An Inherited Abnormality of Neutrophil Adhesion

Crowley, Carol A.; Curnutte, John T.; Rosin, Richard E.; André-Schwartz, J; Gallin, John I.; Klempner, Mark S.; Snyderman, Ralph; Southwick, Fredrick S.; Stossel, Thomas P.; Babior, Bernard M.

doi:10.1056/nejm198005223022102

Cited by 268 publications

(47 citation statements)

References 29 publications

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“…PMN adherence is not only important in PMN margination to vascular endothelium but also provides anchoring of the cell for forward movement. Several children with a PMN membrane glycoprotein deficiency that prevents normal adherence have been described (34,35). These children have markedly decreased PMN chemokinesis and chemotaxis and recurrent bacterial and fungal infections.…”

Section: Discussionmentioning

confidence: 99%

Polymorphonuclear Leukocyte Adherence and Chemotaxis in Stressed and Healthy Neonates

et al. 1986

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ABSTRACT. Defects in polymorphonuclear neutrophil (PMN) adherence and chemotaxis in neonates are thought to be an important cause of their increased susceptibility to overwhelming bacterial infection. Few studies of these functions have been carried out in stressed neonates who are at even greater risk of infection. PMN adherence and chemotaxis were examined in 33 stressed neonates with acute lower respiratory illness, 13 healthy neonates, and 43 healthy adults using whole blood PMN adherence and chemotaxis assays. PMN chemotaxis was significantly decreased in stressed neonates (locomotion index of 38.4 + 9.7 pm) compared with that of healthy neonates (48.9 + 12.8 pm, p < 0.01) or adults (61.6 9 11.9 pm,p < 0.001).PMN chemotaxis was studied during illness and recovery in 13 of the 33 stressed neonates and showed significant improvement during recovery (41.6 2 9.9 and 53.2 + 11.9 pm, respectively, p = 0.012). PMN adherence was de- Bacterial infections are a major cause of morbidity and mortality in newborn infants primarily because of immaturity of their host defense mechanisms (1, 2). Neutrophils (PMNs) are the major cellular elements which defend against bacterial invasion. They respond to infection by adhering to vascular endothehum, moving toward the site of infection along a chemotactic gradient (chemotaxis) and killing ingested bacteria. The functional capacity of neonatal PMNs have been carefully studied and although results are not entirely consistent, PMN adherence (3-5) and chemotaxis (6-8) appear to be depressed in healthy neonates compared with that of adults while phagocytosis and microbial killing (9-12) are intact. In studies of neonates with underlying illness or stress, PMN phagocytosis has been found to be normal ( I 1-1 5) while microbial killing has been found to Received Junc 17. 1985: accepted November 26, 1985 be decreased ( 11-1 3, 15, 16). There have been few studies of PMN adherence and chemotaxis in stressed neonates (17). Since further impairment in these functions could help explain the increased susceptibility of stressed neonates to overwhelming bacterial infection, we prospectively studied PMN adherence and chemotaxis in healthy newborn infants and those with respiratory distress syndrome, pneumonia, and other cardiorespiratory illnesses. MATERIALS AND METHODSSubjects. Blood was obtained from 33 stressed neonates with a median chronological age of 3 days (range 1-88 days) and median gestational age of 36 wk (range 25-43 wk), 13 healthy neonates with a median chronological age of 6 days (range 3-88 days) and median gestational age of 36 wk (range 27-42 wk) and 43 healthy adults.

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Section: Discussionmentioning

confidence: 99%

Polymorphonuclear Leukocyte Adherence and Chemotaxis in Stressed and Healthy Neonates

et al. 1986

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“…Translocation of p47 PHOX from Cytosol to Plasma Membrane-Transfected lymphoblasts were treated for 15 min at 4°C with diisopropylfluorophosphate as described elsewhere (18). The cells were then washed, resuspended in phosphate-buffered saline (10 8 cells/ml), and incubated at 37°C for 10 min.…”

