Log in

Relevant bibliographies by topics / L-selectin

Contents

Journal articles

Academic literature on the topic 'L-selectin'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'L-selectin.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "L-selectin"

1

Peng, Shuang, Shen-Bao Chen, Lin-Da Li, et al. "Impact of real-time shedding on binding kinetics of membrane-remaining L-selectin to PSGL-1." American Journal of Physiology-Cell Physiology 316, no. 5 (2019): C678—C689. http://dx.doi.org/10.1152/ajpcell.00212.2018.

Full text

Abstract:

L-selectin shedding induced by various cytokines is crucial in activating neutrophils (PMNs) in inflammatory cascade. While the real-time shedding in vivo lasts ~10 min after PMN activation, the impact of time-dependent shedding on binding kinetics of membrane-remaining L-selectins to its ligands is poorly understood at transient or steady state. Here, we developed an in vitro L-selectin shedding dynamics approach, together with competitive assays of cell adhesion, and proposed a theoretical model for quantifying the impact of real-time shedding on the binding kinetics of membrane-remaining L-

APA, Harvard, Vancouver, ISO, and other styles

2

Mattila, Polly E., Chad E. Green, Ulrich Schaff, Scott I. Simon, and Bruce Walcheck. "Cytoskeletal interactions regulate inducible L-selectin clustering." American Journal of Physiology-Cell Physiology 289, no. 2 (2005): C323—C332. http://dx.doi.org/10.1152/ajpcell.00603.2004.

Full text

Abstract:

L-selectin (CD62L) amplifies neutrophil capture within the microvasculature at sites of inflammation. Activation by G protein-coupled stimuli or through ligation of L-selectin promotes clustering of L-selectin and serves to increase its adhesiveness, signaling, and colocalization with β2-integrins. Currently, little is known about the molecular process regulating the lateral mobility of L-selectin. On neutrophil stimulation, a progressive change takes place in the organization of its plasma membrane, resulting in membrane domains that are characteristically enriched in glycosyl phosphatidylino

APA, Harvard, Vancouver, ISO, and other styles

3

Miles, Mary P., Sharyn K. Leach, William J. Kraemer, Keiichiro Dohi, Jill A. Bush, and Andrea M. Mastro. "Leukocyte adhesion molecule expression during intense resistance exercise." Journal of Applied Physiology 84, no. 5 (1998): 1604–9. http://dx.doi.org/10.1152/jappl.1998.84.5.1604.

Full text

Abstract:

We hypothesized that expression of L-selectin and very late antigen-4 (VLA-4) integrin adhesion molecules would influence cell type-specific redistribution during exercise. Women subjects performed six sets of 10-repetition maximum squats. L-selectin and VLA-4 integrin were measured by using flow cytometry pre- and postexercise on peripheral blood neutrophils and lymphocytes ( n = 29 subjects) and lymphocyte subsets ( n = 70 subjects), respectively. Neutrophil concentration increased 41.8% ( P < 0.001), whereas the percent expressing L-selectin was unchanged (79%). Lymphocyte concentration

APA, Harvard, Vancouver, ISO, and other styles

4

Alon, R., R. C. Fuhlbrigge, E. B. Finger, and T. A. Springer. "Interactions through L-selectin between leukocytes and adherent leukocytes nucleate rolling adhesions on selectins and VCAM-1 in shear flow." Journal of Cell Biology 135, no. 3 (1996): 849–65. http://dx.doi.org/10.1083/jcb.135.3.849.

Full text

Abstract:

We demonstrate an additional step and a positive feedback loop in leukocyte accumulation on inflamed endothelium. Leukocytes in shear flow bind to adherent leukocytes through L-selectin/ligand interactions and subsequently bind downstream and roll on inflamed endothelium, purified E-selectin, P-selectin, L-selectin, VCAM-1, or peripheral node addressin. Thus adherent leukocytes nucleate formation of strings of rolling cells and synergistically enhance leukocyte accumulation. Neutrophils, monocytes, and activated T cell lines, but not peripheral blood T lymphocytes, tether to each other through

APA, Harvard, Vancouver, ISO, and other styles

5

Nelson, RM, O. Cecconi, WG Roberts, A. Aruffo, RJ Linhardt, and MP Bevilacqua. "Heparin oligosaccharides bind L- and P-selectin and inhibit acute inflammation." Blood 82, no. 11 (1993): 3253–58. http://dx.doi.org/10.1182/blood.v82.11.3253.3253.

