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Query: UMLS:C0026764 (multiple myeloma)
 36,148 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The pathway taken by membrane that is recovered by endocytosis from the surface of secretory cells was investigated with electron-dense tracers 9dextrans and cationized ferritin). The cell types examined included exocrine cells of the parotid and lacrimal glands, endocrine cells of the anterior pituitary gland, and immunoglobulin-secreting cells from lymph nodes or myeloma cell lines. In all cases, when the cells were incubated at 37 degrees C the tracers were initially taken up by endocytosis and they later appeared in the stacked Golgi cisternae, in immature secretion granules or vacuoles and in lysosomes. Similar results were obtained after covalent labelling of surface membrane constituents when myeloma cells were radioiodinated and the fate of the labelled components was followed by autoradiography. Initially only the cell surface was labelled, and the autoradiographic grains were concentrated over the plasmalemma. After incubation at 37 degrees C some of the labelled components were internalized (by endocytosis), and the majority of the internal autoradiographic grains were found over Golgi cisternae and over associated secretory vacuoles, which were the only organelles significantly labelled. The findings indicate the existence of considerable membrane traffic from the plasmalemma to the stacked Golgi cisternae and forming secretion granules or vacuoles in all these cell types. Membrane is thus continually recovered from the cell surface of secretory cells and funnelled through the Golgi complex; moreover, the plasmalemma-to-Golgi traffic appears to represent a major route of membrane traffic in secretory cells. A large portion of this traffic appears to be associated with the recycling of the membrane containers used in the packaging of secretory products.
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PMID:Membrane recycling in secretory cells: pathway to the Golgi complex. 618 82

In 76 patients with clinically well defined multiple myeloma (median age at diagnosis: 68.5 years) serum-ferritin (SF) and beta 2-microglobulin (beta 2M) were measured by RIA-methods. 70 sex and age-matched healthy individuals served as controls. Both serum-ferritin (median: 343 micrograms/l vs. 193 micrograms/l; p less than 10(-7)) and beta 2M (median: 4.25 mg/l vs. 3.5 mg/l; p less than 0.01) showed a significant increase in myeloma patients compared to controls. Intercorrelation analysis revealed significant correlations between SF and tumour mass, serum-creatinine and beta 2M and between beta 2M and tumour mass, percentage of plasma cell infiltration in bone marrow, agglutinin titer, serum-creatinine, hemoglobin and age of the patients. Both tumour proteins might gain clinical importance particularly in those patients in which precise monitoring of disease is impossible either due to lack of paraprotein production or due to the particular paraprotein type. This seems to account for patients with light chain paraproteins, and furthermore for those patients with biclonal gammopathies or with IgE- and/or IgD-paraproteins.
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PMID:[Serum ferritin and beta-2-microglobulin in multiple myeloma]. 618 72

In 76 patients with clinically well-defined multiple myeloma (median age at diagnosis: 68.5 years), serum ferritin (SF) and beta 2-microglobulin (beta 2M) were measured by RIA methods. Seventy sex- and age-matched healthy individuals served as controls. Both serum ferritin (median: 343 vs 193 micrograms/liter; P less than 10(-7] and beta 2M (median: 4.25 vs 3.5 mg/liter) showed a significant increase (P less than 0.05) in myeloma patients compared to controls. Intercorrelation analysis revealed significant correlations between SF and tumor mass, serum creatinine, and beta 2M, and between beta 2M and tumor mass, percentage of plasma cell infiltration in bone marrow, agglutinine titers, serum creatinine, hemoglobin, and age of the patients. Both tumor proteins might gain clinical importance particularly in those patients in which precise monitoring of disease is impossible either due to lack of paraprotein production or due to the particular paraprotein type. This seems to account for patients with light chain paraproteins, and for those patients with biclonal gammopathies or with IgE and/or IgD paraproteins.
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PMID:Serum ferritin and beta 2-microglobulin in patients with multiple myeloma. 619 21

To study human monocyte functions, we attempted to immortalize human monocytes by producing somatic cell hybrids between such monocytes and the mouse myeloma cell line NSI. In this study we report the successful establishment of eight hybrid cell lines that have been grown in culture for more than a year, and some of them retained part of the human chromosome complement, as well as monocyte markers and activities. Karyotype analysis of these hybrid lines revealed that cells of seven out of eight of the lines contained one to 16 human chromosomes and in four of them, more than nine human chromosomes were observed. Several of the cell lines expressed monocytic markers and functions. Thus, in two of the hybrid lines nonspecific esterase could be demonstrated in 10 to 29% of the cells, and Fc receptors were demonstrated in three of the hybrid cell lines. Significant levels of human ferritin were detected in one of the lines, and two other cell lines secreted interleukin 1-like substance into the culture medium. These results encourage us to use human-mouse somatic cell hybridization as an approach for the establishment of human monocyte cell lines, which will preserve their functions and produce monocyte-derived factors.
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PMID:Establishment of cell lines from somatic cell hybrids between human monocytes and mouse myeloma cells. 660 77

The surface anionic site distribution on membranes of a monoclonal antibody-producing hybridoma cell line, and its two parental cells: normal spleen cells of immunized BALB/c mice and cells from a mouse myeloma line (NS-1), were investigated with the aid of the cationized ferritin (CF) labelling method, following glutaraldehyde/formaldehyde fixation of cells. The patch-like CF distribution on the hybridoma cells is similar to that of the NS-1 myeloma cells, but distinct from the even and continuous CF distribution of the immunized and nonimmunized normal spleen lymphocytes. The similarity in the formation of patch-like CF heaps, both on myeloma and hybrid cells is discussed in respect to the surface charge characteristic determined by cell fusion.
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PMID:Distribution of surface anionic sites on mouse hybrid myelomas. 662 23

