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202. Clonal Variation in Drug and Radiation Response among Glioma-Initiating Cells Is Linked to Proneural-Mesenchymal Transition

Author

Segerman, Anna, Niklasson, Mia, Haglund, Caroline, Bergström, Tobias, Jarvius, Malin, Xie, Yuan, Westermark, Ann, Sönmez, Demet, Hermansson, Annika, Kastemar, Marianne, Naimaie-Ali, Zeinab, Nyberg, Frida, Berglund, Malin, Sundström, Magnus, Hesselager, Göran, Uhrbom, Lene, Gustafsson, Mats, Larsson, Rolf, Fryknäs, Mårten, Segerman, Bo, and Westermark, Bengt

Abstract

Intratumoral heterogeneity is a hallmark of glioblastoma multiforme and thought to negatively affect treatment efficacy. Here, we establish libraries of glioma-initiating cell (GIC) clones from patient samples and find extensive molecular and phenotypic variability among clones, including a range of responses to radiation and drugs. This widespread variability was observed as a continuum of multitherapy resistance phenotypes linked to a proneural-mesenchymal shift in the transcriptome. Multitherapy resistance was associated with a semi-stable cell state that was characterized by an altered DNA methylation pattern at promoter regions of mesenchymal master regulators and enhancers. The gradient of cell states within the GIC compartment constitutes a distinct form of heterogeneity. Our findings may open an avenue toward the development of new therapeutic rationales designed to reverse resistant cell states.

Published
2016
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231. Scandinavian society for the study of diabetes Abstracts Seventh Meeting: Sandefjord, April 15–17, 1971

Author

Östmann, J., Cerasi, E., Efendić, S., Luft, R., Nielsen, J. H., Björntorp, P., Sjöström, L., Walaas, E., Walaas, O., Høstmark, A. T., Spydevold, Ø., Hoddevik, G., Lundquist, I., Løvø, A., Hustvedt, B. E., Pelkonen, R., Nikkilä, E. A., Taskinen, M. -R., Madsen, S. N., Lauridsen, U. B., Deokert, T., Pruett, E. D. R., Hanssen, H. F., Westermark, P., Iversen, J., Täljedal, I. -B., Hellman, B., Sehlin, J., Lernmark, Å., Christensen, H. N., Idahl, L. -Å, Gylfe, E., Asplund, K., Hellerström, C., Berne, Ch., Brolin, S. E., Wettermark, G., Lundqvist, G., Edwards, J., Petersson, B., Johansen, K., Gundersen, H. J. G., Christensen, N. J., Arnmman, K., Carlström, S., Hindberg, I., Pedersen, L. M., Pyörälä, K., Pyörälä, T., Weintraub, D., Victor, A., Oseid, S., Søvik, O., Aagenses, Ø., Vagn-Hansen, C., Frey, H., Falch, D., Forfang, K., Norman, N., Fremstad, D., Jervell, J., Spilker, L. S., Lunell, N. O., Persson, B., Pedersenog, L. M., Pedersen, J., Tygstrup, I., and Villumsen, A. L.

Published
1971
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234. Seventh Annual Meeting of the European Association for the Study of Diabetes: Southampton, England, September 15–17, 1971

