This study was aimed to explore the value of quantitative proton MR spectroscopy (1H-MRS) in the differentiation of benign and malignant meningioma. 23 cases, including 19 benign (grade I) and 4 malignant (grade II-III) meningiomas, underwent single voxel 1H-MRS (TR/TE = 2000 ms/68, 136, 272 ms). T2 relaxation time of tissue water and choline were estimated by an exponential decay model. Choline concentration was calculated using tissue water as the internal reference, and corrected according to intra-voxel cystic/necrotic parts. Tissue water T2 of benign and malignant meningiomas were (105 +/- 41) ms and (151 +/- 42) ms, respectively. The difference was statistically significant (P = 0.033). While Choline T2 of benign and malignant meningiomas were (242 +/- 73) ms and (316 +/- 102) ms respectively, the difference was not significant (P = 0.105). Choline concentration was (2.86 +/- 0.86) mmol/ kg wet weight in benign meningiomas and (3.53 +/- 0.60) mmol/kg wet weight in malignant ones; after correction they increased to (2.98 +/- 0.93)mmol/kg wet weight and (4.58 +/- 1.22) mmol/kg wet weight, respectively, and the difference was significant (P = 0.019). In conclusion, quantitative 1H-MRS is useful for the differentiation of benign and malignant meningioma by T2 relaxation time and absolute choline concentration.
Adult ; Aged ; Choline ; metabolism ; Diagnosis, Differential ; Female ; Humans ; Magnetic Resonance Spectroscopy ; methods ; Male ; Meningeal Neoplasms ; diagnosis ; metabolism ; pathology ; Meningioma ; diagnosis ; metabolism ; pathology ; Middle Aged ; Protons ; Young Adult

Glycosylation of the Fc region of IgG has a profound impact on the safety and clinical efficacy of therapeutic antibodies. While the biantennary complex-type oligosaccharide attached to Asn297 of the Fc is essential for antibody effector functions, fucose and outer-arm sugars attached to the core heptasaccharide that generate structural heterogeneity (glycoforms) exhibit unique biological activities. Hence, efficient and quantitative glycan analysis techniques have been increasingly important for the development and quality control of therapeutic antibodies, and glycan profiles of the Fc are recognized as critical quality attributes. In the past decade our understanding of the influence of glycosylation on the structure/function of IgG-Fc has grown rapidly through X-ray crystallographic and nuclear magnetic resonance studies, which provides possibilities for the design of novel antibody therapeutics. Furthermore, the chemoenzymatic glycoengineering approach using endoglycosidase-based glycosynthases may facilitate the development of homogeneous IgG glycoforms with desirable functionality as next-generation therapeutic antibodies. Thus, the Fc glycans are fertile ground for the improvement of the safety, functionality, and efficacy of therapeutic IgG antibodies in the era of precision medicine.
Animals ; Antibodies, Monoclonal ; adverse effects ; pharmacokinetics ; therapeutic use ; Glycosylation ; Humans ; Immunoglobulin G ; chemistry ; metabolism ; Protein Engineering ; methods ; Receptors, Fc ; chemistry ; metabolism ; Treatment Outcome