Social support web-based resources for patients with chronic pain.

The authors performed an electronic search of websites that address psychosocial issues in pain management identified over 5 million sites. A search limited to pychosocial issue sin pain produced nearly 400,000. Nine scientific, professional and consumer-oriented websites were selected for review of social support information and opportunities using criteria focusing on patient information, referrals for counseling services and community-based assistance programs, self-help groups, specific pain syndromes, and readability and interpretability of consumer-oriented content. The internet can empower patients to self-manage their pain and seek out effective social support venues for improving their lives.

A primer of amyloid nomenclature.

The increasing knowledge of the exact biochemical nature of the localized and systemic amyloid disorders has made a logical and easily understood nomenclature absolutely necessary. Such a nomenclature, biochemically based, has been used for several years but the current literature is still mixed up with many clinical and histochemically based designations from the time when amyloid in general was poorly understood. All amyloid types are today preferably named by their major fibril protein. This makes a simple and rational nomenclature for the increasing number of amyloid disorders known in humans and animals.

Amyloid: toward terminology clarification. Report from the Nomenclature Committee of the International Society of Amyloidosis.

The modern nomenclature of amyloidosis now includes 25 human and 8 animal fibril proteins. To be included in the list, the protein has to be a major fibril protein in extracellular deposits, which have the characteristics of amyloid, including affinity for Congo red with resulting green birefringence. Synthetic fibrils with amyloid properties are best named 'amyloid-like'. With increasing knowledge, however, the borders between different protein aggregates tend to become less sharp.

Beta 2 microglobulin serum levels and prediction of survival in AL amyloidosis.

To study the relation between beta 2 microglobulin (beta 2M) and survival in AL amyloidosis, we measured the serum level of beta 2M in 80 patients with AL amyloidosis diagnosed within 1 year of evaluation, who had received no therapy. Patients had a median age of 61 years and 52% were male. Major clinical manifestations were renal disease in 25 patients (31%), cardiomyopathy in 23 patients (29%), and neuropathy or other organ involvement in 32 patients (41%). The beta 2M level, measured by an ELISA assay in serum samples collected at the time of evaluation, ranged from 1.69 to 10 mg/ml (mean = 4.57); in 56% of the patients beta 2M > 4 mg/ml. The patients with a beta 2M < or = 4 mg/ml had serum creatinine levels lower than those with beta 2M > 4 (1.43 vs 2.67 mg/dl; p = 0.02). Survival from study entry was analyzed overall by the level of beta 2M, adjusting for creatinine level and clinical stratum. We found the beta 2M level to be predictive of survival (median survival 16.1 months for beta 2M < or = 4 mg/ml vs 8.0 months for beta 2M > 4 mg/ml, p = 0.044). Thus a beta 2M level less than 4 mg/ml indicated a longer time of survival.

Lysosomal breakdown of amyloid fibrils by macrophages

Mouse peritoneal macrophages incubated with isolated human amyloid fibrils for varying periods of time up to 24 hours were studies by electron microscopy, and by electron microscopic cytochemistry for demonstration of acid phosphatase activity. The sequential changes in cytoplasmatic vacuoles in macrophages containing the amyloid fibrils and related material were analyzed and compared with those in controls and with direct enzymatic digestion of amyloid fibrils. the results suggest that the lysosome into amorphous, granular or finely filamentous material and absorbed, leaving undigested material as membranous or myeling the lysosomal enzymes into the amyloid-phagosome or the amyloid-phagolysosome was studied and interpreted as showing (1) fusion of primary lysosome (s) with the phagocytic vacuole, (2) autophagy of primary lysosome(s) into the heterophagic vacuole, and (3) transport of the enzymes into the phagocytic vacuole durectly from the Golgi associated vesicles or smooth endoplasmatic reticulum.