Human β2-microglobulin is a substrate of tissue transglutaminase: Polymerization in solution and on the cell surface

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Abstract

Incubation of purified human β2-microglobulin (B2-m) with tissue transglutaminase (Tgase) resulted in the formation of high molecular weight polymers revealed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. In the presence of 30 mM [14C]methylamine, the polymer formation was prevented, but incorporation of methylamine into β2-m (equal to 1 methylamine per 1 molecule) could be observed. From the sheddings of peripheral blood mononuclear cells occurring in the presence of Tgase, it is apparent that anti-β2-m immunoadsorbent removed, in addition to human leukocyte antigen (HLA) and β2-m, some other proteins. The enzyme could incorporate [14C]methylamine into β2-m of the shedding cells. On addition of rabbit anti-human β2-m antibody, followed by fluoresceine-labeled goat anti-rabbit IgG antibody to human mononuclear blood cells, the otherwise homogeneous distribution of fluorescence turned into spots and patches on cells previously incubated with Tgase or Ca2+-ionophore A23187.

Original languageEnglish
Pages (from-to)706-710
Number of pages5
JournalJournal of Cell Biology
Volume89
Issue number3
Publication statusPublished - 1981

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Polymerization
Transglutaminases
Blood Cells
Polymers
Rabbits
Immunosorbents
Antibodies
Ionophores
Calcimycin
HLA Antigens
Goats
Sodium Dodecyl Sulfate
Polyacrylamide Gel Electrophoresis
Molecular Weight
Fluorescence
methylamine
transglutaminase 2
Enzymes
Proteins

ASJC Scopus subject areas

  • Cell Biology

Cite this

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title = "Human β2-microglobulin is a substrate of tissue transglutaminase: Polymerization in solution and on the cell surface",
abstract = "Incubation of purified human β2-microglobulin (B2-m) with tissue transglutaminase (Tgase) resulted in the formation of high molecular weight polymers revealed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. In the presence of 30 mM [14C]methylamine, the polymer formation was prevented, but incorporation of methylamine into β2-m (equal to 1 methylamine per 1 molecule) could be observed. From the sheddings of peripheral blood mononuclear cells occurring in the presence of Tgase, it is apparent that anti-β2-m immunoadsorbent removed, in addition to human leukocyte antigen (HLA) and β2-m, some other proteins. The enzyme could incorporate [14C]methylamine into β2-m of the shedding cells. On addition of rabbit anti-human β2-m antibody, followed by fluoresceine-labeled goat anti-rabbit IgG antibody to human mononuclear blood cells, the otherwise homogeneous distribution of fluorescence turned into spots and patches on cells previously incubated with Tgase or Ca2+-ionophore A23187.",
author = "L. F{\'e}s{\"u}s and A. Falus and A. Erdei and K. Laki",
year = "1981",
language = "English",
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pages = "706--710",
journal = "Journal of Cell Biology",
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T1 - Human β2-microglobulin is a substrate of tissue transglutaminase

T2 - Polymerization in solution and on the cell surface

AU - Fésüs, L.

AU - Falus, A.

AU - Erdei, A.

AU - Laki, K.

PY - 1981

Y1 - 1981

N2 - Incubation of purified human β2-microglobulin (B2-m) with tissue transglutaminase (Tgase) resulted in the formation of high molecular weight polymers revealed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. In the presence of 30 mM [14C]methylamine, the polymer formation was prevented, but incorporation of methylamine into β2-m (equal to 1 methylamine per 1 molecule) could be observed. From the sheddings of peripheral blood mononuclear cells occurring in the presence of Tgase, it is apparent that anti-β2-m immunoadsorbent removed, in addition to human leukocyte antigen (HLA) and β2-m, some other proteins. The enzyme could incorporate [14C]methylamine into β2-m of the shedding cells. On addition of rabbit anti-human β2-m antibody, followed by fluoresceine-labeled goat anti-rabbit IgG antibody to human mononuclear blood cells, the otherwise homogeneous distribution of fluorescence turned into spots and patches on cells previously incubated with Tgase or Ca2+-ionophore A23187.

AB - Incubation of purified human β2-microglobulin (B2-m) with tissue transglutaminase (Tgase) resulted in the formation of high molecular weight polymers revealed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. In the presence of 30 mM [14C]methylamine, the polymer formation was prevented, but incorporation of methylamine into β2-m (equal to 1 methylamine per 1 molecule) could be observed. From the sheddings of peripheral blood mononuclear cells occurring in the presence of Tgase, it is apparent that anti-β2-m immunoadsorbent removed, in addition to human leukocyte antigen (HLA) and β2-m, some other proteins. The enzyme could incorporate [14C]methylamine into β2-m of the shedding cells. On addition of rabbit anti-human β2-m antibody, followed by fluoresceine-labeled goat anti-rabbit IgG antibody to human mononuclear blood cells, the otherwise homogeneous distribution of fluorescence turned into spots and patches on cells previously incubated with Tgase or Ca2+-ionophore A23187.

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