Author

Knussman, R., Toeller, M., Kopf, A., Tchobroutsky, G., Eschwege, E., Dauchy, F., Korec, R., Koschinsky, Th., Gries, F. A., Herberg, L., Krug, E., Mialhe, P., Marliss, E. B., Kanazawa, Y., Kikuchi, M., Burr, I. M., Stauffacher, W., Renold, A. E., Lambert, A. E., Orci, L., Blondel, B., Rouiller, C., Langslow, D. R., Freeman, B. M., Laube H., Kruger, C., Goberna, R., Fussganger, R., Teller, W., Pfeiffer, E. F., Raptis, S., Legros, F., Conard, V., Metzger, P., Rogister, C., Tinant, A., Lernmark, A., Hellman, B., Sehlin, J., Täljedal, I. -B., Lesobre, B., Hewitt, J., Canivet, J., Levett, R. E., Korp, W., Loubatières, A., Mariani, M. M., Jallet, F., Lundbak, K., Speich, E., Johansen, K., Ørskov, H., Luyckx, A. S., Massi-Benedetti, F., Lefèbvre, P. J., Malaisse, W. J., Brisson, G. R., Marco, J., Diaz-Fierros, M., Baroja, I. M., Villanueva, M. L., Valverde, I., Massara, F., Camanni, F., Molinatti, G. M., McCarroll, A. M., Murphy, R. F., Teale, J. D., Buchanan, K. D., Menzinger, G., Javicoli, M., Fallucca, F., Tamburrano, G., Andreani, D., Michaelis, D., Jutzi, E., Neumann, I., Schulz, B., Hildmann, W., Bibergeil, H., Mincu, I., Campeanu, S., Dumitrescu, C., Mihalache, N., Mincu, T., Parvulescu, M., Georgescu, S., Nuteanu, V., Mogensen, C. E., Hansen, Aa. Prange, Seyer-Hansen, K., Ruth, C. E., Østerby, C. E., Möller, E. B., Bergström, A. L., Wingstrand, H., Persson, S., Morell, B., Froesch, E. R., Mosora, N., Baciu, Tr., Vincze, J., Motocou, M., Simionesco, Ligia, Duma, V., Gligore, V., Muggio, M., Fedele, D., Bagnariol, G., Tiengo, A., Fellin, R., Enzi, G., Rasmussen, S. Munkgaard, Nielsen, Poul Ebbe, Nielsen, S. Levin, Niklas, L., Otto, H., Fuchs, R., Nye, L., Triggs, S., Landon, J., de Mowbray, R., Oelz, O., Oppermann, W., Iwatsuka, H., Ehrenreich, T., Gordon, A., Camerini-Davalos, R. A., Ammon, H. P. T., Steinke, J., Orsetti, A., Bali, J. P., Serre, Mme A., Mirouze, J., Östman, J., Cerasi, E., Efendić, S., Luft, R., Brinck, U., Sabin, J., Sparthe, R., Wübbens, D., Page, M. A., Williamson, D. H., Panten, U., Kriedstein, Ev., Poser, W., Schönborn, J., Hasselblatt, A., Parry, D. G., Taylor, K. W., Polosa, P., Motta, L., Lunetta, M., Pozza, G., Melogli, O., Viberti, G. C., Pappalettera, A. E., Palmieri, G. C., Tognetti, A., Ghidoni, A., Pyörälä, K., Nikkilä, E. A., Lehtovirta, E., Taskinen, M. -R., Pelkonen, R., Siltanen, P., Schröder, K. E., Rothenbuchner, G., Thum, Ch., Fussgänger, R., Sträub, K., Klör, U., Rastogi, G. K., Sinha, M. K., Dash, R. J., Rehfeld, J. F., Stadil, F., Riveline, B., Verry, M., Rosak, C., Bartelt, K. M., Haupt, E., Beyer, J., Schöffling, K., Rosselin, G., Valleron, A. J., Papoz, L., Birk, J., Loos, U., Rudas, B., Wick, G., Samsel, J., Karmann, H., Schatz, H., Rahman, Y. Abdel, Hinz, M., Katsilambros, N., Maier, V., Fehm, H. L., Schenk, K. E., Quabbe, H. J., Klemens, U., Schröder, R., Schennetten, Felix P. N., Schlichtkrull, J., Scandellari, C., Conte, N., Federspil, G., Frezzato, S., Trisotto, A., Scott, R. D. M., Prud'homme, M., Kipnis, D. M., Bricker, N. S., Klahr, S., Skrabalo, Z., Smith, M. J., Hall, M. R. P., Sodovez, J. C., Sodovez-Goffaux, F., Dunbar, J. C., Foà, P. P., Spaethe, R., Meyer, B., Srivastava, M. C., Sönksen, P. H., Tompkins, C. V., Nabarro, J. D. N., Balant, L., Amherdt, M., Cameron, D. P., Steingaszner, O., Kammerer, L., Bretán, M., Sterne, J., Guilcher, S. Le, Rousselet, M., Stimmler, L., Snodgrass, G. J. A. I., Sutherland, Hamish, Tohobroutsky, G., Assan, R., Tompkins, C. V., Track, N. S., Trap-Jensen, J., Turner, M. R., Heard, C. R. C., Reeds, P. J., Munday, K. A., Vague, P., Oliver, C., Jacquet, P., Vague, J., Warnet, J. M., Claude, J. R., Rathery, M., Lozano, I., van Assche, F. A., van't Laar, A., Vigas, M., Haist, R. E., Braun, W., Drucker, W. R., Vitelli, A., Giangrandi, E., Fusco, E., Scaroina, F., Waldhäusl, W. K., Weiss, L., Löffler, G., Schirmann, A., Wieland, O., Westermark, Per, and Woodroffe, F. J.

