[Application of Nd-YAG laser hyperthermia in urogenital tumors].
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Humans↗
Biomedical subjects
T Shirahama
Publications and source records attributed to T Shirahama.
Isolation of the amyloid P component from the Engelbreth-Holm-Swarm (EHS) tumor of the mouse.
The amyloid P component was isolated from the mouse EHS tumor, a producer of basement membrane-like material. Following collagenase treatment of the tissue homogenate and centrifugation, the supernatant was purified by calcium-dependent binding to agarose, and elution with ethylenediaminetetraacetic acid. Identification of the purified material as the amyloid P component was established by immunodiffusion and electron microscopic appearance as 8.5 nm pentagonal units, frequently assembled into columns. SDS-PAGE gel electrophoresis yielded 25,000 D bands, suggesting that the amyloid P is of the mouse type. It is proposed that the mouse amyloid P component extracted from the tumor is located within the basotubules present in the pericellular matrix.
Amyloid↗
The induction of accelerated murine amyloid with human splenic extract. Probable role of amyloid enhancing factor.
Amyloid enhancing factor (AEF) is derived from the tissues of pre-amyloidotic and amyloidotic animals and, when transferred, greatly accelerates amyloid induction in the recipient murine models. It has also been reported that similarly accelerated amyloid induction can be achieved in mice by injection of human splenic homogenates from patients with amyloidosis. The present study has attempted to characterize further the mechanism of this "heterologous transfer of amyloid". Treatment of mice with the "tissue homogenate" or the "AEF extract" of AA-, AL- and A prealbumin-laden human spleens followed by daily subcutaneous casein injections induced amyloidosis in an accelerated fashion. The resultant amyloid deposits in mice had strongly positive immunohistochemical reactions with anti-mouse AA, and negative reaction with anti-human AA or anti-human prealbumin. The results lend support to the idea that accelerated amyloid induction in the recipient mice is unlikely to be due to transfer of human amyloid substance, but rather to formation of "native" murine amyloid under the influence of a human AEF factor similar to or identical with AEF described in mouse-to mouse transfer models.
Amyloid↗
The association of an elastase with amyloid fibrils.
The fibrils of all systemic forms of amyloid (primary, AL; secondary, AA; and hereditary, AF) that had been isolated by the water extraction procedure demonstrated elastolytic enzyme activity when examined in a specific assay using tritiated elastin. The source of this fibril-bound enzyme activity was consistent with human neutrophil elastase (HNE), since it was readily extracted by high salt solutions and inhibited by an elastase-specific chloromethyl ketone inhibitor, human alpha-1-protease inhibitor or by an antibody specific for HNE. The presence of an elastase on the amyloid fibril may suggest physiologic mechanisms of amyloid precursor protein degradation.
Amyloid↗
[Studies on gamma-glutamyltranspeptidase in warm ischaemic kidneys of rats].
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Animals↗
In vitro formation of amyloid fibrils from intact beta 2-microglobulin.
Prompted by the identification of hemodialysis-associated amyloid protein as beta 2-microglobulin, we attempted to create in vitro amyloid fibrils from the native protein. Beta 2-microglobulin in PBS was slowly dialyzed free of salt and then concentrated. The residue showed Congophilia with green birefringence by light microscopy and polarization, and non-branching fibrils of indeterminate length, measuring 8 to 10 nm in diameter by electron microscopy, thus meeting the morphologic criteria for amyloid. The present study demonstrates the first successful in vitro creation of amyloid fibrils with intact precursor protein molecules and provides supporting evidence that hemodialysis-associated amyloid is constituted from beta 2-microglobulin.
Amyloid↗
A new form of amyloid protein associated with chronic hemodialysis was identified as beta 2-microglobulin.
Amyloid fibrils were isolated from amyloid-laden tissue obtained from a chronic hemodialysis patient with carpal tunnel syndrome. After solubilization in guanidine HCl, a significant amount of the protein was located in a homogeneous low molecular weight fraction. The protein was found to be identical to beta 2-microglobulin, with regard to its molecular weight of 11,000, amino acid composition and 16 amino-terminal amino acids: Ile-Gln-Arg-Thr-Pro-Lys-Ile-Gln-Val-Tyr-Ser-Arg-His-Pro-Ala-Glu-. These results demonstrate that the amyloid associated with chronic hemodialysis contains as major component a new form of amyloid fibril protein that is homologous to beta 2-microglobulin.
Amino Acid Sequence↗
Widespread occurrence of AP in amyloidotic tissues. An immunohistochemical observation.
Plasma (P)-component of amyloid (AP or SAP), while not an integral part of the amyloid fibril, has been considered to be intimately associated with virtually every different type of amyloid. In the present study, we evaluated the distribution of AP in the organs frequently involved in two forms of human systemic amyloidosis (AA and AF) and in mouse AA amyloidosis, by use of immunohistochemistry with anti-AP. Although the amyloid deposits generally showed moderate reactions with anti-AP, they were not always clearly distinguished from the surrounding non-amyloid tissue elements which often stained as well. The basement membrane often showed even stronger reaction to anti-AP than the adjacent amyloid deposits, and liver sections demonstrated such a high overall reaction to anti-AP that the anti-AP reaction on the amyloid deposits was often obscurred. The present results suggest that the binding between AP and the amyloid fibril may not be monospecific, that AP by this technique occurs rather widely throughout the body, and therefore that anti-AP may not be considered as specific a marker for amyloid deposits in immunohistochemical and perhaps other studies as well.
