Humans ; Amyloidosis/pathology*

Adult ; Amyloidosis ; diagnosis ; pathology ; Female ; Humans ; Liver Diseases ; diagnosis ; pathology

Aged ; Amyloidosis ; pathology ; Humans ; Immunohistochemistry ; Male ; Middle Aged ; Tongue ; pathology

Aged ; Amyloidosis ; diagnosis ; pathology ; Humans ; Kidney Pelvis ; pathology ; Male ; Ureter ; pathology ; Urinary Bladder ; pathology

Amyloidosis is a heterogeneous group of diseases caused by deposition of misfolded proteins, which usually leads to organ dysfunction. Accurate typing of amyloid deposits is of paramount importance because organ involvements and disease prognosis differ widely among different subtypes, and its treatments are type specific. Correct identification of amyloidogenic protein is crucial to proper treatment. Traditional antibody-based diagnostic methods such as immunohistochemistry and immunofluorescence are helpful in amyloid typing, but limitations of those approaches including antibody availability and serum protein contamination impair sensitivity and specificity of diagnosis. Sometimes misdiagnosis can lead to catastrophic therapeutic outcome. Genetic testing is important to confirm the diagnosis of hereditary amyloidosis. Nowadays proteomic analysis has been used as an advanced strategy for amyloid typing and the gold-standard today is laser microdissection followed by mass spectrometry (LMD/MS), which can identify causal protein without additional clinical information. Furthermore, LMD/MS is performed on formalin-fixed paraffin-embedded (FFPE) specimens, thus large scale retrospective studies based on archival material can be conducted. In recent studies, LMD/MS has been proven superior to traditional methods without the drawbacks mentioned above. This proteomic approach provides guarantee of appropriate clinical management and probability of new insights into the mechanism of amyloidosis.In this article the new advances of studies on subtyping of systemic amyloidosis are reviewed.
Amyloidosis ; classification ; pathology ; Humans ; Immunoglobulin Light-chain Amyloidosis ; Laser Capture Microdissection ; Mass Spectrometry ; Plasma Cells ; Proteomics ; methods

OBJECTIVE: To analyze the clinical features and treatment protocols of primary laryngeal amyloidosis. METHOD: Retrospective study of 5 patient hospitalized from 1996 - 2011. All of the patients by resection lesions, including four routine throat tumor resection, and burst throat by supporting laryngoscope in 1 case, all did not give lesions resection radiation and hormone therapy. RESULT: All the 5 patients recovered clinically. There were 3 patients followed up for 0.3-7.5 years with a mean time of 3.3 years without recurrence, 2 patients lost follow-up. CONCLUSION Middle ages seemed to be more vulnerable. The most common disease region is true vocal cord, followed by false vocal cord, epiglottis former clearance etc. Early surgical treatment of this disease is the most important treatment, larynx endoscopic and CT for the diagnosis of great value, and pathologic biopsy especially Congo red stain positive is the basis of the specific diagnosis of this disease.
Age Factors ; Amyloidosis ; pathology ; surgery ; Biopsy ; Humans ; Immunoglobulin Light-chain Amyloidosis ; Laryngeal Diseases ; pathology ; surgery ; Laryngoscopy ; Larynx ; pathology ; Retrospective Studies ; Vocal Cords ; pathology

Adult ; Amyloidosis ; pathology ; surgery ; Diagnosis, Differential ; Female ; Humans ; Muscular Diseases ; pathology ; surgery ; Neck Muscles ; pathology ; surgery

Amyloid ; analysis ; Amyloidosis ; pathology ; Female ; Humans ; Ureter ; pathology ; Ureteral Diseases ; pathology

We present a case of localised AA-type amyloidosis of the ureter with spheroids of amyloid. Localised AA-type amyloidosis of the urogenital tract is uncommon and extremely rare as a cause of ureteric obstruction, with only two such cases described in the literature to date. Most previously described cases at this site are related to primary AL-type amyloidosis. Another interesting finding in this case is the presence of spheroids of amyloid, which to the best of our knowledge, has not been previously reported at this site, and is also unusual at other sites.
Adult ; Amyloid ; analysis ; Amyloidosis ; pathology ; Female ; Humans ; Ureter ; pathology ; Ureteral Diseases ; pathology

Amyloidosis ; pathology ; Humans ; Laryngeal Diseases ; etiology ; Larynx ; pathology ; Male ; Middle Aged ; Nasopharynx ; pathology