Published
1972
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239. Poster Session 2: Monday 4 May 2015, 08:00-18:00 * Room: Poster Area

Author

Bouyoucef, S. E., primary, Uusitalo, V., additional, Kamperidis, V., additional, De Graaf, M., additional, Maaniitty, T., additional, Stenstrom, I., additional, Broersen, A., additional, Scholte, A., additional, Saraste, A., additional, Bax, J., additional, Knuuti, J., additional, Furuhashi, T., additional, Moroi, M., additional, Awaya, T., additional, Masai, H., additional, Minakawa, M., additional, Kunimasa, T., additional, Fukuda, H., additional, Sugi, K., additional, Berezin, A., additional, Kremzer, A., additional, Clerc, O., additional, Kaufmann, B., additional, Possner, M., additional, Liga, R., additional, Vontobel, J., additional, Mikulicic, F., additional, Graeni, C., additional, Benz, D., additional, Kaufmann, P., additional, Buechel, R., additional, Ferreira, M., additional, Cunha, M., additional, Albuquerque, A., additional, Ramos, D., additional, Costa, G., additional, Lima, J., additional, Pego, M., additional, Peix, A., additional, Cisneros, L., additional, Cabrera, L., additional, Padron, K., additional, Rodriguez, L., additional, Heres, F., additional, Carrillo, R., additional, Mena, E., additional, Fernandez, Y., additional, Huizing, E., additional, Van Dijk, J., additional, Van Dalen, J., additional, Timmer, J., additional, Ottervanger, J., additional, Slump, C., additional, Jager, P., additional, Venuraju, S., additional, Jeevarethinam, A., additional, Yerramasu, A., additional, Atwal, S., additional, Mehta, V., additional, Lahiri, A., additional, Arjonilla Lopez, A., additional, Calero Rueda, M. J., additional, Gallardo, G., additional, Fernandez-Cuadrado, J., additional, Hernandez Aceituno, D., additional, Sanchez Hernandez, J., additional, Yoshida, H., additional, Mizukami, A., additional, Matsumura, A., additional, Smettei, O., additional, Abazid, R., additional, Sayed, S., additional, Mlynarska, A., additional, Mlynarski, R., additional, Golba, K., additional, Sosnowski, M., additional, Winther, S., additional, Svensson, M., additional, Jorgensen, H., additional, Bouchelouche, K., additional, Gormsen, L., additional, Holm, N., additional, Botker, H., additional, Ivarsen, P., additional, Bottcher, M., additional, Cortes, C. M., additional, Aramayo G, E., additional, Daicz, M., additional, Casuscelli, J., additional, Alaguibe, E., additional, Neira Sepulveda, A., additional, Cerda, M., additional, Ganum, G., additional, Embon, M., additional, Vigne, J., additional, Enilorac, B., additional, Lebasnier, A., additional, Valancogne, L., additional, Peyronnet, D., additional, Manrique, A., additional, Agostini, D., additional, Menendez, D., additional, Rajpal, S., additional, Kocherla, C., additional, Acharya, M., additional, Reddy, P., additional, Sazonova, I., additional, Ilushenkova, Y., additional, Batalov, R., additional, Rogovskaya, Y., additional, Lishmanov, Y., additional, Popov, S., additional, Varlamova, N., additional, Prado Diaz, S., additional, Jimenez Rubio, C., additional, Gemma, D., additional, Refoyo Salicio, E., additional, Valbuena Lopez, S., additional, Moreno Yanguela, M., additional, Torres, M., additional, Fernandez-Velilla, M., additional, Lopez-Sendon, J., additional, Guzman