Seismic Reflection and Electrical Resistivity Imaging Support Pre-Quaternary Glaciation in the Rocky Mountains (Unaweep Canyon, Colorado)

Unaweep Canyon (Uncompahgre Plateau, Colorado) represents an enigmatic landscape with a complex evolution. Interpretations for its origin have ranged from ancestral fluvial erosion in the late Cenozoic to glacial erosion in the Paleozoic, or some combination thereof, with significant implications for global climatic and large-scale tectonic reconstructions. To address the conflicting interpretations, we acquired a high-resolution seismic reflection profile to investigate the depth, structure, and sedimentary infill in the canyon. The data set is further complemented with an electrical resistivity survey. Integrated with other geophysical and geological data, the results show an overdeepened Precambrian basement with transverse U shape and support the hypothesis of a pre-Quaternary glacial origin. Our data constitute the first detailed image of a buried pre-Quaternary glacial valley in North America; if substantiated with core studies, these results have far-reaching implications for our understanding of global ice houses as well as the tectonic conditions, enabling preservation of such systems.AGU allows authors to deposit their journal articles if the version is the final published citable version of record, the AGU copyright statement is clearly visible on the posting, and the posting is made 6 months after official publication by the AGU.Acquisition was partly funded through NSF-EAR- 1338331 and NSF- EAR- 1849623.Ye

Glucose induces anion conductance and cytosol-to-membrane transposition of ICln in INS-1E rat insulinoma cells

The metabolic coupling of insulin secretion by pancreatic beta cells is mediated by membrane depolarization due to increased glucose-driven ATP production and closure of K(ATP) channels. Alternative pathways may involve the activation of anion channels by cell swelling upon glucose uptake. In INS-1E insulinoma cells superfusion with an isotonic solution containing 20 mM glucose or a 30% hypotonic solution leads to the activation of a chloride conductance with biophysical and pharmacological properties of anion currents activated in many other cell types during regulatory volume decrease (RVD), i.e. outward rectification, inactivation at positive membrane potentials and block by anion channel inhibitors like NPPB, DIDS, 4-hydroxytamoxifen and extracellular ATP. The current is not inhibited by tolbutamide and remains activated for at least 10 min when reducing the extracellular glucose concentration from 20 mM to 5 mM, but inactivates back to control levels when cells are exposed to a 20% hypertonic extracellular solution containing 20 mM glucose. This chloride current can likewise be induced by 20 mM 3-Omethylglucose, which is taken up but not metabolized by the cells, suggesting that cellular sugar uptake is involved in current activation. Fluorescence resonance energy transfer (FRET) experiments show that chloride current activation by 20 mM glucose and glucose-induced cell swelling are accompanied by a significant, transient redistribution of the membrane associated fraction of ICln, a multifunctional 'connector hub' protein involved in cell volume regulation and generation of RVD currents

A new gene-finding tool: Using the caenorhabditis elegans operons for identifying functional partner-proteins in human cells

Abstract: How can a large number of different phenotypes be generated by a limited number of genotypes? Promiscuity between different, structurally related and/or unrelated proteins seems to provide a plausible explanation to this pertinent question. Strategies able to predict such functional interrelations between different proteins are important to restrict the number of putative candidate proteins, which can then be subjected to time-consuming functional tests. Here we describe the use of the operon structure of the nematode genome to identify partner proteins in human cells. In this work we focus on ion channels proteins, which build an interface between the cell and the outside world and are responsible for a growing number of diseases in humans. However, the proposed strategy for the partner protein quest is not restricted to this scientific area but can be adopted in virtually every field of human biology where protein-protein interactions are assume

Afamin is a novel human vitamin E-binding glycoprotein characterization and in vitro expression.

Hydrophobic vitamins are transported in human plasma and extravascular fluids by carrier proteins. No specific protein has been described so far for vitamin E, which plays a crucial role in protecting against oxidative damage and disease. We report here the purification of a 75-kDa glycoprotein with vitamin E-binding properties by stepwise chromatography of lipoprotein-depleted human plasma and monitoring of vitamin E (alpha-tocopherol)-binding activity. Partial sequencing identified this protein as afamin, a previously described member of the albumin gene family with four or five potential N-glycosylation sites. Glycosylation analysis indicated that >90% of the glycans were sialylated biantennary complex structures. The vitamin E-binding properties were confirmed using recombinantly expressed afamin. Qualitative and quantitative analysis of plasma and extravascular fluids revealed an abundant presence of this protein not only in plasma (59.8+/-13.3 microg/mL) but also in extravascular fluids such as follicular (34.4+/-12.7 microg/mL) and cerebrospinal (0.28+/-0.16 microg/mL) fluids, suggesting potential roles for afamin in fertility and neuroprotection. Afamin is partly (13%) bound to plasma lipoproteins. Afamin and vitamin E concentrations significantly correlate in follicular and cerebrospinal fluids but not in plasma. The vitamin E association of afamin in follicular fluid was directly demonstrated by gel filtration chromatography and immunoprecipitation which complements the in vitro findings for purified native and recombinant afamin