TY  - JOUR
A1  - Chipman, Ariel D.
A1  - Ferrier, David E. K.
A1  - Brena, Carlo
A1  - Qu, Jiaxin
A1  - Hughes, Daniel S. T.
A1  - Schroeder, Reinhard
A1  - Torres-Oliva, Montserrat
A1  - Znassi, Nadia
A1  - Jiang, Huaiyang
A1  - Almeida, Francisca C.
A1  - Alonso, Claudio R.
A1  - Apostolou, Zivkos
A1  - Aqrawi, Peshtewani
A1  - Arthur, Wallace
A1  - Barna, Jennifer C. J.
A1  - Blankenburg, Kerstin P.
A1  - Brites, Daniela
A1  - Capella-Gutierrez, Salvador
A1  - Coyle, Marcus
A1  - Dearden, Peter K.
A1  - Du Pasquier, Louis
A1  - Duncan, Elizabeth J.
A1  - Ebert, Dieter
A1  - Eibner, Cornelius
A1  - Erikson, Galina
A1  - Evans, Peter D.
A1  - Extavour, Cassandra G.
A1  - Francisco, Liezl
A1  - Gabaldon, Toni
A1  - Gillis, William J.
A1  - Goodwin-Horn, Elizabeth A.
A1  - Green, Jack E.
A1  - Griffiths-Jones, Sam
A1  - Grimmelikhuijzen, Cornelis J. P.
A1  - Gubbala, Sai
A1  - Guigo, Roderic
A1  - Han, Yi
A1  - Hauser, Frank
A1  - Havlak, Paul
A1  - Hayden, Luke
A1  - Helbing, Sophie
A1  - Holder, Michael
A1  - Hui, Jerome H. L.
A1  - Hunn, Julia P.
A1  - Hunnekuhl, Vera S.
A1  - Jackson, LaRonda
A1  - Javaid, Mehwish
A1  - Jhangiani, Shalini N.
A1  - Jiggins, Francis M.
A1  - Jones, Tamsin E.
A1  - Kaiser, Tobias S.
A1  - Kalra, Divya
A1  - Kenny, Nathan J.
A1  - Korchina, Viktoriya
A1  - Kovar, Christie L.
A1  - Kraus, F. Bernhard
A1  - Lapraz, Francois
A1  - Lee, Sandra L.
A1  - Lv, Jie
A1  - Mandapat, Christigale
A1  - Manning, Gerard
A1  - Mariotti, Marco
A1  - Mata, Robert
A1  - Mathew, Tittu
A1  - Neumann, Tobias
A1  - Newsham, Irene
A1  - Ngo, Dinh N.
A1  - Ninova, Maria
A1  - Okwuonu, Geoffrey
A1  - Ongeri, Fiona
A1  - Palmer, William J.
A1  - Patil, Shobha
A1  - Patraquim, Pedro
A1  - Pham, Christopher
A1  - Pu, Ling-Ling
A1  - Putman, Nicholas H.
A1  - Rabouille, Catherine
A1  - Ramos, Olivia Mendivil
A1  - Rhodes, Adelaide C.
A1  - Robertson, Helen E.
A1  - Robertson, Hugh M.
A1  - Ronshaugen, Matthew
A1  - Rozas, Julio
A1  - Saada, Nehad
A1  - Sanchez-Gracia, Alejandro
A1  - Scherer, Steven E.
A1  - Schurko, Andrew M.
A1  - Siggens, Kenneth W.
A1  - Simmons, DeNard
A1  - Stief, Anna
A1  - Stolle, Eckart
A1  - Telford, Maximilian J.
A1  - Tessmar-Raible, Kristin
A1  - Thornton, Rebecca
A1  - van der Zee, Maurijn
A1  - von Haeseler, Arndt
A1  - Williams, James M.
A1  - Willis, Judith H.
A1  - Wu, Yuanqing
A1  - Zou, Xiaoyan
A1  - Lawson, Daniel
A1  - Muzny, Donna M.
A1  - Worley, Kim C.
A1  - Gibbs, Richard A.
