Systemic amyloidosis: a clinical survey of 144 cases.
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Amyloid↗
Biomedical subjects
S Janssen
Publications and source records attributed to S Janssen.
Classification of amyloidosis: immunohistochemistry versus the potassium permanganate method in differentiating AA from AL amyloidosis.
As systemic AA and Al amyloidosis differ considerably with regard to prognosis and therapeutic approach, it is of importance to make an accurate histochemical classification with regard to the amyloid protein involved. In the present study the results of the potassium permanganate (KMnO4) method, an indirect histochemical procedure based on differences in cross-beta-potential of different amyloid fibril proteins, were compared with the results of an immunohistochemical method utilizing anti-AA and anti-AP antibodies. Renal biopsy sections of patients with systemic amyloidosis related to inflammatory conditions, systemic amyloidosis associated with plasma cell dyscrasia, idiopathic systemic amyloidosis, and nonamyloidotic controls were studied. Positive reaction of anti-AA was observed on all KMnO4-sensitive amyloid deposits, whereas the KMnO4-resistant amyloid deposits remained unstained, provided that highly purified anti-AA antiserum was used. Anti-AP produced not only comparable staining of both KMnO4-sensitive and -resistant amyloid deposits, but also of glomerular basement membranes and elastin layers of blood vessels in amyloid and control biopsies. The intensity of anti-AP reactivity was comparable with the reaction of anti-AA on KMnO4-sensitive amyloid deposits. The present results confirm the specificity of the KMnO4 method, which is a simple method available to every laboratory, in differentiating between AA and AL amyloidosis. Furthermore, the results indicate that, at least in renal biopsy specimens, anti-AP may serve as a general marker for AA and AL amyloid deposition; this finding is in contrast to the results of a recently published report.
Amyloid↗
[Possibilities and difficulties. Methodical actions in a general hospital].
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Hospitals, General↗
Soft-tissue uptake of 99mTc-diphosphonate in systemic AL amyloidosis.
A case of systemic AL (amyloid light-chain-derived) amyloidosis is presented, in which a 99mTc-diphosphonate bone scan demonstrated the intense uptake of tracer in the liver, spleen, heart, thyroid, oropharyngeal region, intestinal tract and uterus. The presence of amyloid deposits in these organs was confirmed at autopsy. A review of the literature is given. In amyloidosis, the binding of radionuclide-labeled calcium-seeking agents, such as diphosphonate and pyrophosphate, may be explained by the high calcium content of amyloid. The presence of calcium in amyloid is due to the presence of the non-fibrillar protein, amyloid P-component (AP). In our patient, the amyloid deposits reacted on immunofluorescence with antibodies directed against AP.
Amyloid↗
Mouse epididymal sperm contain active P450 aromatase which decreases as sperm traverse the epididymis.
Recently we reported that mouse germ cells in the testis contain active P450 aromatase (P450arom), the enzyme that converts androgens to estrogens. This finding suggested that germ cells have the ability to produce estrogen. Further studies have shown that germ cells in the testis of several species contain P450arom. The goal of this study was to determine if epididymal sperm contain P450arom and if P450arom activity in sperm changes during traversion of the epididymis in the adult mouse. P450arom was localized in sperm present in the efferent ductules and epididymis by immunocytochemistry using an antiserum generated against purified human placental cytochrome P450arom. P450arom immunostaining in sperm was most prominent in sperm located in the proximal caput epididymis, decreased as sperm traversed the corpus epididymis, and was only slightly apparent in sperm in the cauda epididymis. The immunolocalization of P450arom in epididymal sperm was supported by the measurement of P450arom activity in sperm by the 3H2O assay. We found that P450arom activity in sperm significantly decreases as sperm traverse the epididymis. Based upon these observations, we conclude that sperm can synthesize estrogen and that the synthesis of estrogen by sperm present in the efferent ductules and caput epididymis could be important in the process of sperm maturation.
Animals↗
Rat testicular germ cells and epididymal sperm contain active P450 aromatase.
Although testosterone is the principal sex steroid produced by the testis, estrogen is known to be produced by both Leydig and Sertoli cells during different developmental periods. Additionally, evidence is unfolding to suggest that germ cells might also participate in the synthesis of estrogen within the male reproductive tract. We have recently reported that the messenger ribonucleic acid (mRNA) for P450 aromatase (P450arom), the enzyme that converts androgen to estrogen, is synthesized by rat germ cells. Therefore, the present study was conducted to determine which germ cell types synthesize active P450arom and to measure the activity of this enzyme in germ cells throughout spermatogenesis and in maturing sperm during epididymal transit. First, P450arom activity was measured in pachytene spermatocytes, round spermatids, and a mixture of round spermatids, elongating spermatids, and residual bodies using the tritiated water (3H2O) assay. Second, sperm isolated from different regions of the epididymis were assayed for P450arom activity. Sperm isolated from the caput epididymis with attached efferent ductules had the higher P450arom activity, whereas sperm isolated from the corpus and cauda epididymides had lower P450arom activity. The decrease in P450arom activity in cauda sperm was further confirmed by immunocytochemistry. On the basis of these observations, we conclude that rat testicular germ cells from pachytene spermatocytes through elongating spermatids and epididymal sperm contain active P450arom and that sperm lose aromatase activity as they mature during epididymal transit. Therefore, both post-pachytene rat germ cells and epididymal sperm are capable of estrogen synthesis and are an additional, potentially significant, source of estrogen in the male reproductive tract.
Animals↗