Related Experiment Video
Updated: Jul 7, 2026
09:31
Orthotopic Implantation and Peripheral Immune Cell Monitoring in the II-45 Syngeneic Rat Mesothelioma Model
Published on: October 2, 2015
Pediatric localized amyloidosis in mesopharynx
Masahiro Takahashi1, Hideki Matsuda, Keiko Ito
1Department of Otolaryngology, Yokohama City University, 3-9 Fukuura, Kanazawa-ku, Yokohama, Japan. masahir@qd5.so-net.ne.jp
International Journal of Pediatric Otorhinolaryngology
|October 24, 2002
Summary
This study reports a rare case of primary localized amyloidosis in a 12-year-old girl, the third pediatric case documented. The pharyngeal mass showed no change over 24 months without treatment.
Area of Science:
- Otorhinolaryngology
- Pathology
- Immunohistochemistry
Background:
- Primary localized amyloidosis is a rare condition.
- Amyloidosis of the mesopharynx is exceptionally rare, particularly in pediatric patients.
Observation:
- A 12-year-old girl presented with a pharyngeal mass detected during a school health examination.
- Physical examination identified a mass within the faucial tonsil.
- Histological examination revealed amyloid deposition and chronic inflammatory cell infiltration.
Findings:
- Immunohistochemical analysis confirmed the amyloid deposit was positive for amyloid P component (AP) and negative for amyloid L (AL).
- The mesopharyngeal mass remained unchanged over a 24-month observation period without any intervention.
- The patient was asymptomatic, and no treatment was administered.
Implications:
- This case contributes to the limited literature on pediatric mesopharyngeal amyloidosis.
- The findings highlight the potential for asymptomatic presentation and stability of amyloid P component-positive amyloidosis in the mesopharynx.
- Further research may elucidate the specific mechanisms and long-term behavior of this rare condition in children.
Related Concept Videos
03:03Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
01:22Lysosomal Hydrolases
Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
03:03Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
01:27Esophageal Achalasia
Esophageal achalasia is a chronic neurogenic disorder characterized by impaired relaxation of the lower esophageal sphincter (LES) and absent or ineffective peristalsis in the distal esophagus. This leads to a functional obstruction without a physical blockage, despite significant disruption of esophageal motility.EtiologyAchalasia is caused by degeneration of the myenteric (Auerbach's) plexus, specifically the loss of inhibitory ganglion cells that produce vasoactive intestinal peptide (VIP)...