RESUMO
PURPOSE: The relationship between endometrial polyps (EPs), chronic endometritis (CE), hysteroscopic findings, and antimicrobial in infertility patients was determined. METHODS: We retrospectively enrolled 115 infertility patients with suspected EPs who underwent office hysteroscopy. Patients were divided into 3 groups: 38 with increased plasma cells in EPs (group 1); 31 without increased plasma cells in EPs (group 2); and 46 without EPs (group 3). The 3 groups underwent hysteroscopy with or without polypectomies, and immediately thereafter, an endometrial aspiration biopsy (EAB) was performed. CE was diagnosed based on plasma cell infiltration in the non-polypoid endometrium obtained by EAB. RESULTS: The percentage of CE was 68.4%, 32.2%, and 28.3% in groups 1, 2, and 3, respectively. CE was more frequent in group 1 than group 2 or 3 (P = .01 and P = .002, respectively). The number of polyps was higher in group 1 than group 2. After adjustment for age and assisted reproductive technology, antibiotic therapy was not associated with pregnancy (adjusted odds ratio, 0.44; 95% confidence interval, 0.05-3.57) in patients with EPs and CE. CONCLUSIONS: Group 1 was associated with CE, and hysteroscopic findings were different from group 2. Antibiotic therapy after polypectomy for EPs with CE may not always be necessary.
RESUMO
We demonstrate the preferential orders of molecular chaperones glucose-regulated protein 94 (GRP94), binding immunoglobulin protein (BiP), and calreticulin (CRT) in an endoplasmic reticulum (ER) fraction from rat liver using columns conjugated with denatured myoglobin, RNase A, or ß-lactoglobulin as client proteins in the presence or absence of ATP. The results showed that BiP, CRT, and GRP94 preferentially contributed myoglobin, RNase A, and ß-lactoglobulin, respectively, in the presence of ATP. In the absence of ATP, GRP94 and CRT preferentially recognized misfolded myoglobin (α-helix-rich protein), whereas BiP preferentially recognized misfolded RNase A (α-helix/ß-sheet mixed protein) and ß-lactoglobulin (ß-sheet-rich protein). The preferential order of ER chaperones may be dynamically regulated by ER conditions and the higher-order structure of client proteins.