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3. Contributors to Volume 8

Author

Alexander, Frances C.G., primary, Anderson, A.J., additional, Arita, M., additional, Balvinsdottir, Johanna, additional, Benoit, Evelyne, additional, Benz, Roland, additional, Blaustein, Mordecai, additional, Blumberg, Peter M., additional, Breittmayer, Jean-Philippe, additional, Brewster, Barry S., additional, Cerveñansky, Carlos, additional, Chakraborty, Trinad, additional, Christensen, Jens Dencker, additional, Clementi, F., additional, Comella, Joan X., additional, Creveling, Cyrus R., additional, Dajas, Federico, additional, Daly, John W., additional, Dinh, Thu T., additional, Esparis-Ogando, A., additional, Fjalland, Bjarne, additional, Frelin, Christian, additional, Garcia, Maria L., additional, Garcia-Calvo, Margarita, additional, Gotti, C., additional, Granier, Claude, additional, Harris, John B., additional, Harvey, A.L., additional, Himmelreich, N.H., additional, Izumi, F., additional, Jørgensen, Annette, additional, Kaczorowski, Gregory J., additional, Kobayashi, H., additional, Law, Susan F., additional, Legrand, Anne-Marie, additional, Llewellyn-Smith, Ida J., additional, Lollike, Karsten, additional, Loret, Erwann P., additional, Minson, Jane B., additional, Miranda, Françis, additional, Molgo, Jordi, additional, Moretti, M., additional, Nakamura, Hideshi, additional, Nordmann, Jean J., additional, Ohizumi, Yasushi, additional, Pilowsky, Paul M., additional, Poulain, Bernard, additional, Reisine, Terry, additional, Ritter, Sue, additional, Rochat, Hervé, additional, Rowan, E.G., additional, Sampieri, François, additional, Sato, Kazuki, additional, Sauviat, Martin-Pierre, additional, Shone, Clifford C., additional, Silveira, Rodolfo, additional, Simpson, Lance L., additional, Sokolov, Yu.V., additional, Sorensen, Roger G., additional, Strong, Peter N., additional, Szallasi, Arpad, additional, Takeda, Ken, additional, Takemura, Motohiko, additional, Terletskaya, Ya. T., additional, Tranter, Howard S., additional, Treiman, Marek, additional, Tsuji, K., additional, Uezono, Y., additional, Vazquez, Jesus, additional, Wada, A., additional, Wessler, I., additional, Yanagihara, N., additional, and Zufall, Frank, additional

Published
1992
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6. Lollike, Karsten

Author

Lollike, Karsten and Lollike, Karsten

Published
2008

7. The PEF family proteins sorcin and grancalcin interact in vivo and in vitro.

Author

Hansen, Christian, Tarabykina, Svetlana, la Cour, Jonas Marstrand, Lollike, Karsten, Berchtold, Martin W, Hansen, Christian, Tarabykina, Svetlana, la Cour, Jonas Marstrand, Lollike, Karsten, and Berchtold, Martin W

Abstract

Udgivelsesdato: 2003-Jun-19, The penta-EF hand (PEF) family of calcium binding proteins includes grancalcin, peflin, sorcin, calpain large and small subunits as well as ALG-2. Systematic testing of the heterodimerization abilities of the PEF proteins using the yeast two-hybrid and glutathione S-transferase pull-down assays revealed the new finding that grancalcin interacts strongly with sorcin. In addition, sorcin and grancalcin can be co-immunoprecipitated from lysates of human umbilical vein endothelial cells. Our results indicate that heterodimerization, in addition to differential interactions with target proteins, might be a way to regulate and fine tune processes mediated by calcium binding proteins of the penta-EF hand type.

Published
2003

25. Structure of Ca2+ -loaded human grancalcin.

Author

Jia Jia, Borregaard, Niels, Lollike, Karsten, and Cygler, Miroslaw

Subjects
CALCIUM-binding proteins, CRYSTALS, CRYSTALLOGRAPHY, BIOMOLECULES, CARRIER proteins, PROTEIN binding
Abstract

Grancalcin is a cytosolic Ca2+-binding protein originally identified in human neutrophils. It belongs to a new class of EF-hand proteins, called PEF proteins, which contain five EF-hand motifs. At the N-terminus of grancalcin there is a ∼50 residue-long segment rich in glycines and prolines. The fifth EF-hand, unpaired within the monomer, provides a means for dimerization through pairing with its counterpart in a second molecule. The structure of full-length grancalcin in the apo form and with one EF3 within the dimer occupied by a Ca2+ ion have been determined. Although the N-terminal segment was present in the molecule, this part was disordered in the crystals. Here, the structure of a truncated form of grancalcin, which is lacking 52 N-terminal residues, in the presence and absence of Ca2+ is presented. In the Ca2+-bound form the ions are found in the EF1 and EF3 hands. Binding of Ca2+ to these two EF hands produces only minor conformational changes, mostly within the EF1 Ca2+-binding loop. This observation supports the hypothesis, formulated on the basis of the structure of a homologous protein ALG-2 which shows significant differences in the orientation of EF4 and EF5 compared with grancalcin, that calcium is a necessary factor but not sufficient alone for inducing a significant conformational change in PEF proteins. [ABSTRACT FROM AUTHOR]

Published
2001
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26. Crystallization and preliminary X-ray analysis of human grancalcin, a novel cytosolic Ca2+-binding protein present in leukocytes.

Author

Han, Qing, Jia, Jia, Li, Yunge, Lollike, Karsten, and Cygler, Miroslaw

Subjects
RECOMBINANT proteins, CRYSTALLIZATION, X-ray diffraction, CRYSTALS, LEUCOCYTES, CARRIER proteins
Abstract

Recombinant human grancalcin, a calcium-binding protein from leukocytes, has been crystallized in the presence or absence of Ca2+ by the vapor-diffusion method. Two crystal forms of apo grancalcin were obtained: space group P21, with unit-cell parameters a = 48.4, b = 81.1, c = 46.6 Å, β= 111.3°, diffracting to 1.9 Å, and space group C2, with unit-cell parameters a = 97.0, b = 51.9, c = 75.9 Å, β= 108.5°, diffracting to 2.4 Å. Crystals were also grown in the presence of 5 mM Ca2+. They also belong to space group £2, with unit-cell parameters a = 97.4, b = 50.3, c = 77.6 Å, β = 108.2°, which are very similar to the second apo grancalcin form. These crystals diffract to 2.5 Å. [ABSTRACT FROM AUTHOR]

Published
2000
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27. Ca 2+-dependent translocation of cytosolic proteins to isolated granule subpopulations and plasma membrane from human neutrophils

Author

Borregaard, Niels, Kjeldsen, Lars, Lollike, Karsten, and Sengeløv, Henrik

Abstract

In order to identify cytosolic proteins involved in control of granule exocytosis in human neutrophils, subcellular fractions enriched in each of the 3 major granule subsets were incubated with cytosol from neutrophils in the presence or absence of Ca 2+. After washing, proteins were eluted from the organelles by EGTA, Annexins I, II, IV and VI were found to bind to all organelles studied. In addition, a 28-kDa protein was found to bind exclusively to plasma membranes and secretory vesicles, the most readily exocytosed organelle of neutrophils. Ca 2+-dependent association of cytosolic proteins to different granule subsets may control differential exocytosis of granules.

Published
1992
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