Earlier studies have suggested that indoleamine 2,3-dioxygenase (IDO) has a wide tissue distribution in mammals. However, detailed information on its cellular localization and also the levels of expression in various tissues is still scarce. In the present study, we sought to determine the cellular localization of IDO and also to quantify the level of its expression in various mouse tissues by using the branched DNA signal amplification assay, Western blotting, and immunohistochemical staining. The highest levels of constitutive IDO expression were found to be selectively present in the caput of epididymis, except for its initial segment. IDO expression was also detected inside the luminal compartment and even in the stereocilia within this region. In the prostate, high levels of IDO were selectively expressed in the capsular cells. In addition, high levels of IDO expression were also selectively detected in certain types of cells in the placenta, spleen, thymus, lung, and digestive tract. Notably, the morphological features of most of the positively stained cells in these organs closely resembled those of antigen-presenting cells. Based on the tissue distribution and cellular localization characteristics of IDO, it is hypothesized that its expression may serve two main functions: one is to deplete tryptophan in an enclosed microenvironment (such as in the epididymal duct lumen) to prevent bacterial or viral infection, and the other is to produce bioactive tryptophan catabolites that would serve to suppress T-cell-mediated immune responses against self-antigens, fetal antigens, or allogeneic antigens, in different situations.
ObjectiveThis study was performed to assess the efficacy and outcome of endovascular
aneurysm repair (EVAR) for treatment of primary mycotic aortic aneurysms
(PMAAs).MethodsFourteen consecutive patients who presented with PMAA from April 2010 to July
2017 were retrospectively reviewed. Preoperative, intraoperative, and
postoperative clinical data were recorded, and late infection-related
complications and long-term survival were assessed.ResultsThe aneurysms were located in the abdominal aorta in 10 patients and in the
left common iliac artery in 4 patients. Positive microbial cultures were
found in 12 patients, including Salmonella species in 11
and Streptococcus in 1. The remaining two patients had
negative culture results. Ten patients received preoperative antibiotics
before elective EVAR for 7 ± 9 days after admission. Four patients who
underwent emergent EVAR due to ruptured aneurysms were given their first
dose of antibiotics before EVAR. Three patients underwent surgical drainage,
and six underwent percutaneous drainage within 30 days after EVAR. No death
occurred within 30 days of the initial procedure. The mean follow-up was
34.8 (range, 3–84 months). One patient underwent re-intervention to resolve
obstruction of the iliac/femoral artery 5 months postoperatively. Relapse of
infection occurred in six patients (42.8%) during follow-up;
infection-related death occurred in three of these patients. The other
patients recovered with either conversion to open radical surgery or medical
therapy. The actuarial 7-year survival after EVAR was 75.7%.ConclusionsEVAR and aggressive antibiotic therapy might be suitable for PMAAs. Favorable
results may be typical for infection caused by
Salmonella.
fTEVAR using PMSGs may be a viable alternative for patients who present with ABAD without healthy proximal landing zones and who are unable to wait for a custom made fenestrated device.
Members of the protein disulfide isomerase (PDI) family play a critical role in catalyzing the formation of disulfide bonds in secretory proteins, and most of these enzymes have a wide tissue distribution. However, the pancreas-specific PDI homolog was previously suggested to be exclusively expressed in the pancreas (thus commonly referred to as PDIp). In the present study, we found that PDIp was also highly expressed in several other tissues in mice, including the stomach, cecum, ileum, adrenal glands, epididymis, and prostate. Notably, in the digestive organs, such as the stomach and pancreas, very high levels of PDIp were selectively expressed in the digestive enzyme-secreting cells (e.g., gastric chief cells and pancreatic acinar cells). This observation suggests that PDIp may function as a protein-folding catalyst for secretory digestive enzymes. In ileum, PDIp was exclusively expressed in Paneth cells. In addition, high levels of PDIp expression were also detected in normal human pancreas, but its expression was mostly absent in human pancreatic duct adenocarcinoma and pancreatic cancer cell lines. The absence of PDIp expression in pancreatic adenocarcinoma may serve as an additional biomarker for pancreatic cancer.
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