Martinez, G., additional, Puente, A., additional, Rosales, S., additional, Martinez, C., additional, Cabada, M., additional, Melendez, G., additional, Ferreira, R., additional, Gonzaga, A., additional, Santos, J., additional, Vijayan, S., additional, Smith, S., additional, Smith, M., additional, Muthusamy, R., additional, Takeishi, Y., additional, Oikawa, M., additional, Goral, J. L., additional, Napoli, J., additional, Montana, O., additional, Damico, A., additional, Quiroz, M., additional, Forcada, P., additional, Schmidberg, J., additional, Zucchiatti, N., additional, Olivieri, D., additional, Dumo, A., additional, Ruano, S., additional, Rakhit, R., additional, Davar, J., additional, Nair, D., additional, Cohen, M., additional, Darko, D., additional, Yokota, S., additional, Maas, A., additional, Mouden, M., additional, Knollema, S., additional, Sanja Mazic, S., additional, Lazovic, B., additional, Marina Djelic, M., additional, Jelena Suzic Lazic, J., additional, Tijana Acimovic, T., additional, Milica Deleva, M., additional, Vesnina, Z., additional, Zafrir, N., additional, Bental, T., additional, Mats, I., additional, Solodky, A., additional, Gutstein, A., additional, Hasid, Y., additional, Belzer, D., additional, Kornowski, R., additional, Ben Said, R., additional, Ben Mansour, N., additional, Ibn Haj Amor, H., additional, Chourabi, C., additional, Hagui, A., additional, Fehri, W., additional, Hawala, H., additional, Shugushev, Z., additional, Patrikeev, A., additional, Maximkin, D., additional, Chepurnoy, A., additional, Kallianpur, V., additional, Mambetov, A., additional, Dokshokov, G., additional, Teresinska, A., additional, Wozniak, O., additional, Maciag, A., additional, Wnuk, J., additional, Dabrowski, A., additional, Czerwiec, A., additional, Jezierski, J., additional, Biernacka, K., additional, Robinson, J., additional, Prosser, J., additional, Cheung, G., additional, Allan, S., additional, Mcmaster, G., additional, Reid, S., additional, Tarbuck, A., additional, Martin, W., additional, Queiroz, R., additional, Falcao, A., additional, Giorgi, M., additional, Imada, R., additional, Nogueira, S., additional, Chalela, W., additional, Kalil Filho, R., additional, Meneghetti, W., additional, Matveev, V., additional, Bubyenov, A., additional, Podzolkov, V., additional, Baranovich, V., additional, Faibushevich, A., additional, Kolzhecova, Y., additional, Volkova, O., additional, Fernandez, J., additional, Lopez, G., additional, Dondi, M., additional, Paez, D., additional, Butcher, C., additional, Reyes, E., additional, Al-Housni, M., additional, Green, R., additional, Santiago, H., additional, Ghiotto, F., additional, Hinton-Taylor, S., additional, Pottle, A., additional, Mason, M., additional, Underwood, S., additional, Casans Tormo, I., additional, Diaz-Exposito, R., additional, Plancha-Burguera, E., additional, Elsaban, K., additional, Alsakhri, H., additional, Yoshinaga, K., additional, Ochi, N., additional, Tomiyama, Y., additional, Katoh, C., additional, Inoue, M., additional, Nishida, M., additional, Suzuki, E., additional, Manabe, O., additional, Ito, Y., additional, Tamaki, N., additional, Tahilyani, A., additional, Jafary, F., additional, Ho Hee Hwa, H., additional, Ozdemir, S., additional, Kirilmaz, B., additional, Barutcu, A., additional, Tan, Y., additional, Celik, F., additional, Sakgoz, S., additional, Cabada Gamboa, M., additional, Puente Barragan, A., additional, Morales Vitorino, N., additional, Medina Servin, M., additional, Hindorf, C., additional, Akil, S., additional, Hedeer, F., additional, Jogi, J., additional, Engblom, H., additional, Martire, V., additional, Pis Diez, E., additional, Martire, M., additional, Portillo, D., additional, Hoff, C., additional, Balche, A., additional, Majgaard, J., additional, Tolbod, L., additional, Harms, H., additional, Soerensen, J., additional, Froekiaer, J., additional, Nudi, F., additional, Neri, G., additional, Procaccini, E., additional, Pinto, A., additional, Vetere, M., additional, Biondi-Zoccai, G., additional, Soares, J., additional, Do