Amyloid↗
Histochemical and immunohistochemical characterization of amyloid associated with chronic hemodialysis as beta 2-microglobulin.
The carpal tunnel syndrome has been associated with amyloid deposits and is now regarded as a major complication in patients undergoing chronic hemodialysis. The hemodialysis-associated amyloidosis appears to have systemic rather than local involvement, although its full extent is yet to be determined. In an attempt to examine the chemical and immunologic nature of the amyloid, the authors carried out a series of histochemical and immunohistochemical studies with the following results. The amyloid was "sensitive" to the "permanganate treatment," suggesting it was the AA (secondary) type. On immunohistochemistry, however, anti-human AA did not give positive reaction with the amyloid deposits, suggesting that this would be a new form of amyloid. As reported elsewhere, the authors' preliminary results on the amino acid sequence analysis in one specimen have revealed homology of its amino terminal sequence to beta 2-microglobulin. In the present study, anti-beta 2-microglobulin did indeed react positively (with appropriate controls) with the amyloid deposits in the tissues collected from five different patients, confirming the beta 2-microglobulin-related nature of the amyloid. The present observations are significant in two points: (a) they confirm that hemodialysis-associated amyloid is of beta 2-microglobulin origin since it shares same antigenic determinant(s) with it and since the amino acid sequence is homologous; and (b) it adds what many have suspected, i.e., "permanganate-sensitive" amyloid is not specific for the AA type but includes AA and beta 2-microglobulin amyloid deposits at the minimum.
Amyloid↗
Immunocytochemical study of hepatocyte synthesis of amyloid AA. Demonstration of usual site of synthesis and intracellular pathways but unusual retention on the surface membrane.
For determination of the intracellular site of synthesis and the pathways followed by amyloid protein AA, immunocytochemical localization of the anti-AA reactive substance was investigated in the livers of CBA/J mice in an acute-phase response evoked by a single subcutaneous injection of 0.5 ml of 10% casein. In the cytoplasm of the hepatocytes, the positive reaction was localized on and/or in the rough endoplasmic reticulum and the single membrane-bound vesicles, vacuoles and lamellae including the Golgi apparatus, confirming that amyloid protein AA follows the common routes of synthesis and secretion established for other proteins. The anti-AA-reactive substance was also localized on the free surface of the hepatocyte membrane, including the microvilli. The latter reaction appeared as early as but lasted at least several hours longer than its cytoplasmic counterpart, suggesting that a certain retention period exists before the release of the AA-reactive substance from the cellular surface to the free blood plasma.
Amyloid↗
[Induction of human monocyte-mediated tumor cell killing by alpha or beta interferon].
Human blood monocytes, separated on a continuous percoll gradient, were not cytotoxic to allogeneic A375 melanoma cells. The monocyte monolayers were activated to become tumoricidal by incubation for 24 hr with interferon (IFN)-alpha or beta at concentrations of more than 1,000 IU/ml. Significant and reproducible activation of the monocytes was achieved by incubating them with 10,000 IU/ml of IFN-alpha or IFN-beta for 24 hr. Similarly, suspended, but not plated, monocytes were activated to a tumoricidal state by interaction with IFN-alpha or IFN-beta. Monocytes that had lost tumoricidal activity during culture, were reactivated by a second exposure to IFN-alpha. Fluorescence analysis showed that the monocyte-rich adherent monolayers were contaminated with up 2.0% of natural killer (NK) cells. Pretreatment of isolated monocyte preparations with anti-NK cell monoclonal antibody (Leu-11b) to deplete them of NK cell activity did not inhibit the monocyte-mediated cytotoxicity. These results indicate that human monocytes are rendered tumoricidal by direct interaction with IFN-alpha or IFN-beta, although more than 1,000 IU/ml of IFN-alpha or IFN-beta is required for maximal expression of monocyte activation.
Cell Line↗
Induction by interferon-alpha of tumoricidal activity of adherent mononuclear cells from human blood: monocytes as responder and effector cells.
Human blood monocytes, separated on a Percoll gradient, were not cytotoxic to allogeneic melanoma (A375) cells. Fluorescent analysis showed that the monocytes were contaminated with up to 2.0% natural killer (NK) cells. The monocytes became tumoricidal on incubation for 24 h with greater than or equal to 1,000 IU/ml interferon-alpha (IFN-alpha) derived from human lymphoblastic leukemia cells. Anti-IFN-alpha antibody abolished the ability of IFN-alpha to render the monocytes tumoricidal, whereas anti-IFN-beta antibody had no effect. Pretreatment of isolated monocyte preparations with anti-NK cell monoclonal antibodies (Leu-7 and Leu-11b), to inhibit NK cell activity, did not affect the cytotoxicity of IFN-alpha-activated monocytes on tumor cells. Full expression of cytotoxicity on tumor cells required the interaction of monocytes with IFN-alpha for 24 h. These results indicate that IFN-alpha directly activates human monocytes to become tumoricidal, although greater than or equal to 1,000 IU/ml IFN-alpha is required for maximal activation.
