Non-linear relationship between basal serum albumin concentration and cardiac arrest in critically ill patients with end-stage renal disease: a cross-sectional study.

OBJECTIVES: The aim of our study was to investigate the association between serum albumin concentration and the risk of cardiac arrest in critically ill patients with end-stage renal disease in the intensive care unit (ICU). DESIGN: This was a secondary analysis. SETTING: The Phillip electronic-ICU collaborative database from 2014 to 2015. PARTICIPANTS: This study included 4990 critically ill patients diagnosed with end-stage renal disease. PRIMARY AND SECONDARY OUTCOME MEASURES: The exposure of interest was serum albumin concentration. The outcome variable was cardiac arrest. RESULTS: A non-linear relationship was observed between serum albumin concentration and risk of cardiac arrest, with an inflection point of 3.26 g/dL after adjusting for potential confounders. The effect sizes and the CIs on the left and right sides of the inflection point were 0.88 (0.65 to 1.19) and 0.32 (0.16 to 0.64), respectively. CONCLUSIONS: Within an albumin range of 3.26-5.6 g/dL, each 1 g/dL increase in serum levels is associated with a 68% decrease of the risk of cardiac arrest in critically ill patients with end-stage renal disease.

Food digestion by cathepsin L and digestion-related rapid cell differentiation in shrimp hepatopancreas.

Cathepsin L (CatL) has been readily localized in the large vacuole and in the apical complex of the digestive B-cell of the shrimp hepatopancreas. Immunogold technique revealed the occurrence of CatL in zymogen granule, digestive body and digestive vacuole of the B-cell in the hepatopancreas of Metapenaeus ensis. Coalescences of zymogen granule with sub-apical vacuole, and of two small digestive bodies were observed. This progressive coalescence of CatL vesicles is direct evidence of involvement of CatL in intracellular digestion. Released CatL vesicles and free CatL were found in the lumen of hepatopancreatic tubule. CatL mRNA existed in F-cell, but not in the mature B-cell. This finding supports the previous suggestion that F-cell is the precursor of B-cell. F-cell is a transient form. Transition from F-cell to B-cell is fast. We define F-cell as the transcribing cell, F/B-cell as the enzyme-synthesizing cell and B-cell as the enzyme-secreting cell. For the first time, we suggest that R-cell is the replacing cell for the leaving B-cell. CatL degrades nutrient intracellularly and extracellularly. The most interesting finding is that CatL is transcribed in one type of cell, and the very cell evolves quickly to a morphologically different cell where the enzyme functions.

Complete, precise, and innocuous loss of multiple introns in the currently intronless, active cathepsin L-like genes, and inference from this event.

Retrotransposition typically generates pseudogenes. Here we demonstrate a different fate of the retro-processed genes through a novel mechanism in which the retro-processed genes still maintain their sequence intactness and the original functions. We show that the shrimp cathepsin L (CatL) gene MeCatL has lost all of its five introns. Also, ProEPB, the ancestor of the CatL-like barley EPBs and rice REP1, has lost all of its three introns. The multiple introns in a gene might have been eliminated simultaneously and precisely at the original locus for the CatL-like genes of shrimp, barley, rice, Drosophila, and Theileria. We reason that retrotransposition is not responsible for the generation of a processed active intronless (PAI) gene when the gene product retains its sequence intactness and its original function. We propose that double-strand-break repair (DSBR) machinery might play a role in cDNA-mediated homologous recombination (cDMHR) that causes the loss of introns. The cDMHR/DSBR pathway is probably a fundamental mechanism for intron loss in PAI genes and in some asymmetric-intron genes.

Shrimp cathepsin L encoded by an intronless gene has predominant expression in hepatopancreas, and occurs in the nucleus of oocyte.

We have cloned the cDNA and genomic DNA of an active intronless cathepsin L from Metapenaeus ensis. The encoded enzyme has the shortest prosequence among cathepsin L subgroup. It was predominantly expressed in hepatopancreas with an expression level of at least 10 times higher than in any other tissues. It also has expression in stomach, intestine, eye, testis, ovary and muscle. Western blots visualized the mature enzyme in hepatopancreas and a procathepsin L in ovary, intestine and stomach. Metapenaeus cathepsin L (MeCatL) is localized in the large digestive vacuole of the digestive B cell of hepatopancreas. MeCatL has a role in food digestion. An interesting finding is that it exists in the nucleus of oocyte. MeCatL might have a specified physiological role in the nucleus of oocyte. MeCatL might also have a house-keeping function as is suggested for mammalian cathepsin L.