25 research outputs found
Secretion of Novel SEL1L Endogenous Variants Is Promoted by ER Stress/UPR via Endosomes and Shed Vesicles in Human Cancer Cells
We describe here two novel endogenous variants of the human endoplasmic reticulum (ER) cargo receptor SEL1LA, designated p38 and p28. Biochemical and RNA interference studies in tumorigenic and non-tumorigenic cells indicate that p38 and p28 are N-terminal, ER-anchorless and more stable relative to the canonical transmembrane SEL1LA. P38 is expressed and constitutively secreted, with increase after ER stress, in the KMS11 myeloma line and in the breast cancer lines MCF7 and SKBr3, but not in the non-tumorigenic breast epithelial MCF10A line. P28 is detected only in the poorly differentiated SKBr3 cell line, where it is secreted after ER stress. Consistently with the presence of p38 and p28 in culture media, morphological studies of SKBr3 and KMS11 cells detect N-terminal SEL1L immunolabeling in secretory/degradative compartments and extracellularly-released membrane vesicles. Our findings suggest that the two new SEL1L variants are engaged in endosomal trafficking and secretion via vesicles, which could contribute to relieve ER stress in tumorigenic cells. P38 and p28 could therefore be relevant as diagnostic markers and/or therapeutic targets in cancer
Study of in the vicinity of
Using 2917 of data accumulated at 3.773~,
44.5~ of data accumulated at 3.65~ and data accumulated
during a line-shape scan with the BESIII detector, the reaction
is studied considering a possible interference
between resonant and continuum amplitudes. The cross section of
,
, is found to have two
solutions, determined to be () pb with the phase angle
(0.11 pb at the 90% confidence level),
or ) pb with both of which
agree with a destructive interference. Using the obtained cross section of
, the cross section of , which is useful information for the future PANDA experiment, is
estimated to be either () nb ( nb at 90% C.L.) or
nb