On exact solutions for quantum particles with spin S= 0, 1/2, 1 and de Sitter event horizon

Exact wave solutions for particles with spin 0, 1/2 and 1 in the static coordinates of the de Sitter space-time model are examined in detail. Firstly, for a scalar particle, two pairs of linearly independent solutions are specified explicitly: running and standing waves. A known algorithm for calculation of the reflection coefficient $R_{\epsilon j}$ on the background of the de Sitter space-time model is analyzed. It is shown that the determination of R_{\epsilon j} requires an additional constrain on quantum numbers \epsilon \rho / \hbar c >> j, where \rho is a curvature radius. When taken into account of this condition, the R_{\epsilon j} vanishes identically. It is claimed that the calculation of the reflection coefficient R_{\epsilon j} is not required at all because there is no barrier in an effective potential curve on the background of the de Sitter space-time. The same conclusion holds for arbitrary particles with higher spins, it is demonstrated explicitly with the help of exact solutions for electromagnetic and Dirac fields.Comment: 30 pages. This paper is an updated and more comprehensive version of the old paper V.M. Red'kov. On Particle penetrating through de Sitter horizon. Minsk (1991) 22 pages Deposited in VINITI 30.09.91, 3842 - B9

PTBP1 promotes hematopoietic stem cell maintenance and red blood cell development by ensuring sufficient availability of ribosomal constituents.

Ribosomopathies constitute a range of disorders associated with defective protein synthesis mainly affecting hematopoietic stem cells (HSCs) and erythroid development. Here, we demonstrate that deletion of poly-pyrimidine-tract-binding protein 1 (PTBP1) in the hematopoietic compartment leads to the development of a ribosomopathy-like condition. Specifically, loss of PTBP1 is associated with decreases in HSC self-renewal, erythroid differentiation, and protein synthesis. Consistent with its function as a splicing regulator, PTBP1 deficiency results in splicing defects in hundreds of genes, and we demonstrate that the up-regulation of a specific isoform of CDC42 partly mimics the protein-synthesis defect associated with loss of PTBP1. Furthermore, PTBP1 deficiency is associated with a marked defect in ribosome biogenesis and a selective reduction in the translation of mRNAs encoding ribosomal proteins. Collectively, this work identifies PTBP1 as a key integrator of ribosomal functions and highlights the broad functional repertoire of RNA-binding proteins