Splenic lymphocytes of mice, immunized with membrane-enriched fractions of metastatic human mammary carcinoma tissues, were fused with the NS-1 non-immunoglobulin-secreting murine myeloma cell line. This resulted in the generation of hybridoma cultures secreting immunoglobulins reactive in solid-phase radioimmunoassays with extracts of metastatic mammary carcinoma cells from involved livers, but not with extracts of apparently normal human liver. As a result of further screening of immunoglobulin reactivities and double cloning of cultures, 11 monoclonal antibodies were chosen that demonstrated reactivities with human mammary tumor cells and not with apparently normal human tissues. These monoclonal antibodies could be placed into at least five major groups on the basis of their differential binding to the surface of various live human mammary tumor cells in culture, to extracts of mammary tumor tissues, or to tissue sections of mammary tumor cells studied by the immunoperoxidase technique. Whereas a spectrum of reactivities to mammary tumors was observed with the 11 monoclonal antibodies, no reactivity was observed to apparently normal cells of the following human tissues: breast, lymph node, lung, skin, testis, kidney, thymus, bone marrow, spleen, uterus, thyroid, intestine, liver, bladder, tonsils, stomach, prostate, and salivary gland. Several of the antibodies also demonstrated a "pancarcinoma" reactivity, showing binding to selected non-breast carcinomas. None of the monoclonal antibodies showed binding to purified ferritin or carcinoembryonic antigen. Monoclonal antibodies of all five major groups, however, demonstrated binding to human metastatic mammary carcinoma cells both in axillary lymph nodes and at distal sites.
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PMID:A spectrum of monoclonal antibodies reactive with human mammary tumor cells. 678 31

Balb/c Mice were immunized with splenic isoferritin. Spleen cells from immunized Mice were fuzed with SP2O myeloma cells. Four monoclonal antibodies designated respectively M29, M211, M386 and B8 were selected. Various isoferritins were analysed by immunodiffusion (Ouchterlony technic). With these monoclonal antibodies and with Rabbit polyclonal sera: human basic and acidic isoferritins and Horse spleen ferritin. Ferritin could be precipitated by these monoclonal antibodies. These results confirm that the ferritin molecule consists of repeating antigenic sites. No immunoreactivity difference could be detected between acidic and basic human ferritine. Species specificity was recognized. The high affinity constant of the M29 monoclonal antibody allowed development of a standardized radioimmunossay of ferritin.
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PMID:[Analysis of various isoferritins with monoclonal antibodies]. 681 79

Data from 90 patients with a variety of hematologic malignant neoplasms were studied to determine the relation between changes in serum ferritin concentration and the clinical status of the patients. Patients with Hodgkin's disease, non-Hodgkin's lymphoma, multiple myeloma, blastic crisis of chronic myelocytic leukemia, acute myeloblastic leukemia and acute lymphoblastic leukemia were found to have significantly elevated serum ferritin levels. Further study of serum ferritin concentration in certain hematologic malignant neoplasms might provide a valuable insight into the role of serum ferritin determination in the diagnosis and follow-up of patients with malignant diseases.
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PMID:Serum ferritin levels in hematologic malignant neoplasms. 693 89

The proteinase from culture supernatants of Candida albicans strain CBS-2730 was purified virtually to homogeneity by ion-exchange chromatography and affinity chromatography. The enzyme consists of a single polypeptide chain with tryptophan at the N- and leucine at the C-terminus. Its molecular weight is approx. 45,000 and the isoelectric point is at pH 4.4. With albumin as a substrate an apparent Km was determined to be 7 . 10(-5) M. The enzyme is inhibited by pepstatin at equimolar ratio and thus is a carboxyl proteinase (EC 3.4.23.6). Other group-specific inhibitors, though, did not efficiently block the enzyme. Above pH 8.4 the enzyme undergoes alkaline denaturation which is accompanied by dimerization. The enzyme is a glycoprotein. It is stable in presence of non-ionic detergents and can be freeze-dried. The enzyme clots milk at pH 5.5 and has trypsinogen kinase activity. Among several purified proteins that have been tested as a substrate, only horse ferritin was resistant to proteolysis, while myeloma proteins of the A1- and A2-type were readily cleaved, as were two proteinase inhibitors of human serum. Antibodies against purified enzyme did not react with several commercial Candida antigen preparations; antibodies against the enzyme, though, have been detected repeatedly in sera from patients with manifest candidiasis.
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PMID:Properties of a purified proteinase from the yeast Candida albicans. 701 86

In a group of 111 patients with multiple myeloma (MM) comprising a group of 34 patients examined when the diagnosis was established and a group of 77 patients evaluated in different stages of the disease, the author examined the relationship between the interleukin-6 serum level (IL-6), assessed by the method of enzyme immunoanalysis and selected laboratory indicators of the disease. Elevated IL-6 values were recorded in 38% of the patients. In neither of the groups significant relations were found between IL-6 and calcium, urea, creatinine levels, the amount and type of monoclonal immunoglobulin, lacticode dehydrogenase, beta 2-microglobulin, ferritin, IL-2 and its soluble receptor in serum and the incidence of myeloma plasmocytes in bone marrow. In the second (but not in the first) group a significant relationship was recorded between IL-6 levels and the red cell sedimentation rate, the Hb value, the CRP level and serum albumin and the value of thymidinekinase in serum of patients with a value beyond the normal range. From the investigation ensues that examination of IL-6 serum levels in MM contributes so far mainly to improvement of the diagnosis and expedient classification of this disease in clinical practice.
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PMID:[Serum interleukin-6 in multiple myeloma: I. Relation to selected laboratory indicators of disease]. 748 49


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