Section: Methodsmentioning

confidence: 99%

Activation of p47 , a Cytosolic Subunit of the Leukocyte NADPH Oxidase

Johnson

Park²,

Benna³

et al. 1998

Journal of Biological Chemistry

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131

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“…In addition it has been shown that both molecules act as adhesion molecules on granulocytes [7,23,24]. However, Mo-1 and LFA-1 have different a chains and are distributed on different cell types.…”

Section: Biological Properties Of Mo-1 and Lfa-1mentioning

confidence: 99%

Biochemical and functional characteristics of the human leukocyte membrane antigen family LFA‐1, Mo‐1 and p!50,95

et al. 1985

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Biochemical and functional characteristics of the human leukocyte membrane antigen family LFA-1, Mo-1 and pl50,95*The human leukocyte function-associated (LFA-1) antigen, the monocyte differentia tion antigen Mo-1 which is characterized as the C3bi receptor and the glycoprotein p i50,95 are characterized biochemically. Immunoprecipitations carried out with 6 different monoclonal antibodies (mAb) against LFA-1 indicated that four mAb (SPV-L l, SPV-L5, SPV-L7 and SPV-L11) were directed against the a chain, whereas mAb CLB54 and MHM-23 were found to react with the common |3 chain of LFA-1, Mo-1 and p 150,95. LFA-1 and Mo-1 expressed on KG-1 cells or lymphocytes, monocytes and granulocytes from one donor were homogeneous. Interestingly the a chain of pl50,95 showed heterogeneity. The molecular weight of the a chain expressed on monocytes was consistently higher than that of the a chain on granulocytes. The |3 subunits of LFA-1 and Mo-1 (as detected by mAb Bear-1) are not only similar in molecular weight and isoelectric focusing patterns, but it is demonstrated here that they are also identically glycosylated and have similar protein backbones as judged by tryptic peptide mapping. In spite of their structural similarities, LFA-1 and Mo-1 differ completely in some of their biological functions, Anti-LFA-1 mAb strongly inhibited monocyte-dependent T cell proliferation induced by tetanus toxoid or Helix pomatia hemocyanin and pokeweed mitogen-driven specific antibody production in vitro, whereas the anti-Mo-1 antibody Bear-1 was ineffective. These results suggest that the differences in these biological functions of LFA-1 and Mo-1 may be related to their different a subunits, which may recognize specific counter structures, IntroductionThe human leukocyte function associated (LFA-1) antigen, the monocyte differentiation antigen Mo-1 which is character ized as the C3bi receptor and the glycoprotein termed pl50,95 belong to a family of related human leukocyte membrane anti gens. LFA-1 is expressed on lymphocytes, monocytes and granulocytes [1], whereas Mo-1 and pl50,95 are present on monocytes, granulocytes and "null" cells [2], Recently, it has been shown that these molecules contribute to the adhesion reaction of these cells. Blocking experiments with anti-LFA monoclonal antibodies (mAb) demonstrated that LFA-1 inhibits the adhesion step between effector and target cells in cytotoxic T lymphocyte, natural killer and lectin-dependent cellular cytotoxicity [1,3,4], LFA-1 also participates in monocyte-dependent lectin-induced T cell proliferation suggesting that it also acts as an adhesion molecule between monocytes and T cells. Mo-1, which is the receptor for the inactivated form of C3b, mediates the adhesion of soluble complexes or particles selec tively opsonized with C3bi [5,6]. The third member of this family, p i50,95, is less well investigated but studies in patients with an inherited LFA-1, Mo-1 and pl50,95 deficiency syn drome indicated that this molecule, probably similarly to LFA-1 and Mo-1, is associated with t...

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An Inherited Abnormality of Neutrophil Adhesion

Cited by 268 publications

References 29 publications

Polymorphonuclear Leukocyte Adherence and Chemotaxis in Stressed and Healthy Neonates

Polymorphonuclear Leukocyte Adherence and Chemotaxis in Stressed and Healthy Neonates

Activation of p47 , a Cytosolic Subunit of the Leukocyte NADPH Oxidase

Biochemical and functional characteristics of the human leukocyte membrane antigen family LFA‐1, Mo‐1 and p!50,95

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