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1.
Eur J Obstet Gynecol Reprod Biol ; 295: 118-123, 2024 Apr.
Article in English | MEDLINE | ID: mdl-38354603

ABSTRACT

OBJECTIVES: To assess the prevalence and risk factors for premalignancy and malignancy in endometrial polyps and to evaluate trends over the past decade. STUDY DESIGN: This was a retrospective study of patients who underwent hysteroscopic polypectomy at Inha University Hospital, South Korea between January 2013 and June 2023. The demographic and clinical characteristics of the patients reviewed to identify risk factors for premalignancy and malignancy in endometrial polyps included the following: age, parity, body mass index, menopausal status, abnormal uterine bleeding symptoms, diabetes mellitus, hypertension, polycystic ovarian syndrome, use of menopausal hormonal therapy or oral contraceptives, tamoxifen treatment in patients with breast cancer, and the number of polyps. RESULTS: In total, 725 patients were enrolled, among whom 52 (7.2 %) had premalignant and malignant lesions. In logistic regression analysis, menopause (OR: 8.37, 95 % CI [3.33-21.04]), abnormal uterine bleeding (OR: 7.42, 95 % CI [2.13-25.86]), obesity (OR: 3.22, 95 % CI [1.53-6.77]), multiple polyps (OR: 2.86, 95 % CI [1.39-5.88]) and nulliparity (OR: 2.64, 95 % CI [1.13-6.19]) were significantly associated with premalignancy and malignancy in polyps. Annual trends during the study period showed an increase in the number of patients with three of the five risk factors (obesity, multiple polyps, and nulliparity) and an increase in the prevalence of premalignancy and malignancy in polyps. CONCLUSIONS: Menopause, abnormal uterine bleeding, obesity, multiple polyps, and nulliparity increase the risk of premalignancy and malignancy in endometrial polyps. The prevalence of premalignant and malignant polyps has been increasing over the past decade. The risk factors that have contributed to this trend were obesity, nulliparity, and multiple polyps.


Subject(s)
Endometrial Neoplasms , Polyps , Precancerous Conditions , Uterine Diseases , Uterine Neoplasms , Pregnancy , Humans , Female , Retrospective Studies , Endometrial Neoplasms/pathology , Postmenopause , Hysteroscopy , Uterine Neoplasms/pathology , Uterine Diseases/complications , Risk Factors , Precancerous Conditions/epidemiology , Precancerous Conditions/pathology , Obesity/complications , Obesity/epidemiology , Polyps/complications , Uterine Hemorrhage/etiology , Uterine Hemorrhage/complications
2.
Front Immunol ; 12: 778829, 2021.
Article in English | MEDLINE | ID: mdl-34868052

ABSTRACT

Since the coronavirus disease outbreak in 2019, several antibody therapeutics have been developed to treat severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infections. Antibody therapeutics are effective in neutralizing the virus and reducing hospitalization in patients with mild and moderate infections. These therapeutics target the spike protein of SARS-CoV-2; however, emerging mutations in this protein reduce their efficiency. In this study, we developed a universal SARS-CoV-2 neutralizing antibody. We generated a humanized monoclonal antibody, MG1141A, against the receptor-binding domain of the spike protein through traditional mouse immunization. We confirmed that MG1141A could effectively neutralize live viruses, with an EC50 of 92 pM, and that it exhibited effective Fc-mediated functions. Additionally, it retained its neutralizing activity against the alpha (UK), beta (South Africa), and gamma (Brazil) variants of SARS-CoV-2. Taken together, our study contributes to the development of a novel antibody therapeutic approach, which can effectively combat emerging SARS-CoV-2 mutations.


