2,343 research outputs found
Loss and reappearance of gap junctions in regenerating liver
Changes in intercellular junctional morphology associated with rat liver regeneration were examined in a freeze-fracture study. After a two-thirds partial hepatectomy, both gap junctions and zonulae occludentes were drastically altered. Between 0 and 20 h after partial hepatectomy, the junctions appeared virtually unchanged. 28 h after partial hepatectomy, however, the large gap junctions usually located close to the bile canaliculi and the small gap junctions enmeshed within the strands of the zonulae occudentes completely disappeared. Although the zonulae occludentes bordering the bile canaliculi apparently remained intact, numerous strands could now be found oriented perpendicular to the canaliculi. In some instances, the membrane outside the canaliculi was extensively filled with isolated junctional strands, often forming very complex configurations. About 40 h after partial hepatectomy, very many small gap junctions reappeared in close association with the zonulae occludentes. Subsequently, gap junctions increased in size and decreased in number until about 48 h after partial hepatectomy when gap junctions were indistinguishable in size and number from those of control animals. The zonulae occludentes were again predominantly located around the canalicular margins. These studies provide further evidence for the growth of gap junctions by the accretion of particles and of small gap junctions to form large maculae
Molecular cloning and characterization of a new member of the gap junction gene family, connexin-31
A new member of the connexin gene family has been identified and designated rat connexin-31 (Cx31) based on its predicted molecular mass of 30,960 daltons. Cx31 is 270 amino acids long and is coded for by a single copy gene. It is expressed as a 1.7-kilobase mRNA that is detected in placenta, Harderian gland, skin, and eye. Cx31 is highly conserved and can be detected in species as distantly related to rat as Xenopus laevis. It exhibits extensive sequence similarity to the previously identified connexins, 58, 50, and 40% amino acid identity to Cx26, Cx32, and Cx43, respectively. When conservation of predicted phosphorylation sites is used to adjust the alignment of Cx31 to other connexins, a unique alignment of three predicted protein kinase C phosphorylation sites near the carboxyl terminus of Cx31 with three sites at the carboxyl terminus of Cx43 is revealed
Inhibition of gap junction and adherens junction assembly by connexin and A-CAM antibodies
We examined the roles of the extracellular domains of a gap junction protein and a cell adhesion molecule in gap junction and adherens junction formation by altering cell interactions with antibody Fab fragments. Using immunoblotting and immunocytochemistry we demonstrated that Novikoff cells contained the gap junction protein, connexin43 (Cx43), and the cell adhesion molecule, A-CAM (N-cadherin). Cells were dissociated in EDTA, allowed to recover, and reaggregated for 60 min in media containing Fab fragments prepared from a number of antibodies. We observed no cell-cell dye transfer 4 min after microinjection in 90% of the cell pairs treated with Fab fragments of antibodies for the first or second extracellular domain of Cx43, the second extracellular domain of connexin32 (Cx32) or A-CAM. Cell-cell dye transfer was detected within 30 s in cell pairs treated with control Fab fragments (pre-immune serum, antibodies to the rat major histocompatibility complex or the amino or carboxyl termii of Cx43). We observed no gap junctions by freeze-fracture EM and no adherens junctions by thin section EM between cells treated with the Fab fragments that blocked cell-cell dye transfer. Gap junctions were found on approximately 50% of the cells in control samples using freeze-fracture EM. We demonstrated with reaggregated Novikoff cells that: (a) functional interactions of the extracellular domains of the connexins were necessary for the formation of gap junction channels; (b) cell interactions mediated by A-CAM were required for gap junction assembly; and (c) Fab fragments of antibodies for A-CAM or connexin extracellular domains blocked adherens junction formation
The 43-kD polypeptide of heart gap junctions: immunolocalization, topology, and functional domains
