The intracellular localisation of immunoglobulin in human lymphoid cells and haematopoietic cell lines by immunoperoxidase electron microscopy

Newell, D. G.; Bohane, C.; Payne, S V; Smith, Joan K.

doi:10.1016/0022-1759(80)90313-0

Cited by 15 publications

(2 citation statements)

References 9 publications

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“…Although the biochemical and immunofluorescence studies indicated that the hairy cells were synthesizing and expressing immunoglobulin of h light chain and a heavy chain classes exclusively, the expression and synthesis of other classes of immunoglubulin heavy chains and x light chains, by apparently normal cells, was confusing, particularly in the presence of the Ax paraprotein. Using a recently developed immunoperoxidase technique for the electron microscopic localization of immunoglobulin (Newell et al 1980) hairy cells, identified by the presence of RLC were demonstrated to contain immunoglobulin of a and h classes in the cisternae of the perinuclear space, rough endoplasmic reticulum and Golgi apparatus. This distribution of immunoglobulin is consistent with that found in lymphoblastoid and myeloma cell lines and reflects the synthesis and excretion of immunoglobulin in these cell lines (Newell et a1 1982).…”

Section: Discussionmentioning

confidence: 99%

Hairy Cell Leukaemia Occurring with an Unrelated Paraproteinaemia

Newell

Sattar

Hannam-Harris

et al. 1982

Scandinavian Journal of Haematology

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A detailed study is described of a case of hairy cell leukaemia, presenting with a serum paraprotein of an immunoglobulin (Ig) class different from that synthesised by the neoplastic cells. The case was unusual in its association with leukaemic arthropathy but ultrastructurally the hairy cells were typical. By immunofluorenscence and immuno!electron microscopy the neoplastic cells expressed IgAh both on the cell surface and intracellularly in the rough endoplasmic reticulum, perinuclear space and Golgi apparatus. No Ig was observed in the ribosomal-lamellae complexes. These cells also synthesised and secreted Ig of class Ah in culture. However the serum paraprotein was of class IgAx and could not be attributed to an abnormal population of plasma cells in the bone marrow. There was no other evidence for myeloma and the IgAx paraproteinaemia appeared to be benign, apparently unrelated to the neoplastic proliferation of hairy cells.

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Section: Discussionmentioning

confidence: 99%

Hairy Cell Leukaemia Occurring with an Unrelated Paraproteinaemia

Newell

Sattar

Hannam-Harris

et al. 1982

Scandinavian Journal of Haematology

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“…During this investigation we have utilized a technique recently developed to observe the ultrastructural localization of immunoglobulin in nine human lymphoid cell lines (Newell et al, 1980) and correlated this information with the immunoglobulin biosynthesis determined by the incorporation of 3H-leucine. The results obtained suggest that marked differences in the distribution of heavy and light chains exist in these cell lines.…”

mentioning

confidence: 99%

The differential ultrastructural localization of immunoglobulin heavy and light chains in human haematopoietic cell lines

Newell

Hannam-Harris

Karpas³

et al. 1982

Br J Haematol

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The ultrastructural localization of immunoglobulin heavy and light chains has been investigated in nine haematopoietic cell lines, using a technique which involves the treatment of lightly prefixed cells with saponin to allow penetration of the antibody‐peroxidase conjugate. The synthesis and secretion of immunoglobulin was also studied in these cell lines. Immunoglobulin was found to be localized in the cisternae and on the membranes of the rough endoplasmic reticulum, perinuclear space and/or Golgi apparatus. In each case staining for heavy chains was weak or absent in the perinuclear space while staining for light chains was usually strong. Additionally in three cell lines immunoperoxidase staining indicated that heavy chains were absent from the Golgi apparatus despite the observed presence of light chains in the Golgi apparatus and the secretion of combined immunoglobulin into the supernatant. The results obtained suggest compartmentalization of the synthesis of light and heavy chains and indicate that the technique of immunoelectron microscopy may significantly contribute to an understanding of the mechanisms involved in immunoglobulin synthesis, intracellular transport and secretion.

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Intracellular immunoglobulin G ‘Pseudocrystals’ in a patient with chronic B-cell leukemia

Ottolander

Brederoo

Schuurman

et al. 1986

Cancer

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A patient with chronic B-cell leukemia in whom the malignant lymphocytes showed intracellular inclusions of immunoglobulin (Ig) G kappa molecules is described. Electron microscopy revealed filamentous material in the nuclear envelopes and in the cisternae of the rough endoplasmic reticulum. These in vivo surface Ig-negative, nonexcreting cells could be stimulated in vitro to excrete immunoglobulin-free light chain molecules into the supernatant, which were not found in the cytoplasm after stimulation.

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The intracellular localisation of immunoglobulin in human lymphoid cells and haematopoietic cell lines by immunoperoxidase electron microscopy

Cited by 15 publications

References 9 publications

Hairy Cell Leukaemia Occurring with an Unrelated Paraproteinaemia

Hairy Cell Leukaemia Occurring with an Unrelated Paraproteinaemia

The differential ultrastructural localization of immunoglobulin heavy and light chains in human haematopoietic cell lines

Intracellular immunoglobulin G ‘Pseudocrystals’ in a patient with chronic B-cell leukemia

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