Pituitary adenomas are the most common tumors of the sellar region, but the occurrence of spherical amyloid deposits in a pituitary adenoma is rare. We describe the clinical features, radiologic characteristics, and pathologic findings of 45-year-old man who presented with galactorrhea, hypogonadism, and hyperprolactinemia who had a pituitary adenoma with extensive spherical amyloid deposits. Approximately 30 cases have been reported, almost exclusively in patients with prolactinomas. Treatment with dopaminergic agonists will result in the expected reduction in prolactin levels; however, in most cases, macroadenomas with spherical amyloid deposits fail to decrease in size. The source of the amyloid deposits in prolactinomas is not clearly defined but may be due to abnormal processing of prolactin or its prohormone. These adenomas with spherical amyloid have a characteristic appearance on magnetic resonance imaging with low or heterogeneous intensity on T1 and low intensity on T2-weighted images. Following infusion of gadolinium, there is enhancement of the periphery but not most of the tumor mass. These magnetic resonance imaging characteristics are different than those of typical pituitary adenomas. These differences should alert clinicians to the possibility of extensive spherical amyloid deposits in a prolactin-secreting pituitary adenoma, which may have important clinical implications. In this report, we correlate the radiologic finds with the pathology and compared them with other sellar and parasellar lesions.
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http://dx.doi.org/10.1016/j.anndiagpath.2013.03.001 | DOI Listing |
J Phys Chem B
January 2025
Department of Chemistry, North-Eastern Hill University, Shillong 793 022, India.
The interaction of protein with nanoparticles (NPs) of varying shape and/or size boosts our understanding on their bioreactivity and establishes a comprehensive database for use in medicine, diagnosis, and therapeutic applications. The present study explores the interaction between lysozyme (LYZ) and different NPs like graphene oxide (GO) and zinc oxide (ZnO) having various shapes (spherical, 's', and rod-shaped, 'r') and sizes, focusing on their binding dynamics and subsequent effects on both the protein fibrillation and antimicrobial properties. Typically, GO is considered a promising medium due to its apparent inhibition and prolonged lag phase for LYZ fibrillation.
View Article and Find Full Text PDFACS Appl Mater Interfaces
January 2025
School of Chemical and Biological Engineering, Institute of Engineering Research, College of Engineering, Seoul National University, Seoul 08826, Republic of Korea.
Stable hollow-type microspheres (MSs) have been fabricated using α-synuclein (αS), an amyloidogenic protein, via freeze-induced protein self-assembly. This assembly process involves three steps: rapid freezing to form spherical protein condensates from αS oligomers, frozen annealing to form a crust on the condensate and freeze-drying to create an interior lumen via the three-dimensional (3D) coffee-stain effect. The crust produced during the frozen-annealing step is a β-sheet-mediated protein structure that is presumed to be created at the quasi-liquid layer of the protein-ice interface and thus contributes to the stability of MSs in aqueous solutions at room temperature without any additional surface stabilization.
View Article and Find Full Text PDFACS Chem Neurosci
December 2024
Centre for Nano and Material Science, Jain University, Jain Global Campus, Bengaluru 562112, Karnataka India.
Nanoconjugates are promising for therapeutic drug delivery and targeted applications due to the numerous opportunities to functionalize their surface. The present study reports the synthesis of 5-fluorouracil (5-FU)-entrapped polyvinylpyrrolidone (PVP) nanoconjugates, precisely 5-FU-PVP and 5-FU-PVP-Au, and the evaluation of protein aggregation inhibition efficiency. The 5-FU-loaded polymer nanoconjugates were functionalized with gold nanoparticles and analyzed using characterization techniques like dynamic light scattering, UV-visible spectroscopy, Fourier-transform infrared spectroscopy, and zeta potential analysis.
View Article and Find Full Text PDFLangmuir
December 2024
Department of Chemistry, Laboratory of Peptide and Amyloid Research, Indian Institute of Technology Guwahati, Guwahati 781039, Assam, India.
Peptides possess a remarkable propensity to adopt distinct morphologies, ranging from simple aggregates to complex structures such as fibrils and nanotubes. Morphology transformation in peptides is intricately linked to the physicochemical properties of peptides and external factors such as pH, temperature, and solvent conditions. Thus, it is more complex.
View Article and Find Full Text PDFAdv Mater
November 2024
State Key Laboratory of Drug Research & Center of Pharmaceutics, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, China.
Filamentous structures exert biological functions mediated by multivalent interactions with their counterparts in sharp contrast with spherical ones. The physicochemical properties and unique behaviors of nanofilaments that are associated with multivalent interaction with protein are poorly understood. Here, peptide-based nanofilaments containing different homotetrapeptidic inserts are reported and their protein adsorption and biological fates are tested.
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