Analysis by SDS-PAGE of gap junction fractions isolated from heart suggests that the junctions are comprised of a protein with an Mr 43,000. Antibodies against the electroeluted protein and a peptide representing the 20 amino terminal residues bind specifically on immunoblots to the 43-kD protein and to the major products arising from proteolysis during isolation. By immunocytochemistry, the protein is found in ventricle and atrium in patterns consistent with the known distribution of gap junctions. Both antibodies bind exclusively to gap junctions in fractions from heart examined by EM after gold labeling. Since only domains of the protein exposed at the cytoplasmic surface should be accessible to antibody, we conclude that the 43-kD protein is assembled in gap junctions with the amino terminus of the molecule exposed on the cytoplasmic side of the bilayer, that is, on the same side as the carboxy terminus as determined previously. By combining proteolysis experiments with data from immunoblotting, we can identify a third cytoplasmic region, a loop of some 4 kD between membrane protected domains. This loop carries an antibody binding site. The protein, if transmembrane, is therefore likely to cross the membrane four times. We have used the same antisera to ascertain if the 43-kD protein is involved in cell-cell communication. The antiserum against the amino terminus blocked dye coupling in 90% of cell pairs tested; the antiserum recognizing epitopes in the cytoplasmic loop and cytoplasmic tail blocked coupling in 75% of cell pairs tested. Preimmune serum and control antibodies (one against MIP and another binding to a cardiac G protein) had no or little effect on dye transfer. Our experimental evidence thus indicates that, in spite of the differences in amino acid sequence, the gap junction proteins in heart and liver share a general organizational plan and that there may be several domains (including the amino terminus) of the molecule that are involved in the control of junctional permeability
Large collectivity in 29Ne at the boundary of the island of inversión
Artículo escrito por un elevado número de autores, solo se referencian el que aparece en primer lugar, los autores pertenecientes a la UAM y el nombre del grupo de colaboración, si lo hubiereThe heavy-ion inelastic scattering of the neutron-rich nucleus 29Ne to its excited states was studied using a 100.1 MeV/u 29Ne rare isotope beam on 181Ta and 9Be targets. The combined setup consisting of the GRETINA array, the TRIPLEX device and the S800 Spectrograph facilitates the simultaneous measurements of the two inelastic reactions, providing the first measurement of the transition strengths for this isotope. A sizable E2 strength B(E2↑) which amounts to 163(30) e2 fm4 was determined in the excitation to the 931-keV state, demonstrating a large degree of collectivity. The present results of B(E2↑) are compared to various shell-model calculations, confirming the role of intruder configurations in 29Ne at the boundary of the island of inversionThe authors would like to thank K. Wimmer for providing us the input for FRESCO calculations and A. Moro for giving access to an unpublished version of the FRESCO code. This work was supported by the U.S. Department of Energy (DOE), Office of Science, Office of Nuclear Physics, under Grant No. DE-SC0020451, the U.S. National Science Foundation (NSF) under Grant No. PHY1565546 (Operation of the NSCL) and PHY2110365, and by the DOE National Nuclear Security Administration through the Nuclear Science and Security Consortium, under Award No. DE-NA0003180. GRETINA was funded by the DOE, Office of Science. Operation of the array at NSCL was supported by DOE under Grants No. DE-SC0019034 (NSCL) and No. DE-AC02-05CH11231 (LBNL). A.P. acknowledges the Grant CEX2020-001007-S funded by MCIN/AEI/10.13039/501100011033 and PGC2018-094583. Y.U. and N.S. acknowledge KAKENHI Grant No. 20K03981 from the Ministry of Education, Culture, Sports, Science and Technology (MEXT), Japan. N.S. acknowledges support from “Program for Promoting Researches on the Supercomputer Fugaku” (JPMXP1020200105, hp210165, and hp220174) by JICFuS and MEXT, Japan. T.M. acknowledges the support by the Croatian Science Foundation under project No. IP-2018-01-125
Análisis histórico-epistemológico de las concepciones de salud desde una perspectiva didáctica : narrando la “historia” de la peste negra medieval
En este trabajo presentamos el caso de la peste negra medieval como insumo para analizar y comparar la potencia didáctica de algunos modelos explicativos de la noción de enfermedad. Comenzamos examinando, desde una perspectiva educativa, algunas de las diferentes concepciones de salud que se han generado a lo largo del tiempo, concepciones que se inscriben en perspectivas uni- o multicausales. Proponemos utilizar la narración de “pequeñas historias” con el propósito de que los y las estudiantes las analicen a partir de diferentes enfoques, de manera que puedan explorar las aportaciones de cada uno de ellos
Review of particle-in-cell modeling for the extraction region of large negative hydrogen ion sources for fusion
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