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561 results on '"Gahmberg, Carl G."'

14. RIFINs are adhesins implicated in severe Plasmodium falciparum malaria

Author

Goel, Suchi, Palmkvist, Mia, Moll, Kirsten, Joannin, Nicolas, Lara, Patricia, Akhouri, Reetesh R., Moradi, Nasim, Ojemalm, Karin, Westman, Mattias, Angeletti, Davide, Kjellin, Hanna, Lehtio, Janne, Blixt, Ola, Idestrom, Lars, Gahmberg, Carl G., Storry, Jill R., Hult, Annika K., Olsson, Martin L., von Heijne, Gunnar, Nilsson, IngMarie, and Wahlgren, Mats

Subjects
Physiological aspects, Development and progression, Risk factors, Health aspects, Red blood cells -- Physiological aspects, Plasmodium falciparum -- Health aspects, Malaria -- Development and progression -- Risk factors, Erythrocytes -- Physiological aspects
Abstract

Sequestration and rosetting in individuals with severe Plasmodium falciparum malaria has been attributed to P. falciparum erythrocyte membrane protein 1 (PfEMP1) (1-8). However, antibodies to PfEMP1 disrupt rosettes of parasites [...], Rosetting is a virulent Plasmodium falciparum phenomenon associated with severe malaria. Here we demonstrate that P falciparum-encoded repetitive interspersed families of polypeptides (RIFINs) are expressed on the surface of infected red blood cells (iRBCs), bind to RBCs--preferentially of blood group A--to form large rosettes and mediate microvascular binding of iRBCs. We suggest that RIFINs have a fundamental role in the development of severe malaria and thereby contribute to the varying global distribution of ABO blood groups in the human population.

Published
2015
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15. Del-1, an Endogenous Leukocyte-Endothelial Adhesion Inhibitor, Limits Inflammatory Cell Recruitment

Author

Choi, Eun Young, Chavakis, Emmanouil, Czabanka, Marcus A., Langer, Harald F., Fraemohs, Line, Economopoulou, Matina, Kundu, Ramendra K., Orlandi, Alessia, Zheng, Ying Yi, Prieto, DaRue A., Ballantyne, Christie M., Constant, Stephanie L., Aird, William C., Papayannopoulou, Thalia, Gahmberg, Carl G., Udey, Mark C., Vajkoczy, Peter, Quertermous, Thomas, Dimmeler, Stefanie, Weber, Christian, and Chavakis, Triantafyllos

Published
2008
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40. Specific integrin [alpha] and [beta] chain phosphorylations regulate LFA-1 activation through affinity-dependent and -independent mechanisms

Author

Fagerholm, Susanna C., Hilden, Tiina J., Nurmi, Susanna M., and Gahmberg, Carl G.

Subjects
Affinity labeling -- Analysis, Phosphorylation -- Analysis, Biological sciences
Abstract

Integrins are adhesion receptors that are crucial to the functions of multicellular organisms. Integrin-mediated adhesion is a complex process that involves both affinity regulation and cytoskeletal coupling, but the molecular mechanisms behind this process have remained incompletely understood. In this study, we report that the phosphorylation of each cytoplasmic domain of the leukocyte function-associated antigen-1 integrin mediates different modes of integrin activation. [alpha] Chain phosphorylation on Ser1140 is needed for conformational changes in the integrin after chemokine- or integrin ligand-induced activation or after activation induced by active Rap1 (Rap1V12). In contrast, the [beta] chain Thr758 phosphorylation mediates selective binding to 14-3-3 proteins in response to inside-out activation through the T cell receptor, resulting in cytoskeletal rearrangements. Thus, site-specific phosphorylation of the integrin cytoplasmic domains is important for the dynamic regulation of these complex receptors in cells.

Published
2005

42. P marks the spot: site-specific integrin phosphorylation regulates molecular interactions

Author

Fagerholm, Susanna C., Hilden, Tiina J., and Gahmberg, Carl G.

Subjects
Biochemistry -- Research, Metabolism, Molecular microbiology, Phosphorylation, Biological sciences, Chemistry
Abstract

Integrins are heterodimeric adhesion receptors at the cell membrane that function as two-way signaling devices. The short intracellular tails of integrins are devoid of catalytic activity, but are nevertheless important for adhesion and signaling, presumably, through interactions with cytoplasmic molecules. Recently, the structure of the intracellular tails has been investigated using NMR, giving important new insight into how integrins might be regulated, but many questions remain unanswered. Signaling by many cell-surface receptors involves protein phosphorylation; over the past few years, phosphorylation of the integrin tails at specific sites has started to emerge as a dynamic mechanism that regulates molecular interactions between integrins and cytoplasmic molecules. This phosphorylation might give rise to signaling specificity and fine-tuning of the integrin-mediated responses.

Published
2004

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