Val, R., additional, Oliveira, M., additional, Meneghetti, J., additional, Tekabe, Y., additional, Anthony, T., additional, Li, Q., additional, Schmidt, A., additional, Johnson, L., additional, Groenman, M., additional, Tarkia, M., additional, Kakela, M., additional, Halonen, P., additional, Kiviniemi, T., additional, Pietila, M., additional, Yla-Herttuala, S., additional, Roivainen, A., additional, Nekolla, S., additional, Swirzek, S., additional, Higuchi, T., additional, Reder, S., additional, Schachoff, S., additional, Bschorner, M., additional, Laitinen, I., additional, Robinson, S., additional, Yousefi, B., additional, Schwaiger, M., additional, Kero, T., additional, Lindsjo, L., additional, Antoni, G., additional, Westermark, P., additional, Carlson, K., additional, Wikstrom, G., additional, Sorensen, J., additional, Lubberink, M., additional, Rouzet, F., additional, Cognet, T., additional, Guedj, K., additional, Morvan, M., additional, El Shoukr, F., additional, Louedec, L., additional, Choqueux, C., additional, Nicoletti, A., additional, Le Guludec, D., additional, Jimenez-Heffernan, A., additional, Munoz-Beamud, F., additional, Sanchez De Mora, E., additional, Borrachero, C., additional, Salgado, C., additional, Ramos-Font, C., additional, Lopez-Martin, J., additional, Hidalgo, M., additional, Lopez-Aguilar, R., additional, Soriano, E., additional, Okizaki, A., additional, Nakayama, M., additional, Ishitoya, S., additional, Sato, J., additional, Takahashi, K., additional, Burchert, I., additional, Caobelli, F., additional, Wollenweber, T., additional, Nierada, M., additional, Fulsche, J., additional, Dieckmann, C., additional, Bengel, F., additional, Shuaib, S., additional, Mahlum, D., additional, Port, S., additional, Refoyo, E., additional, Cuesta, E., additional, Guzman, G., additional, Lopez, T., additional, Valbuena, S., additional, Del Prado, S., additional, Moreno, M., additional, Harbinson, M., additional, Donnelly, L., additional, Einstein, A. J., additional, Johnson, L. L., additional, Deluca, A. J., additional, Kontak, A. C., additional, Groves, D. W., additional, Stant, J., additional, Pozniakoff, T., additional, Cheng, B., additional, Rabbani, L. E., additional, Bokhari, S., additional, Schuetze, C., additional, Aguade-Bruix, S., additional, Pizzi, M., additional, Romero-Farina, G., additional, Terricabras, M., additional, Villasboas, D., additional, Castell-Conesa, J., additional, Candell-Riera, J., additional, Brunner, S., additional, Gross, L., additional, Todica, A., additional, Lehner, S., additional, Di Palo, A., additional, Niccoli Asabella, A., additional, Magarelli, C., additional, Notaristefano, A., additional, Ferrari, C., additional, Rubini, G., additional, Sellem, A., additional, Melki, S., additional, Elajmi, W., additional, Hammami, H., additional, Ziadi, M., additional, Montero, J., additional, Ameriso, J., additional, Villavicencio, R., additional, Benito Gonzalez, T. F., additional, Mayorga Bajo, A., additional, Gutierrez Caro, R., additional, Rodriguez Santamarta, M., additional, Alvarez Roy, L., additional, Martinez Paz, E., additional, Barinaga Martin, C., additional, Martin Fernandez, J., additional, Alonso Rodriguez, D., additional, Iglesias Garriz, I., additional, Rosillo, S., additional, Taleb, S., additional, Cherkaoui Salhi, G., additional, Regbaoui, Y., additional, Ait Idir, M., additional, Guensi, A., additional, Martin Lopez, C. E., additional, and Castano Ruiz, M., additional