A1  - Akam, Michael
A1  - Richards, Stephen
T1  - The first myriapod genome sequence reveals conservative arthropod gene content and genome organisation in the centipede Strigamia maritima
JF  - PLoS biology
N2  - Myriapods (e. g., centipedes and millipedes) display a simple homonomous body plan relative to other arthropods. All members of the class are terrestrial, but they attained terrestriality independently of insects. Myriapoda is the only arthropod class not represented by a sequenced genome. We present an analysis of the genome of the centipede Strigamia maritima. It retains a compact genome that has undergone less gene loss and shuffling than previously sequenced arthropods, and many orthologues of genes conserved from the bilaterian ancestor that have been lost in insects. Our analysis locates many genes in conserved macro-synteny contexts, and many small-scale examples of gene clustering. We describe several examples where S. maritima shows different solutions from insects to similar problems. The insect olfactory receptor gene family is absent from S. maritima, and olfaction in air is likely effected by expansion of other receptor gene families. For some genes S. maritima has evolved paralogues to generate coding sequence diversity, where insects use alternate splicing. This is most striking for the Dscam gene, which in Drosophila generates more than 100,000 alternate splice forms, but in S. maritima is encoded by over 100 paralogues. We see an intriguing linkage between the absence of any known photosensory proteins in a blind organism and the additional absence of canonical circadian clock genes. The phylogenetic position of myriapods allows us to identify where in arthropod phylogeny several particular molecular mechanisms and traits emerged. For example, we conclude that juvenile hormone signalling evolved with the emergence of the exoskeleton in the arthropods and that RR-1 containing cuticle proteins evolved in the lineage leading to Mandibulata. We also identify when various gene expansions and losses occurred. The genome of S. maritima offers us a unique glimpse into the ancestral arthropod genome, while also displaying many adaptations to its specific life history.
Y1  - 2014
U6  - https://doi.org/10.1371/journal.pbio.1002005
SN  - 1545-7885
VL  - 12
IS  - 11
PB  - PLoS
CY  - San Fransisco
ER  - 
TY  - JOUR
A1  - Hauser, Sandra
A1  - Wodtke, Robert
A1  - Tondera, Christoph
A1  - Wodtke, Johanna
A1  - Neffe, Axel T.
A1  - Hampe, Jochen
A1  - Lendlein, Andreas
A1  - Löser, Reik
A1  - Pietzsch, Jens
T1  - Characterization of Tissue Transglutaminase as a Potential Biomarker for Tissue Response toward Biomaterials
JF  - ACS biomaterials science & engineering
N2  - Tissue transglutaminase (TGase 2) is proposed to be important for biomaterial-tissue interactions due to its presence and versatile functions in the extracellular environment. TGase 2 catalyzes the cross-linking of proteins through its Ca2+-dependent acyltransferase activity. Moreover, it enhances the interactions between fibronectin and integrins, which in turn mediates the adhesion, migration, and motility of the cells. TGase 2 is also a key player in the pathogenesis of fibrosis. In this study, we investigated whether TGase 2 is present at the biomaterial tissue interface and might serve as an informative biomarker for the visualization of tissue response toward gelatin-based biomaterials. Two differently cross-linked hydrogels were used, which were obtained by the reaction of gelatin with lysine diisocyanate ethyl ester. The overall expression of TGase 2 by endothelial cells, macrophages, and granulocytes was partly influenced by contact to the hydrogels or their degradation products, although no clear correlation was evidenced. In contrast, the secretion of TGase 2 differed remarkably between the different cells, indicating that it might be involved in the cellular reaction toward gelatin-based hydrogels. The hydrogels were implanted subcutaneously in immunocompetent, hairless SKH1-Elite mice. Ex vivo immunohistochemical analysis of tissue sections over 112 days revealed enhanced expression of TGase 2 around the hydrogels, in particular at days 14 and 21 post-implantation. The incorporation of fluorescently labeled cadaverine derivatives for the detection of active TGase 2 was in accordance with the results of the expression analysis. The presence of an irreversible inhibitor of TGase 2 led to attenuated incorporation of the cadaverines, which verified the catalytic action of TGase 2. Our in vitro and ex vivo results verified TGase 2 as a potential biomarker for tissue response toward gelatin-based hydrogels. In vivo, no TGase 2 activity was detectable, which is mainly attributed to the unfavorable physicochemical properties of the cadaverine probe used.
KW  - extracellular matrix modifying enzymes
KW  - gelatin-based hydrogels
KW  - biomaterial-tissue interface
KW  - polyamines
KW  - optical imaging
Y1  - 2019
U6  - https://doi.org/10.1021/acsbiomaterials.9b01299
SN  - 2373-9878
VL  - 5
IS  - 11
SP  - 5979
EP  - 5989
PB  - American Chemical Society
CY  - Washington
ER  -