Alzheimer Disease: Saeger W

Röcken C, Ernst J, Hund E, Michels H, Perz J, Saeger W, Sezer O, Spuler S, Willig F, Schmidt HH, Anonymous00262. · Institut für Pathologie, Charité-Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin. · Dtsch Med Wochenschr. · Pubmed #16835821 No free full text.

Abstract: Within the past 10 years, a new range of knowledge has been achieved in the field of amyloidosis, especially with regard to pathogenesis, diagnosis and therapy. Amyloidosis leads to variable and distinct symptoms and is caused by different underlying conditions. Some amyloidoses are acquired secondary to a chronic condition; others are caused by genetic mutations. Amyloid and amyloidosis occur more frequently than they are perceived. Among the frequent localized forms are the cerebral amyloidosis linked to Alzheimer disease (AD) and the pancreatic amyloidosis linked to diabetes mellitus. Among the most frequent systemic (extracerebral) forms is AL amyloidosis, which often has a poor prognosis and if untreated can rapidly lead to death. Systemic amyloidosis that happen at infancy are mainly AA amyloidosis that can progress to death already at early or at middle adulthood. Amyloidosis can be treated but therapeutic success significantly depends upon early diagnosis and proper classification of the amyloid type. It is mandatory that differential diagnosis demonstrate the presence of amyloid and clearly identify the type of the disease. Development of methods and techniques have contributed to improvements in the diagnosis and treatment. Early diagnosis and proper classification of amyloid is decisive for therapeutic options and upon them depend quality of life and mortality. The therapeutic spectrum is various and includes organ transplantation, chemotherapy, and anti-inflammatory strategies. Gene therapy and biological active substances have to be considered in the near future.

Foitschik T, Saeger W, Riebe M, Röcken C. · Institute of Pathology, Marienkrankenhaus, Hamburg, Germany. · Amyloid. · Pubmed #16194872 No free full text.

Abstract: Advanced glycation end-products (AGEs) may be involved in either amyloidogenesis or complications related to amyloid. The incidence of AGE increases with age as does the prevalence of amyloid affecting the hip joint capsule and intervertebral discs. We hypothesized that AGEs may be involved in the pathology of these amyloidoses and investigated the spatial and temporal relationship between AGEs and amyloid of intervertebral discs and hip joint capsules. Using immunohistochemistry, AGEs were found in all 71 intervertebral discs and all 87 hip joint capsules. Amyloid was present in 59 (83%) intervertebral discs and 65 (75%) hip joint capsules. AGEs were found in the immediate vicinity of amyloid deposits in 104 of 253 (41%) investigated amyloid deposits of the intervertebral discs and 159 of 311 (51%) investigated amyloid deposits of the hip joint capsules. However, only rarely were AGEs demonstrated within amyloid deposits. No linear correlation was found between the amount of AGEs and the amount of amyloid deposited. As AGEs are more common than amyloid in intervertebral discs and hip joint capsules, it is conceivable to suggest that AGEs might be involved in the pathogenesis of amyloid at these anatomical sites. However, the amyloid proteins appear not to be modified and AGE modification is not a general characteristic of senile amyloidoses.