Subject(s)
Antibodies, Monoclonal/immunology , Antibodies, Neutralizing/immunology , Antibodies, Viral/immunology , COVID-19/therapy , SARS-CoV-2/immunology , Animals , Antibodies, Monoclonal/therapeutic use , Antibodies, Neutralizing/therapeutic use , Antibodies, Viral/therapeutic use , Antibody Affinity , Complementarity Determining Regions/chemistry , Epitopes , Humans , Immunization , Mice , Molecular Docking Simulation , Protein Interaction Domains and Motifs , Receptors, IgG/immunology , Spike Glycoprotein, Coronavirus/chemistry , Spike Glycoprotein, Coronavirus/genetics , Spike Glycoprotein, Coronavirus/immunology
3.
Arch Gynecol Obstet ; 301(4): 949-954, 2020 04.
Article in English | MEDLINE | ID: mdl-32144571

ABSTRACT

PURPOSE: Progesterone receptor membrane component 1 (PGRMC1) have anti-inflammatory and anti-apoptotic properties. This study aimed to determine the expression of PGRMC1 in fetal membranes among women with preterm labor (PTL), preterm premature rupture of membranes (PPROM), and acute histologic chorioamnionitis (HCA) during preterm birth. METHODS: Full thickness fetal membranes were obtained from women with gestational age-matched (32-34 weeks of gestational age), and categorized as PTL without HCA (PTL, n = 10), PPROM without HCA (PPROM, n = 10), PPROM with HCA (HCA, n = 10), and term without labor and HCA (term birth (TB), n = 9). The expression of PGRMC1 was assessed using western blot and Immunohistochemistry (IHC). As CD14 is a component of the innate immune system during inflammation, CD14 was used as inflammatory indicator. Nonparametric statistics were used for analysis. RESULTS: PGRMC1 expression for all of preterm birth was lower than in TB (P = 0.01). In HCA, PGRMC1 expression was significantly decreased compared to that in PTL and PPROM (P = 0.006. P = 0.001, respectively). PGRMC1 expression in PPROM was higher than that in PTL (P = 0.002). There was a negative correlation between PGRMC1 and CD 14/ß-actin ratio (r = - 0.518; P = 0.002). IHC showed that PGRMC1 was predominant in the cytoplasm of cells, these results were consistent with those of the western blot analysis. CONCLUSION: Preterm birth with PTL, PPROM, and especially HCA is associated with a decreased PGRMC1 in fetal membranes and inversely associated with increased CD 14.


Subject(s)
Chorioamnionitis/physiopathology , Premature Birth/physiopathology , Receptors, Progesterone/metabolism , Adult , Female , Humans , Infant, Newborn , Pregnancy , Young Adult
4.
Biochem Biophys Res Commun ; 501(3): 718-723, 2018 06 27.
Article in English | MEDLINE | ID: mdl-29753735

ABSTRACT

Pep27 from Streptococcus pneumoniae is reported to initiate pneumococcal autolysis, thereby constituting a major virulence factor. Although a few antisera recognizing Pep27 have been reported, no monoclonal, well-characterized antibody for Pep27 has been developed. Here we screened two single-chain antibody variable fragments (scFv) using a phage display from a large human synthetic scFv library to select clones E2 and F9. Dissociation constants (Kd) of E2 and F9 were 1.1 µM and 0.50 µM, respectively. E2 and F9 did not cross-react with other pneumococcal and unrelated proteins. The epitopes of Pep27 were localized to residues 24, 26 and 27 by alanine scanning. Molecular docking analysis supported the experimentally investigated epitope. The E2 and F9 clones specifically detected Pep27 in an environment mimicking in vivo conditions, demonstrated in human serum. The scFv clones characterized here represent molecular tools for the detection of pneumococcal diseases with potential for further improvement in affinity.


Subject(s)
Antibodies, Monoclonal/immunology , Peptides/immunology , Pneumococcal Infections/immunology , Single-Chain Antibodies/immunology , Streptococcus pneumoniae/immunology , Virulence Factors/immunology , Amino Acid Sequence , Antibodies, Monoclonal/chemistry , Antibody Affinity , Epitope Mapping , Epitopes/chemistry , Epitopes/immunology , Humans , Molecular Docking Simulation , Peptide Library , Peptides/chemistry , Single-Chain Antibodies/chemistry , Streptococcus pneumoniae/chemistry , Virulence Factors/chemistry
5.
Biochem Biophys Res Commun ; 482(1): 141-146, 2017 Jan 01.
Article in English | MEDLINE | ID: mdl-27845043

