0022-1759(87)90314-0
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journal_title:Journal of immunological methods
pub_type: 杂志文章
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journal_title:Journal of immunological methods
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journal_title:Journal of immunological methods
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