CD66a, CD66b, CD66c, and CD66d each Independently stimulate neutrophils

Abstract

Four members of the carcinoembryonic antigen family, CD66a, CD66b, CD66c, and CD66d, are expressed on human neutrophils. In neutrophils these proteins are activation antigens in that their surface expression is increased following stimulation. To examine their potential role in neutrophil signaling, the effects on neutrophil adhesion to human umbilical vein endothelial cells of a panel of well-characterized CD66 mAbs was tested. CD66a, CD66b, CD66c, and CD66d antibodies each increased neutrophil adhesion to human umbilical vein endothelial cell monolayers. This increase in neutrophil adhesion caused by CD66 antibodies was blocked by a CD18 antibody and associated with up-regulation of CD11/CD18 on the neutrophil surface. This increase in neutrophil adhesion required physiological extracellular calcium concentrations at or near the time of CD66 antibody binding to the neutrophil. The incubation of CD66 antibodies with neutrophils in the absence of calcium for 10 min before repletion of calcium resulted in no increase in neutrophil adhesion. The data suggest that CD66a, CD66b, CD66c, and CD66d antibody binding to the neutrophil surface triggers a transient activation signal that requires extracellular calcium and regulates the adhesive activity of CD11/CD18. Sequential desensitization experiments indicated that CD66a, CD66b, CD66c, and CD66d can each independently transmit signals in neutrophils.

Inhibition of Plasmin Activity by Tranexamic Acid Does Not Influence Inflammatory Pathways During Human Endotoxemia

“…34 CD66b is a glycoprotein believed to be involved in neutrophil activation and migration, by means of regulating the adhesive activity of CD11b/CD18. 35 L-selectin that is constitutively present on the neutrophil membrane is necessary for initial neutrophil-endothelial cell interaction that results in rolling of neutrophils on endothelium. 36 Activation of neutrophils by LPS causes shedding of L-selectin.…”

Establishment and phenotypic characterization of human U937 cells with inducible P210 BCR/ABL expression reveals upregulation of CEACAM1 (CD66a)

“…[45][46][47]50 It has been suggested that the tyrosine kinase activity associated with CEACAM1 may play a role in signal transduction and cellular adhesion, and that CEACAM1 might affect many important regulatory functions, such as proliferation, apoptosis, differentiation, angiogenesis, immune responses, granulocyte activation and polarization of epithelial cells. 45,47,[51][52][53][54][55] Moreover, CEA-CAM1, like BCR/ABL, has been shown to associate with the actin cytoskeleton, possible by interacting with paxillin. [56][57][58][59][60] In the hematopoietic system no detailed studies on the expression of CEACAM1 in different cellular compartments are available, but during normal hematopoiesis the expression pattern of the CEACAM1, CEACAM6 and CEACAM8 molecules has been shown to change with different maturation stages, first appearing at the promyelocytic stage and then showing increased expression on myelocytes and metamyelocytes.…”

Intratumoral neutrophils and plasmacytoid dendritic cells indicate poor prognosis and are associated with pSTAT3 expression in AJCC stage I/II melanoma

“…CD66b is a granulocyte activation marker. 20 The neutrophils were defined as cells with red cytoplasmatic staining and a segmented nucleus. Neutrophils were only evaluated in the intratumoral area.…”