ABSTRACT

Streptococcus pneumoniae is a major infectious agent responsible for pneumonia, otitis media, sepsis and meningitis. Pneumococcal surface protein A (PspA) is a well-characterized virulence factor localized on the surface and a target for vaccine development. In this study, we screened a single-chain antibody variable fragment (scFv) using phage display from a human synthetic library to select a clone 2B11. Affinity (Kd) of 2B11 was measured to be 5 nM using biolayer interferometry. 2B11 exhibited a dose-dependent recognition of recombinant PspA with no cross-reactivity towards pneumococcal antigens. The epitope on PspA was defined to residues 231-242 by mutational analysis. Molecular docking analysis supported the experimentally determined epitope, suggesting that the helix spanning residues 231-242 can bind to 2B11 with residues in the CDR-H3 (complementarity determining region 3 in the heavy chain) actively participating in the molecular contacts. Comparison of 2B11 with a commercial PspA antibody revealed that 2B11 exhibited a better specificity towards recombinant PspA antigen. 2B11 was capable of detecting endogenous PspA from pneumococcal lysates with affinity similar to that of the commercial antibody. Our study provides a molecular tool for biosensors detecting pneumococcal diseases.


Subject(s)
Bacterial Proteins/chemistry , Bacterial Proteins/immunology , Single-Chain Antibodies/chemistry , Single-Chain Antibodies/immunology , Streptococcus pneumoniae/immunology , Bacterial Proteins/isolation & purification , Binding Sites , Biosensing Techniques , Immunoassay , Molecular Docking Simulation , Protein Binding , Single-Chain Antibodies/isolation & purification , Streptococcus pneumoniae/chemistry
6.
Aesthetic Plast Surg ; 36(1): 207-12, 2012 Feb.
Article in English | MEDLINE | ID: mdl-21701946

ABSTRACT

BACKGROUND: We report on a case of leakage and migration to the upper abdomen of an unknown injected material that was used for breast augmentation. It was revealed to be prolamin by Fourier transform infrared (FTIR) analysis and pyrolysis gas chromatography/mass spectrometry (PY-GC/MS). METHODS: A 35-year-old woman who had undergone mammary augmentation by transaxillary injection 8 years previously presented with a decreased size of her left breast and a palpable mass in the left upper quadrant (LUQ). Mammogram and ultrasonography showed multiple dense masses and several hypoechoic areas, respectively. Abdominal ultrasound showed a hypoechoic lesion between the subcutaneous layer and the abdominal wall muscles. When the left breast and the lump in the LUQ were explored, 90 and 160 cc of yellow, sticky, granular gel gushed out. FTIR analysis and PY-GC/MS were used to investigate the component of the removed gel. RESULTS: When this gel was analyzed by FTIR with the transmittance mode, intensity bands appeared at 3295.2 (NH2), 2927.2 (CH), 1650 (C=C), 1544.6 (C-C), and 1403.1 (C-N) cm(-1). The result showed a 93.84% match with purified zein, a 91.19% match with zein from corn, and a 90.27% match with poly(N-methyl acrylamide). FTIR with the attenuated total reflectance (ATR) mode revealed that the gel matched with wheat gluten flour. Based on the result of PY-GC/MS, the gel was suspected to be protein. CONCLUSION: This is the first such report on performing chemical analysis of a leaked injected gel from human breast implantation. The removed gel from the breast augmentation was revealed to be prolamin, which is a cereal seed storage protein. We think FTIR might be a useful tool for analyzing and confirming extracted materials that were previously injected to the body.


Subject(s)
Breast Implantation/adverse effects , Foreign-Body Migration/etiology , Hydrogel, Polyethylene Glycol Dimethacrylate/adverse effects , Hydrogel, Polyethylene Glycol Dimethacrylate/chemistry , Zein/analysis , Adult , Female , Gas Chromatography-Mass Spectrometry , Humans , Spectroscopy, Fourier Transform Infrared
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