Cross-calibration of atomic pressure sensors and deviation from quantum diffractive collision universality for light particles

The total room-temperature, velocity-averaged cross section for atom-atom and atom-molecule collisions is well approximated by a universal function depending only on the magnitude of the leading order dispersion coefficient, $C_6$. This feature of the total cross section together with the universal function for the energy distribution transferred by glancing angle collisions ($P_{\rm{QDU}6}$) can be used to empirically determine the total collision cross section and realize a self-calibrating, vacuum pressure standard. This was previously validated for Rb+N$_2$ and Rb+Rb collisions. However, the post-collision energy distribution is expected to deviate from $P_{\rm{QDU}6}$ in the limit of small $C_6$ and small reduced mass. Here we observe this deviation experimentally by performing a direct cross-species loss rate comparison between Rb+H$_2$ and Li+H$_2$ and using the \textit{ab initio} value of $\langle \sigma_{\rm{tot}} \, v \rangle_{\rm{Li+H}_2}$. We find a velocity averaged total collision cross section ratio, $R = \langle \sigma_{\rm{tot}} \, v \rangle_{\rm{Li+H}_2} : \langle \sigma_{\rm{tot}} \, v \rangle_{\rm{Rb+H}_2} = 0.83(5)$. Based on an \textit{ab initio} computation of $\langle \sigma_{\rm{tot}} \, v \rangle_{\rm{Li+H}_2} = 3.13(6)\times 10^{-15}$ m$^3$/s, we deduce $\langle \sigma_{\rm{tot}} \, v \rangle_{\rm{Rb+H}_2} = 3.8(2) \times 10^{-15}$ m$^3$/s, in agreement with a Rb+H$_2$ \textit{ab initio} value of $\langle \sigma_{\mathrm{tot}} v \rangle_{\mathrm{Rb+H_2}} = 3.57 \times 10^{-15} \mathrm{m}^3/\mathrm{s}$.By contrast, fitting the Rb+H$_2$ loss rate as a function of trap depth to the universal function we find $\langle \sigma_{\rm{tot}} \, v \rangle_{\rm{Rb+H}_2} = 5.52(9) \times 10^{-15}$ m$^3$/s. Finally, this work demonstrates how to perform a cross-calibration of sensor atoms to extend and enhance the cold atom based pressure sensor.Comment: 14 pages, 9 figure

Differential stromal reprogramming in benign and malignant naturally occurring canine mammary tumours identifies disease-modulating stromal components

While cancer-associated stroma (CAS) in malignant tumours is well described, stromal changes in benign forms of naturally occurring tumours remain poorly characterized. Spontaneous canine mammary carcinomas (mCA) are viewed as excellent models of human mCA. We have recently reported highly conserved stromal reprogramming between canine and human mCA based on transcriptome analysis of laser-capture-microdissected FFPE specimen. To identify stromal changes between benign and malignant mammary tumours, we have analysed matched normal and adenoma-associated stroma (AAS) from 13 canine mammary adenomas and compared them to previous data from 15 canine mCA. Our analyses reveal distinct stromal reprogramming even in small benign tumours. While similarities between AAS and CAS exist, the stromal signature clearly distinguished adenomas from mCA. The distinction between AAS and CAS is further substantiated by differential enrichment in several hallmark signalling pathways as well as differential abundance in cellular composition. Finally, we identify COL11A1, VIT, CD74, HLA-DRA, STRA6, IGFBP4, PIGR, and TNIP1 as strongly discriminatory stromal genes between adenoma and mCA, and demonstrate their prognostic value for human breast cancer. Given the relevance of canine CAS as a model for the human disease, our approach identifies disease-modulating stromal components with implications for both human and canine breast cancer

Plant-Type Trehalose Synthetic Pathway in Cryptosporidium and Some Other Apicomplexans

The trehalose synthetic pathway is present in bacteria, fungi, plants and invertebrate animals, but is absent in vertebrates. This disaccharide mainly functions as a stress protectant against desiccation, heat, cold and oxidation. Genes involved in trehalose synthesis have been observed in apicomplexan parasites, but little was known about these enzymes. Study on trehalose synthesis in apicomplexans would not only shed new light into the evolution of this pathway, but also provide data for exploring this pathway as novel drug target.We have observed the presence of the trehalose synthetic pathway in Cryptosporidium and other apicomplexans and alveolates. Two key enzymes (trehalose 6-phosphate synthase [T6PS; EC 2.4.1.15] and trehalose phosphatase [TPase; EC 3.1.3.12] are present as Class II bifunctional proteins (T6PS-TPase) in the majority of apicomplexans with the exception of Plasmodium species. The enzyme for synthesizing the precursor (UDP-glucose) is homologous to dual-substrate UDP-galactose/glucose pyrophosphorylases (UGGPases), rather than the "classic" UDP-glucose pyrophosphorylase (UGPase). Phylogenetic recontructions indicate that both T6PS-TPases and UGGPases in apicomplexans and other alveolates are evolutionarily affiliated with stramenopiles and plants. The expression level of T6PS-TPase in C. parvum is highly elevated in the late intracellular developmental stage prior to or during the production of oocysts, implying that trehalose may be important in oocysts as a protectant against environmental stresses. Finally, trehalose has been detected in C. parvum oocysts, thus confirming the trehalose synthetic activity in this parasite.A trehalose synthetic pathway is described in the majority of apicomplexan parasites including Cryptosporidium and the presence of trehalose was confirmed in the C. parvum oocyst. Key enzymes in the pathway (i.e., T6PS-TPase and UGGPase) are plant-type and absent in humans and animals, and may potentially serve as novel drug targets in the apicomplexans