Published
2015
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240. Purification of Transthyretin and Transthyretin Fragments From Amyloid-Rich Human Tissues.

Author

Walker, John M., Sigurdsson, Einar M., Westermark, Per, and Westermark, Gunilla T.

Abstract

Transthyretin is the major amyloid fibril protein in many forms of familial systemic amyloidosis where a missense mutation creates an amyloidogenic protein, and in senile systemic amyloidosis in which wild-type transthyretin aggregates into amyloid fibrils. The amyloid deposits may consist of full-length transthyretin but is very often, in senile systemic amyloidosis always, a mixture of full-length transthyretin and C-terminal transthyretin fragments. The amyloid fibril protein mixture can be purified by extraction of fibrils followed by sequential gel filtration after solubilization in a solution of guanidine hydrochloride. Since the C-terminal transthyretin fragments lack cysteine residues, a method to separate full-length transthyretin from fragments by covalent chromatography has been developed. [ABSTRACT FROM AUTHOR]

Published
2005
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241. Purification of Amyloid Protein AA Subspecies From Amyloid-Rich Human Tissues.

Author

Walker, John M., Sigurdsson, Einar M., Westermark, Gunilla T., and Westermark, Per

Abstract

Protein AA, the major amyloid fibril protein in reactive (secondary) systemic amyloidosis is derived from the acute phase reactant liver-produced apolipoprotein serum AA (SAA) by proteolytic cleavage, usually in the C-terminal half of the 104 amino acid residues long precursor. The cleavage points in SAA vary between patients and the deposited protein AA is often quite heterogeneous. In this chapter, we describe methods to extract amyloid fibrils and to purify protein AA by sequential gel filtration. Further purification of subspecies of protein AA is best achieved by the use of differences in charge and chromatofocusing is described as the method of choice. Analytic methods include sodium dodecylsulfate polyacrylamide gel electrophoresis and analytic isoelectric focusing. [ABSTRACT FROM AUTHOR]

Published
2005
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242. NMR structure of C-terminal domain from A. ventricosus minor ampullate spidroin (MiSp)

Author

Otikovs, M., primary, Jaudzems, K., additional, Andersson, M., additional, Chen, G., additional, Landreh, M., additional, Nordling, K., additional, Kronqvist, N., additional, Westermark, P., additional, Jornvall, H., additional, Knight, S., additional, Ridderstrale, Y., additional, Holm, L., additional, Meng, Q., additional, Chesler, M., additional, Johansson, J., additional, and Rising, A., additional

Published
2014
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243. Luminescent conjugated oligothiophenes: A novel dye for amyloid diagnostics

Author

Sjölander, Daniel, Mason, Jeffrey, Westermark, G. T., Westermark, P., Hammarström, Per, Nilsson, Peter, Sjölander, Daniel, Mason, Jeffrey, Westermark, G. T., Westermark, P., Hammarström, Per, and Nilsson, Peter

Abstract

The alkaline Congo red staining method has, for almost half a century, been the gold standard of amyloid diagnosis. Unfortunately, the method is both laborious and requires great skill to achieve proper diagnosis. In this study we are presenting an alternative method that is compatible with immunofluorescence typing. We used a novel dye, h-FTAA, designed and synthesized by us. The dye belongs to the novel class of conformation sensitive dyes known as Luminescent conjugated oligothiophenes (LCOs). We examined 37 different cases of systemic amyloidoses from various tissues. It was found that h-FTAA binds to amyloid with higher sensitivity and greater selectivity than Congo red, as was determined by both fluorescence- and light polarization microscopy. Due to the methods ease of use and performance compared to Congo red, it is concluded that h-FTAA is a better first choice for screening of systemic amyloidoses.

Published
2013

244. Transplantation of macroencapsulated human islets within the bioartificial pancreas βAir to patients with type 1 diabetes mellitus

Author

Carlsson, Per‐Ola, Espes, Daniel, Sedigh, Amir, Rotem, Avi, Zimerman, Baruch, Grinberg, Helena, Goldman, Tali, Barkai, Uriel, Avni, Yuval, Westermark, Gunilla T., Carlbom, Lina, Ahlström, Håkan, Eriksson, Olof, Olerud, Johan, and Korsgren, Olle

