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11.
K Michałek M Laszczyńska AK Ciechanowicz A Herosimczyk I Rotter M Oganowska 《Biotechnic & histochemistry》2014,89(5):342-347
Aquaporin 2 (AQP2) is a small, integral tetrameric plasma membrane protein that is expressed in mammalian kidneys. The specific constitution of this protein and its selective permeability to water means that AQP2 plays an important role in hypertonic urine production. Immunolocalization of AQP2 has been studied in humans, monkeys, sheep, dogs, rabbits, rats, mice and adult cattle. We analyzed the expression of AQP2 in kidneys of 7-month-old Polish-Friesian var. black and white male calves. AQP2 was localized in the principal cells of collecting ducts in medullary rays penetrating the renal cortex and in the collecting ducts of renal medulla. AQP2 was expressed most strongly in the apical plasma membrane, but expression was observed also in the intracellular vesicles and basolateral plasma membrane. Our study provides new information concerning the immunolocalization of AQP2 in calf kidneys. 相似文献
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The sequences of the 5' long-terminal repeat (LTR) and adjacent leader
regions of 27 full-length copia elements isolated from natural populations
of Drosophila melanogaster, D. simulans, and D. mauritiana are presented.
Phylogenetic analyses indicate that although D. melanogaster copia elements
are distinct from those of D. simulans and D. mauritiana, the elements of
these latter two species are not distinguishable from one another. LTRs and
adjacent 5' leader regions of elements isolated from D. simulans and D.
mauritiana are structurally similar to one another and carry substantial
deletional variation mapping to regions previously identified as being of
potential importance for copia expression.
相似文献
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Rosalba Lepore Andriy Kryshtafovych Markus Alahuhta Harshul A. Veraszto Yannick J. Bomble Joshua C. Bufton Alex N. Bullock Cody Caba Hongnan Cao Owen R. Davies Ambroise Desfosses Matthew Dunne Krzysztof Fidelis Celia W. Goulding Manickam Gurusaran Irina Gutsche Christopher J. Harding Marcus D. Hartmann Christopher S. Hayes Andrzej Joachimiak Petr G. Leiman Peter Loppnau Andrew L. Lovering Vladimir V. Lunin Karolina Michalska Ignacio Mir-Sanchis AK Mitra John Moult George N. Phillips Jr Daniel M. Pinkas Phoebe A. Rice Yufeng Tong Maya Topf Jonathan D. Walton Torsten Schwede 《Proteins》2019,87(12):1037-1057
The functional and biological significance of selected CASP13 targets are described by the authors of the structures. The structural biologists discuss the most interesting structural features of the target proteins and assess whether these features were correctly reproduced in the predictions submitted to the CASP13 experiment. 相似文献
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Adults of the human parasitic trematode Schistosoma mansoni, which causes
hepatosplenic/intestinal complications in humans, synthesize
glycoconjugates containing the Lewis x (Lex) Galbeta1-->4(Fucalpha1--
>3)GlcNAcbeta1-->R, but not sialyl Lewis x (sLex), antigen. We now
report on our analyses of Lexand sLexexpression in S.haematobium and
S.japonicum, which are two other major species of human schistosomes that
cause disease, and the possible autoimmunity to these antigens in infected
individuals. Antigen expression was evaluated by both ELISA and Western
blot analyses of detergent extracts of parasites using monoclonal
antibodies. Several high molecular weight glycoproteins in both S.
haematobium and S. japonicum contain the Lexantigen, but no sialyl
Lexantigen was detected. In addition, sera from humans and rodents infected
with S.haematobium and S.japonicum contain antibodies reactive with Lex.
These results led us to investigate whether Lexantigens are expressed in
other helminths, including the parasitic trematode Fasciola hepatica , the
parasitic nematode Dirofilaria immitis (dog heartworm), the ruminant
nematode Haemonchus contortus , and the free-living nematode Caenorhabditis
elegans . Neither Lexnor sialyl-Lexis detectable in these other helminths.
Furthermore, none of the helminths, including schistosomes, express Lea,
Leb, Ley, or the H- type 1 antigen. However, several glycoproteins from all
helminths analyzed are bound by Lotus tetragonolobus agglutinin , which
binds Fucalpha1-->3GlcNAc, and Wisteria floribunda agglutinin, which
binds GalNAcbeta1-->4GlcNAc (lacdiNAc or LDN). Thus, schistosomes may be
unique among helminths in expressing the Lexantigen, whereas many different
helminths may express alpha1,3-fucosylated glycans and the LDN motif.
相似文献
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