PMID- 12444150
OWN - NLM
STAT- MEDLINE
DCOM- 20021224
LR  - 20201219
IS  - 0022-1767 (Print)
IS  - 0022-1767 (Linking)
VI  - 169
IP  - 11
DP  - 2002 Dec 1
TI  - Function of the lectin domain of Mac-1/complement receptor type 3 (CD11b/CD18) in 
      regulating neutrophil adhesion.
PG  - 6417-26
AB  - A lectin function within CD11b mediates both cytotoxic priming of 
      Mac-1/complement receptor type 3 (CR3) by beta-glucan and the formation of 
      transmembrane signaling complexes with GPI-anchored glycoproteins such as CD16b 
      (FcgammaRIIIb). A requirement for GPI-anchored urokinase plasminogen activator 
      receptor (uPAR; CD87) in neutrophil adhesion and diapedesis has been demonstrated 
      with uPAR-knockout mice. In this study, neutrophil activation conditions 
      generating high-affinity (H-AFN) or low-affinity (L-AFN) beta(2) integrin 
      adhesion were explored. A role for the Mac-1/CR3 lectin domain and uPAR in 
      mediating H-AFN or L-AFN adhesion was suggested by the inhibition of 
      Mac-1/CR3-dependent adhesion to ICAM-1 or fibrinogen by beta-glucan or anti-uPAR. 
      The formation of uPAR complexes with Mac-1/CR3 activated for L-AFN adhesion was 
      demonstrated by fluorescence resonance energy transfer. Conversely, Jurkat cell 
      LFA-1 H-AFN-adhesion to ICAM-1 was not associated with uPAR/LFA-1 complexes, any 
      requirement for GPI-anchored glycoproteins, or inhibition by beta-glucan. A 
      single CD11b lectin site for beta-glucan and uPAR was suggested because the 
      binding of either beta-glucan or uPAR to Mac-1/CR3 selectively masked two CD11b 
      epitopes adjacent to the transmembrane domain. Moreover, treatment with 
      phosphatidylinositol-specific phospholipase C that removed GPI-anchored proteins 
      increased CD11b-specific binding of (125)I-labeled beta-glucan by 3-fold and this 
      was reversed with soluble recombinant uPAR. Conversely, neutrophil activation for 
      generation of Mac-1/CR3/uPAR complexes inhibited CD11b-dependent binding of 
      (125)I-labeled beta-glucan by 75%. These data indicate that the same lectin 
      domain within CD11b regulates both the cytotoxic and adhesion functions of 
      Mac-1/CR3.
FAU - Xia, Yu
AU  - Xia Y
AD  - Chemoattractant Group of the James Graham Brown Cancer Center, Department of 
      Pathology, University of Louisville, KY 40202, USA.
FAU - Borland, Gita
AU  - Borland G
FAU - Huang, Jibiao
AU  - Huang J
FAU - Mizukami, Ikuko F
AU  - Mizukami IF
FAU - Petty, Howard R
AU  - Petty HR
FAU - Todd, Robert F 3rd
AU  - Todd RF 3rd
FAU - Ross, Gordon D
AU  - Ross GD
LA  - eng
GR  - AI27409/AI/NIAID NIH HHS/United States
GR  - CA42246/CA/NCI NIH HHS/United States
GR  - CA86412/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (CD11b Antigen)
RN  - 0 (CD18 Antigens)
RN  - 0 (Epitopes)
RN  - 0 (Glycosylphosphatidylinositols)
RN  - 0 (Lectins)
RN  - 0 (Lymphocyte Function-Associated Antigen-1)
RN  - 0 (Macrophage-1 Antigen)
RN  - 0 (PLAUR protein, human)
RN  - 0 (Plaur protein, mouse)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (Receptors, Urokinase Plasminogen Activator)
SB  - IM
MH  - Animals
MH  - Binding Sites
MH  - CD11b Antigen/*chemistry/metabolism
MH  - CD18 Antigens/*chemistry/metabolism
MH  - Cell Adhesion/immunology
MH  - Epitopes/chemistry
MH  - Glycosylphosphatidylinositols/metabolism
MH  - Humans
MH  - In Vitro Techniques
MH  - Jurkat Cells
MH  - Lectins/chemistry/metabolism
MH  - Lymphocyte Function-Associated Antigen-1/metabolism
MH  - Macrophage-1 Antigen/*chemistry/metabolism
MH  - Mice
MH  - Neutrophils/*cytology/*immunology
MH  - Protein Structure, Tertiary
MH  - Receptors, Cell Surface/metabolism
MH  - Receptors, Urokinase Plasminogen Activator
MH  - T-Lymphocytes/cytology/immunology
EDAT- 2002/11/22 04:00
MHDA- 2002/12/27 04:00
CRDT- 2002/11/22 04:00
PHST- 2002/11/22 04:00 [pubmed]
PHST- 2002/12/27 04:00 [medline]
PHST- 2002/11/22 04:00 [entrez]
AID - 10.4049/jimmunol.169.11.6417 [doi]
PST - ppublish
SO  - J Immunol. 2002 Dec 1;169(11):6417-26. doi: 10.4049/jimmunol.169.11.6417.