Full text

Abstract:

Abstract Initial attachment of leukocytes to the vessel wall at sites of inflammation is supported by a family of carbohydrate-binding adhesion molecules called the selectins. Selectin ligands include sialyl-Lewis x (sLex, Neu5Ac alpha 2–3Gal beta 1–4[Fuc alpha 1–3]GlcNAc--) and related structures. We report here that defined heparin oligosaccharides interact with the selectins. Heparin chains containing four or more monosaccharide residues inhibited the function of L- and P-selectin, but not E-selectin, in vitro. In a competition enzyme-linked immunosorbent assay measuring inhibition of solut

APA, Harvard, Vancouver, ISO, and other styles

6

Nelson, RM, O. Cecconi, WG Roberts, A. Aruffo, RJ Linhardt, and MP Bevilacqua. "Heparin oligosaccharides bind L- and P-selectin and inhibit acute inflammation." Blood 82, no. 11 (1993): 3253–58. http://dx.doi.org/10.1182/blood.v82.11.3253.bloodjournal82113253.

Full text

Abstract:

Initial attachment of leukocytes to the vessel wall at sites of inflammation is supported by a family of carbohydrate-binding adhesion molecules called the selectins. Selectin ligands include sialyl-Lewis x (sLex, Neu5Ac alpha 2–3Gal beta 1–4[Fuc alpha 1–3]GlcNAc--) and related structures. We report here that defined heparin oligosaccharides interact with the selectins. Heparin chains containing four or more monosaccharide residues inhibited the function of L- and P-selectin, but not E-selectin, in vitro. In a competition enzyme-linked immunosorbent assay measuring inhibition of solution-phase

APA, Harvard, Vancouver, ISO, and other styles

7

Matala, Erik, Shelia R. Alexander, Takashi K. Kishimoto, and Bruce Walcheck. "The Cytoplasmic Domain of L-Selectin Participates in Regulating L-Selectin Endoproteolysis." Journal of Immunology 167, no. 3 (2001): 1617–23. http://dx.doi.org/10.4049/jimmunol.167.3.1617.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Jutila, M. A., G. Watts, B. Walcheck, and G. S. Kansas. "Characterization of a functionally important and evolutionarily well-conserved epitope mapped to the short consensus repeats of E-selectin and L-selectin." Journal of Experimental Medicine 175, no. 6 (1992): 1565–73. http://dx.doi.org/10.1084/jem.175.6.1565.

Full text

Abstract:

Selectins represent a new family of adhesion molecules, expressed by leukocytes and endothelial cells, that are involved in the regulation of leukocyte traffic. Here we have characterized a new monoclonal antibody (mAb) (EL-246) that recognizes both human leukocyte L-selectin (previously called LAM-1, LECAM-1, or gp90MEL-14) and endothelial cell E-selectin (previously called ELAM-1). EL-246 recognized a 110-kD protein expressed on cells transfected with E-selectin cDNA and stained many postcapillary venules in inflamed human tonsil. EL-246 also stained human peripheral blood leukocytes and sho

APA, Harvard, Vancouver, ISO, and other styles

9

Alon, Ronen, Shuqi Chen, Kamal D. Puri, Erik B. Finger, and Timothy A. Springer. "The Kinetics of L-selectin Tethers and the Mechanics of Selectin-mediated Rolling." Journal of Cell Biology 138, no. 5 (1997): 1169–80. http://dx.doi.org/10.1083/jcb.138.5.1169.

Full text

Abstract:

Two mechanisms have been proposed for regulating rolling velocities on selectins. These are (a) the intrinsic kinetics of bond dissociation, and (b) the reactive compliance, i.e., the susceptibility of the bond dissociation reaction to applied force. To determine which of these mechanisms explains the 7.5–11.5-fold faster rolling of leukocytes on L-selectin than on E- and P-selectins, we have compared the three selectins by examining the dissociation of transient tethers. We find that the intrinsic kinetics for tether bond dissociation are 7–10-fold more rapid for L-selectin than for E- and P-

APA, Harvard, Vancouver, ISO, and other styles

10

Dwir, Oren, Geoffrey S. Kansas, and Ronen Alon. "Cytoplasmic anchorage of L-selectin controls leukocyte capture and rolling by increasing the mechanical stability of the selectin tether." Journal of Cell Biology 155, no. 1 (2001): 145–56. http://dx.doi.org/10.1083/jcb.200103042.

Full text

Abstract:

L-selectin is a leukocyte lectin that mediates leukocyte capture and rolling in the vasculature. The cytoplasmic domain of L-selectin has been shown to regulate leukocyte rolling. In this study, the regulatory mechanisms by which this domain controls L-selectin adhesiveness were investigated. We report that an L-selectin mutant generated by truncation of the COOH-terminal 11 residues of L-selectin tail, which impairs association with the cytoskeletal protein α-actinin, could capture leukocytes to glycoprotein L-selectin ligands under physiological shear flow. However, the conversion of initial

APA, Harvard, Vancouver, ISO, and other styles

More sources

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!