Disseminated superficial porokeratosis with amyloid deposits

Manuel Ginarte1, Alvaro León, Jaime Toribio

  • 1Department of Dermatology, Complejo Hospitalario Universitario de Santiago, Faculty of Medicine Santiago de Compostela, Spain. mginartev@medynet.com

Insights

Porokeratosis lesions can contain amyloid deposits, which are often missed by standard stains. Routine use of special histochemical techniques could improve detection of amyloid in porokeratosis.

Area of Science:

  • Dermatopathology
  • Histology
  • Biochemistry

Background:

  • Porokeratosis is a rare epidermal nevus characterized by abnormal keratinization.
  • Amyloidosis is a group of disorders characterized by the deposition of amyloid protein.
  • The association between porokeratosis and amyloid deposition is not well-established.

Observation:

  • A 65-year-old Caucasian male presented with disseminated superficial porokeratosis.
  • Histological examination revealed eosinophilic amorphous material in dermal deposits.
  • This material stained positively with crystal violet and showed yellow fluorescence with thioflavin-T, confirming amyloid.

Findings:

  • Amyloid deposits can arise from degenerated colloid bodies within porokeratotic lesions.
  • Standard hematoxylin and eosin staining may not detect small quantities of amyloid.
  • Specialized histochemical stains are crucial for accurate amyloid identification.

Implications:

  • Routine use of histochemical techniques could increase the frequency of amyloid detection in porokeratosis.
  • This finding may have implications for understanding the pathogenesis of porokeratosis.
  • Further research is needed to explore the clinical significance of amyloid in porokeratosis.

Related Concept Videos

Amyloid Fibrils03:03

Amyloid 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 Fibrils03:03

Amyloid 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...
Lysosomal Hydrolases01:22

Lysosomal 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,...
Skin Diseases and Disorders01:23

Skin Diseases and Disorders

Skin is the first line of defense and encounters a variety of microbes. Some pathogenic strains are often the cause of a broad range of infections of the skin and other body systems. These conditions can affect people of all ages and may have different causes, including genetic factors, infections, autoimmune reactions, environmental factors, and lifestyle choices.
Gram-positive Staphylococcus spp. and Streptococcus spp. are responsible for many of the most common skin infections. However, many...
Alzheimer Disease ll: Pathophysiology01:23

Alzheimer Disease ll: Pathophysiology

Alzheimer disease involves structural changes in the brain that begin long before symptoms appear. The most distinctive features are extracellular neuritic plaques and intracellular neurofibrillary tangles.Neuritic plaques form in the cerebral cortex and around blood vessels. These plaques contain a dense core of beta-amyloid (Aβ)—a toxic protein fragment that clumps outside neurons. The core is surrounded by damaged neuronal extensions, as well as reactive astrocytes and microglia. Abnormal...