Abstract

Macroencapsulation devices provide the dual possibility of immunoprotecting transplanted cells while also being retrievable, the latter bearing importance for safety in future trials with stem cell–derived cells. However, macroencapsulation entails a problem with oxygen supply to the encapsulated cells. The βAir device solves this with an incorporated refillable oxygen tank. This phase 1 study evaluated the safety and efficacy of implanting the βAir device containing allogeneic human pancreatic islets into patients with type 1 diabetes. Four patients were transplanted with 1‐2 βAir devices, each containing 155 000‐180 000 islet equivalents (ie, 1800‐4600 islet equivalents per kg body weight), and monitored for 3‐6 months, followed by the recovery of devices. Implantation of the βAir device was safe and successfully prevented immunization and rejection of the transplanted tissue. However, although beta cells survived in the device, only minute levels of circulating C‐peptide were observed with no impact on metabolic control. Fibrotic tissue with immune cells was formed in capsule surroundings. Recovered devices displayed a blunted glucose‐stimulated insulin response, and amyloid formation in the endocrine tissue. We conclude that the βAir device is safe and can support survival of allogeneic islets for several months, although the function of the transplanted cells was limited (Clinicaltrials.gov: NCT02064309). An investigator‐initiated phase 1 study of the safety and efficacy of implanting the macroencapsulation device βAir with an incorporated refillable oxygen tank containing allogeneic human pancreatic islets into 4 patients with type 1 diabetes shows that the device is safe and can support survival of allogeneic islets for several months, though the function of the transplanted cells is limited.

Published
2018
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245. Living by the shore: Mesolithic dwellings and household in Motala, eastern central Sweden, 5600–5000calBC

Author

Molin, Fredrik, Hagberg, Linus, and Westermark, Ann

Abstract

Dwellings symbolize culture, give meaning to everyday activities and provide central places for a range of household activities. This study focuses on hunter-gatherer households at the Late Mesolithic settlement in Motala, and the spatial arrangement of indoor and outdoor activities of two well preserved dwellings, Dwelling 4 and 6, at the site Strandvägen. We present structural elements as well as utilized lithics, firewood selection and choices in diet and food consumption. By studying methods of fishing and remains of fish processing we conclude that the inhabitants must have had ways of storage at the site. Through a combination of archaeobothanical studies and chemical analyzes we also confirm the exploitation of starch rich rhizomes and root tubers as part of the diet at the settlement. Post-built constructions, indoor hearths and estimated floor areas suggest the use of the dwellings as winter residences and probably utilized by multiple family units.

Published
2018
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246. In VivoSeeding and Cross-Seeding of Localized Amyloidosis

Author

Oskarsson, Marie E., Paulsson, Johan F., Schultz, Sebastian W., Ingelsson, Martin, Westermark, Per, and Westermark, Gunilla T.

Abstract

Several proteins have been identified as amyloid forming in humans, and independent of protein origin, the fibrils are morphologically similar. Therefore, there is a potential for structures with amyloid seeding ability to induce both homologous and heterologous fibril growth; thus, molecular interaction can constitute a link between different amyloid forms. Intravenous injection with preformed fibrils from islet amyloid polypeptide (IAPP), proIAPP, or amyloid-beta (Aβ) into human IAPP transgenic mice triggered IAPP amyloid formation in pancreas in 5 of 7 mice in each group, demonstrating that IAPP amyloid could be enhanced through homologous and heterologous seeding with higher efficiency for the former mechanism. Proximity ligation assay was used for colocalization studies of IAPP and Aβ in islet amyloid in type 2 diabetic patients and Aβ deposits in brains of patients with Alzheimer disease. Aβ reactivity was not detected in islet amyloid although islet β cells express AβPP and convertases necessary for Aβ production. By contrast, IAPP and proIAPP were detected in cerebral and vascular Aβ deposits, and presence of proximity ligation signal at both locations showed that the peptides were <40 nm apart. It is not clear whether IAPP present in brain originates from pancreas or is locally produced. Heterologous seeding between IAPP and Aβ shown here may represent a molecular link between type 2 diabetes and Alzheimer disease.

