Calcium signaling capacity of the integrin on human neutrophils

Ng-Sikorski, Janet; Andersson, R; Patarroyo, Manuel Elkín; Andersson, Tommy

doi:10.1016/0014-4827(91)90402-g

Cited by 126 publications

(60 citation statements)

References 26 publications

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“…Leukocyte integrins have been reported to signal an increase in intracellular calcium, inositol phospholipid hydrolysis (31,36,58,67,79), and tyrosine phosphorylation of a number of intracellular proteins, including Fgr (8), paxillin (23), PLC-␥ (31, 39), p130…”

Section: Discussionmentioning

confidence: 99%

“…Phosphorylation may depend on the ␣-subunit, as suggested by the observation that phosphorylation of paxillin in TNF-treated neutrophils is dependent on Mac-1 but not LFA-1 binding (26). Ligation of ␤ 2 -integrins on polymorphonuclear neutrophils (PMN) also induces an increase in the intracellular calcium concentration (31,36,58) and the formation of D-myo-inositol 1,4,5-trisphosphate [Ins(1,4,5)P 3 ], possibly by tyrosine phosphorylation of phospholipase C (PLC)-␥ and D-myoinositol-trisphosphate 3-kinase, respectively (31,48). Antibody cross-linking of ␤ 2 -integrins on adherent human neutrophils has been shown to trigger activation of p21 ras through tyrosine phosphorylation of the protooncogene product Vav (84).…”

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confidence: 99%

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Mac-1-dependent tyrosine phosphorylation during neutrophil adhesion

Takami

Herrera²,

Petruzzelli

2001

American Journal of Physiology-Cell Physiology

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Activated neutrophils display an array of physiological responses, including initiation of the oxidative burst, phagocytosis, and cell migration, that are associated with cellular adhesion. Under conditions that lead to cellular adhesion, we observed rapid tyrosine phosphorylation of an intracellular protein with an approximate relative molecular mass of 92 kDa (p92). Phosphorylation of p92 was inducible when Mac-1 was activated by phorbol 12-myristate 13-acetate, the β2-specific activating antibody CBR LFA-1/2, or interleukin-8 (77 amino acids). In addition, tyrosine phosphorylation of p92 was dependent on engagement of Mac-1 with ligand. Several observations suggest that this event may be an important step in the signaling pathway initiated by Mac-1 binding. p92 phosphorylation was specifically blocked with antibodies to CD11b, the α-subunit of Mac-1, and was rapidly reversible on disengagement of the integrin ligand interaction. Integrin-stimulated phosphorylation of p92 created binding sites that were recognized in vitro by the SH2 domains of c-CrkII and Src. Our observations suggest that neutrophil adhesion mediated through the binding of the β2-integrin Mac-1 initiates a signaling cascade that involves the activation of protein tyrosine kinases and leads to the regulation of protein-protein interactions via SH2 domains, a key process shared with growth factor signaling pathways.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Mac-1-dependent tyrosine phosphorylation during neutrophil adhesion

Takami

Herrera²,

Petruzzelli

2001

American Journal of Physiology-Cell Physiology

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“…Using neutrophils and the monocytic cell line THP-1, which express large amounts of CDllWCD18, it has been shown that CD1 I b or CD18 antibodies induce increased levels of intracellular Ca" (Ng-Sikorski et al, 1991;Altieri et al, 1992). These Ca2 + levels oscillate, and this phenomenon may be an important molecular mechanism of regulation of adhesion.…”

Section: -1 \ P H O S P H a T A S Ementioning

confidence: 99%

Leukocyte Adhesion

Gahmberg

Tolvanen

Kotovuori

1997

European Journal of Biochemistry

207

191

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Leukocyte adhesion is of pivotal functional importance and this has resulted in extensive research and rapid develonient in the field. Leukocyte adhesion involves members of three molecular families: integrins, members of the immunoglobulin superfatnily and carbohydrate binding selectins and sialoadhesins. Recently, considerable structural information on leukocyte integrins and members of the immunoglobulin superfrtinily of adhesion molecules has been obtained. This fact. combined with the identification of several novel adhesion molecules. has increased our understanding o f how they function at the molecular level. Furthermore, the important issue of how integrins are activated to become adhesive is rapidly advancing,.. It is clearly evident that the knowledge accuniulated from basic research will increasingly be applied in clinical medicine. In this review we focus on two iinportant families of adhesion molecules. Norc. This Review will be reprinted in EJR Kei?cw.\ 1997 which will be av;iil;ible in April I99X.A number of different leukocytes are known and most probably more subgroups will be found concomitantly with the development in typing procedures. 111 addition, the cells rnay represent different stages of differentiation. An individual leukocyte m 11 s t be able to interact with a number of fundamentally different cells. often modified in various ways. and sometimes with the extracellular matrix or foreign microbes. These facts may partially be the reason that many different leukocyte adhesion systems and molecules exist. In addition i t is certainly useful for the organism to have a certain redundancy i n adhcsion molecule expression and function. which could seciire vital functions cven if some adhesion functions are lost or weakened.Cellular immunology used to be largely phenomenal and not inolecular. But with the development of monoclonal antibody and inolecular cloning techniques, combined with the rapid advance in structural elucidation. present day immunology is certainly ii molecular science, and in inany respects in the forefiont of modern biomedical research. In fact, a number of dcvelopinents in other fields of present day biomedical research originate from breakthroughs in iinmunology. and an excellent exaniple is leukocyte adhesion. Although much remains poorly understood, adhesion receptor-ligand interactions are now appreciated to such an extent that much can be applied t o several other areas of research.But research on leiikocytc adhesion is not rewarding only from a basic point of view. Undoubtedly. the large interest in this field steins from iiuinerous potential clinical applications. Many of the iniljor diseases affecting mankind. like cardiovnscular disease. stroke, chronic and iicute inflammations. cancer. malaria, and inany bacterial and viral infections directly involve leukocyte adhesion molecules. Therefore. it comes as no surprise

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“…The 120-kDa FN was purchased from GIBCO-BRL (Gaithersburg, MD). Intact FN and purified FN fragments (29,40,45, and 70 kDa) were prepared in the Department of Physiology and Cell Biology at the Albany Medical College. The blocking monoclonal antibody to the LRI (7G2) was generously provided by the laboratory of Dr. Eric Brown (Washington University, St. Louis, MO).…”

Section: Reagentsmentioning

confidence: 99%