Cell Line↗
[Antiproliferative activities of interferon-alpha].
The antiproliferative activities of human lymphoblastoid interferon-alpha (MOR-22) against 22 cultured human cell lines were examined. Daudi cells and ACHN cells were highly sensitive to interferon compared with other human cells. The cell lines derived from renal and brain tumors showed concentration-dependent growth inhibition as determined from a 7-day growth curve but the concentration dependency was different in various cell lines. It was shown that longer exposure to interferon was necessary to obtain antiproliferative activity, and cell growth inhibition was completely reversible by washing the cultures. It was suggested that interferon had a time-dependent antiproliferative action.
Brain Neoplasms↗
Colchicine inhibition of serum amyloid protein SAA and SAP synthesis in primary mouse liver cell cultures.
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Amyloid↗
Familial amyloid polyneuropathy. Demonstration of prealbumin in a kinship of German/English ancestry with onset in the seventh decade.
A family with autosomal dominant transmitted familial amyloid polyneuropathy residing in Texas is described. Clinically, the prominent sensory and severe autonomic nervous system involvement resembles the Andrade (Portuguese) type I familial amyloid polyneuropathy but is unique in that the age of onset is in the seventh decade in all family members affected to date. Using an immunoperoxidase technique, prealbumin was demonstrated in the amyloid deposits. This finding suggests that this family shares biochemical as well as clinical characteristics consistent with similar kinships with type I familial amyloid polyneuropathy of diverse geographic origin.
Age Factors↗
Heterogeneous participation of the hepatocyte population in amyloid protein AA synthesis.
Amyloid protein AA is believed to be synthesized in the liver in a form of its precursor, the acute phase reactant, SAA. To identify precisely the cell involved in SAA biosynthesis, immunohistochemical reaction to anti-mouse AA was analysed on the liver sections from CBA/J mice which had received a single casein injection and were sacrificed at predetermined times up to 48 hours. Two different primary localizations of the reaction were revealed. One was in the cytoplasm of certain hepatocytes. This reaction peaked at 6-8 hours after the casein injection in the intensity of the reaction and in the number of the cells involved. The hepatocytes with positive cytoplasmic reaction were scattered over the lobule and even at the peak did not exceed 20% of the total hepatocyte population. The other localization of the reaction covered linearly the surface of the hepatocyte cords, and peaked at 12-16 hours after the casein injection.
Amyloid↗
In vitro cytotoxicity to various human tumor cell lines of a tumor cytotoxic factor(s) produced by human alveolar macrophages.
When human alveolar macrophages (AM) obtained by lavage of the lungs of healthy donors were incubated in medium with or without lipopolysaccharide (LPS) they released a factor(s) with tumor cell killing activity. This tumor cytolytic and/or cytotoxic factor(s) (TCF) was assayed by measuring its effect in inhibiting target cell growth. TCF activity was not observed in the supernatant from cultures of LPS-treated hematopoietic malignant cell lines (monocytic leukemia, B-cell leukemia and T-cell leukemia cell lines). Human TCF was significantly cytotoxic to 13 of 15 solid-tumor cell lines tested and to 7 of 9 hematopoietic malignant cell lines, but not to two different normal, nontumorigenic cell lines. TCF-rich supernatants contained low levels of interferon (IFN) activity that were not significantly cytotoxic to A-375 melanoma cells. Human TCF and IFN-alpha or IFN-beta had additive cytotoxic effects. These data suggest that human TCF released by activated human AM may be of potential use in the treatment of malignant disseminated diseases.
B-Lymphocytes↗
Purification and immunochemical studies of pyruvate dehydrogenase complex from rat heart, and cell-free synthesis of lipoamide dehydrogenase, a component of the complex.
Pyruvate dehydrogenase complex was purified from rat heart. The complex showed four polypeptide bands on sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis, corresponding to lipoate acetyltransferase (mol.wt. 68 000), lipoamide dehydrogenase (mol.wt. 56 000), alpha-subunit (mol.wt. 41 000) and beta-subunit (mol.wt. 35 000) of pyruvate dehydrogenase. Rat heart pyruvate dehydrogenase complex was dissociated into three component enzymes and the antibodies against each component enzyme were prepared. Anti-pyruvate dehydrogenase and anti-lipoate acetyltransferase antibodies effectively precipitated pyruvate dehydrogenase complex, but an anti-lipoamide dehydrogenase antibody released lipoamide dehydrogenase from the complex and effectively precipitated lipoamide dehydrogenase. Lipoamide dehydrogenase was synthesized in a cell-free reticulocyte lysate system with total RNA from rat liver. Its translation product was detected as a putative precursor which is 3000 Da larger than the mature subunit. In cell-free translation programmed with free and membrane-bound polysomes, activity of mRNA coding for the precursor of the enzyme was much higher in free polysomes than in membrane-bound polysomes.
Animals↗