Library

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Dimethyl sulfoxide  (1)
  • Immunoelectron microscopy  (1)
  • 1
    ISSN: 1432-2307
    Keywords: Amyloid ; Resorption ; Dimethyl sulfoxide ; Colchicine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The induction of amyloid in C3H mice by either casein solution or complete Freund's adjuvant emulsion with Mycobacterium butyricum was confirmed by partial splenectomy. The animals were autopsied after treatment w ith dimethyl sulfoxide (550 mg/kg, 50 times), colchicine (0.02 mg/kg, 15–37 times), or saline solution as a control. Detailed histological comparisons of biopsy and autopsy spleens provided evidence that dimethyl sulfoxide was significantly effective in the resorption of amyloid, while in the animals treated with colchicine amyloid deposition was increased. The effect of dimethyl sulfoxide was discussed with reference to the modification of amyloid fibrils.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    ISSN: 1432-2307
    Keywords: Amyloid ; Spleen ; Immunoelectron microscopy ; Intralysosomal formation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Early amyloid deposition in the spleen was studied by immunoelectron microscopy following the administration of rapid amyloid-inducing agents to mice. Two days after the injection of an amyloidenhancing factor and casein solution, a small amount of amyloid material was observed at the border of the white pulp and the marginal zone (perifollicular area) and also within the white pulp. At this stage, amyloid fibrils were seen mainly in an extracellular distribution along the cytoplasmic processes of reticular cells and also in the cytoplasmic invaginations of macrophages. By immunoelectron microscopy, gold particles labelled fibrillar structures in lysosome-derived organelles in some macrophages as well as dense bodies consisted of a homogeneous, granular matrix not having any recognizable fibrillar structures. Similar immunolabelled organelles were also observed in the amyloid resorption stage, although, at that stage, they commonly contained other phagocytized materials as well. From these findings, we suggest that at least some amyloid fibrils are polymerized in the cytoplasm of the macrophages by the proteolytic cleavage of previously pinocytized serum amyloid A protein (SAA).
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...