Published
2015
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248. Fibrils from designed non-amyloid-related synthetic peptides induce AA-amyloidosis during inflammation in an animal model

Author

Westermark, P., Lundmark, Katarzyna, Westermark, Gunilla, Westermark, P., Lundmark, Katarzyna, and Westermark, Gunilla

Abstract

Background: Mouse AA-amyloidosis is a transmissible disease by a prion-like mechanism where amyloid fibrils act by seeding. Synthetic peptides with no amyloid relationship can assemble into amyloid-like fibrils and these may have seeding capacity for amyloid proteins. Principal Findings: Several synthetic peptides, designed for nanotechnology, have been examined for their ability to produce fibrils with Congo red affinity and concomitant green birefringence, affinity for thioflavin S and to accelerate AA-amyloidosis in mice. It is shown that some amphiphilic fibril-forming peptides not only produced Congo red birefringence and showed affinity for thioflavin S, but they also shortened the lag phase for systemic AA-amyloidosis in mice when they were given intravenously at the time of inflammatory induction with silver nitride. Peptides, not forming amyloid-like fibrils, did not have such properties. Conclusions: These observations should caution researchers and those who work with synthetic peptides and their derivatives to be aware of the potential health concerns. © 2009 Westermark et al., Original Publication:P. Westermark, Katarzyna Lundmark and Gunilla Westermark, Fibrils from designed non-amyloid-related synthetic peptides induce AA-amyloidosis during inflammation in an animal model, 2009, PLoS ONE, (4), 6, e6041.http://dx.doi.org/10.1371/journal.pone.0006041

Published
2009
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249. Serum amyloid A and protein AA : Molecular mechanisms of a transmissible amyloidosis

Author

Westermark, Gunilla, Westermark, P., Westermark, Gunilla, and Westermark, P.

Abstract

Systemic AA-amyloidosis is a complication of chronic inflammatory diseases and the fibril protein AA derives from the acute phase reactant serum AA. AA-amyloidosis can be induced in mice by an inflammatory challenge. The lag phase before amyloid develops can be dramatically shortened by administration of a small amount of amyloid fibrils. Systemic AA-amyloidosis is transmissible in mice and may be so in humans. Since transmission can cross species barriers it is possible that AA-amyloidosis can be induced by amyloid in food, e.g. foie gras. In mice, development of AA-amyloidosis can also be accelerated by other components with amyloid-like properties. A new possible risk factor may appear with synthetically made fibrils from short peptides, constructed for tissue repair.

Published
2009
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250. Amyloid fibril composition is related to the phenotype of hereditary transthyretin V30M amyloidosis

Author

Ihse, E., Ybo, A., Suhr, Ole B., Lindqvist, Per, Backman, Christer, Westermark, P., Ihse, E., Ybo, A., Suhr, Ole B., Lindqvist, Per, Backman, Christer, and Westermark, P.

Abstract

Swedish familial systemic amyloidosis with polyneuropathy (FAP) depends on a mutation leading to a methionine‐for‐valine substitution in transthyretin. The disease appears with different clinical manifestations, including age of onset and involvement of the heart. Liver transplantation is currently the only curative treatment, but progressive cardiomyopathy may occur post‐transplant. Two amyloid deposition patterns have previously been described in the heart. In one, the amyloid consists partially of transthyretin fragments and is weakly stainable by Congo red, while in the other, only full‐length molecules are found and the fibrils have a strong affinity for Congo red. The present study aimed to see whether these morphological and biochemical variations have clinical implications. Subcutaneous adipose tissue biopsies were taken from 33 patients with Val30Met FAP and examined by microscopy, electrophoresis and western blot. Clinical data included age, sex, duration of disease and echocardiographic determination of the interventricular septum (IVS) thickness. It was found that fibrils composed of only full‐length transthyretin were associated with early age of onset (44.8 ± 12.9 years), no clinical cardiac involvement and a strong affinity for Congo red. In contrast, presence of transthyretin fragments in the amyloid was associated with late age of onset (67.3 ± 7.0 years), signs of cardiac involvement and weak Congo red staining. For each individual, the same molecular type of amyloid was found in different organs. This is the first report showing that variations in clinical appearance of familial ATTR amyloidosis are associated with specific structural differences in the amyloid fibrils, and therefore may have a molecular cause. The molecular type of amyloid can be determined from a subcutaneous fat tissue biopsy.

Published
2008
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