A marker and putative pathoantigen of Hodgkin's cells.

Elisabeth M. Paietta, R. J. Stockert, A. Morell, Janis Racevskis, P. H. Wiernik

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

A galactose-specific lectin, recently described by our laboratory, is immunologically demonstrable on the surface of neoplastic cells derived from patients with Hodgkin's disease. This Hodgkin's lectin is shown to be functionally and antigenically related to the galactose-N-acetylgalactosamine-specific lectin of the hepatocyte (HBP). Poly- and monoclonal antibodies against either the cytoplasmic tail or the cell-surface binding site of HBP recognize the Hodgkin's lectin as a 55 Kd protein. Expression of the 55 Kd antigen appears to be restricted to Hodgkin's disease involved tissues and cells of the monocyte/macrophage lineage. The putative identification of the Hodgkin's lectin as an ectosialyltransferase unique to Hodgkin's cells is supported by inhibition of enzymatic activity by anti-HBP antibodies. Cultured Hodgkin's cells, in analogy to purified HBP, agglutinate T-lymphocytes mediated by the Hodgkin's lectin. This cell-to-cell interaction results in the incorporation of sialic acid into lymphocyte surface asialoglycans as well as in the stimulation of lymphocyte proliferation. The function of the Hodgkin's lectin as lymphocyte agglutinant in vitro suggests its role as an immunomodulator contributing to the immunodeficiencies associated with Hodgkin's disease.

Original languageEnglish (US)
Pages (from-to)91-98
Number of pages8
JournalRecent results in cancer research. Fortschritte der Krebsforschung. Progres dans les recherches sur le cancer
Volume117
StatePublished - 1989

Fingerprint

Hodgkin Disease
Lectins
Galactose
Lymphocytes
Sialyltransferases
Acetylgalactosamine
Immunologic Factors
N-Acetylneuraminic Acid
Lymphocyte Activation
Cell Communication
Monocytes
Anti-Idiotypic Antibodies
Hepatocytes
Cultured Cells
Macrophages
Binding Sites
Monoclonal Antibodies
T-Lymphocytes
Antigens

ASJC Scopus subject areas

  • Medicine(all)

Cite this

@article{ef906e4b102a4542a1f79a78d4aee5cb,
title = "A marker and putative pathoantigen of Hodgkin's cells.",
abstract = "A galactose-specific lectin, recently described by our laboratory, is immunologically demonstrable on the surface of neoplastic cells derived from patients with Hodgkin's disease. This Hodgkin's lectin is shown to be functionally and antigenically related to the galactose-N-acetylgalactosamine-specific lectin of the hepatocyte (HBP). Poly- and monoclonal antibodies against either the cytoplasmic tail or the cell-surface binding site of HBP recognize the Hodgkin's lectin as a 55 Kd protein. Expression of the 55 Kd antigen appears to be restricted to Hodgkin's disease involved tissues and cells of the monocyte/macrophage lineage. The putative identification of the Hodgkin's lectin as an ectosialyltransferase unique to Hodgkin's cells is supported by inhibition of enzymatic activity by anti-HBP antibodies. Cultured Hodgkin's cells, in analogy to purified HBP, agglutinate T-lymphocytes mediated by the Hodgkin's lectin. This cell-to-cell interaction results in the incorporation of sialic acid into lymphocyte surface asialoglycans as well as in the stimulation of lymphocyte proliferation. The function of the Hodgkin's lectin as lymphocyte agglutinant in vitro suggests its role as an immunomodulator contributing to the immunodeficiencies associated with Hodgkin's disease.",
author = "Paietta, {Elisabeth M.} and Stockert, {R. J.} and A. Morell and Janis Racevskis and Wiernik, {P. H.}",
year = "1989",
language = "English (US)",
volume = "117",
pages = "91--98",
journal = "Recent Results in Cancer Research",
issn = "0080-0015",
publisher = "Springer New York",

}

TY - JOUR

T1 - A marker and putative pathoantigen of Hodgkin's cells.

AU - Paietta, Elisabeth M.

AU - Stockert, R. J.

AU - Morell, A.

AU - Racevskis, Janis

AU - Wiernik, P. H.

PY - 1989

Y1 - 1989

N2 - A galactose-specific lectin, recently described by our laboratory, is immunologically demonstrable on the surface of neoplastic cells derived from patients with Hodgkin's disease. This Hodgkin's lectin is shown to be functionally and antigenically related to the galactose-N-acetylgalactosamine-specific lectin of the hepatocyte (HBP). Poly- and monoclonal antibodies against either the cytoplasmic tail or the cell-surface binding site of HBP recognize the Hodgkin's lectin as a 55 Kd protein. Expression of the 55 Kd antigen appears to be restricted to Hodgkin's disease involved tissues and cells of the monocyte/macrophage lineage. The putative identification of the Hodgkin's lectin as an ectosialyltransferase unique to Hodgkin's cells is supported by inhibition of enzymatic activity by anti-HBP antibodies. Cultured Hodgkin's cells, in analogy to purified HBP, agglutinate T-lymphocytes mediated by the Hodgkin's lectin. This cell-to-cell interaction results in the incorporation of sialic acid into lymphocyte surface asialoglycans as well as in the stimulation of lymphocyte proliferation. The function of the Hodgkin's lectin as lymphocyte agglutinant in vitro suggests its role as an immunomodulator contributing to the immunodeficiencies associated with Hodgkin's disease.

AB - A galactose-specific lectin, recently described by our laboratory, is immunologically demonstrable on the surface of neoplastic cells derived from patients with Hodgkin's disease. This Hodgkin's lectin is shown to be functionally and antigenically related to the galactose-N-acetylgalactosamine-specific lectin of the hepatocyte (HBP). Poly- and monoclonal antibodies against either the cytoplasmic tail or the cell-surface binding site of HBP recognize the Hodgkin's lectin as a 55 Kd protein. Expression of the 55 Kd antigen appears to be restricted to Hodgkin's disease involved tissues and cells of the monocyte/macrophage lineage. The putative identification of the Hodgkin's lectin as an ectosialyltransferase unique to Hodgkin's cells is supported by inhibition of enzymatic activity by anti-HBP antibodies. Cultured Hodgkin's cells, in analogy to purified HBP, agglutinate T-lymphocytes mediated by the Hodgkin's lectin. This cell-to-cell interaction results in the incorporation of sialic acid into lymphocyte surface asialoglycans as well as in the stimulation of lymphocyte proliferation. The function of the Hodgkin's lectin as lymphocyte agglutinant in vitro suggests its role as an immunomodulator contributing to the immunodeficiencies associated with Hodgkin's disease.

UR - http://www.scopus.com/inward/record.url?scp=0024838645&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024838645&partnerID=8YFLogxK

M3 - Article

C2 - 2690234

AN - SCOPUS:0024838645

VL - 117

SP - 91

EP - 98

JO - Recent Results in Cancer Research

JF - Recent Results in Cancer Research

SN - 0080-0015

ER -