Claus Munck Petersen

Cell association and degradation of pregnancy zone protein-chymotrypsin complex in cultured human monocytes

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Cell association and degradation of pregnancy zone protein-chymotrypsin complex in cultured human monocytes. / Jensen, Poul Henning; Davidsen, O; Gliemann, J; Petersen, C M.

In: Scandinavian Journal of Clinical & Laboratory Investigation, Vol. 48, No. 2, 1988, p. 165-76.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Jensen, PH, Davidsen, O, Gliemann, J & Petersen, CM 1988, 'Cell association and degradation of pregnancy zone protein-chymotrypsin complex in cultured human monocytes', Scandinavian Journal of Clinical & Laboratory Investigation, vol. 48, no. 2, pp. 165-76.

APA

Jensen, P. H., Davidsen, O., Gliemann, J., & Petersen, C. M. (1988). Cell association and degradation of pregnancy zone protein-chymotrypsin complex in cultured human monocytes. Scandinavian Journal of Clinical & Laboratory Investigation, 48(2), 165-76.

CBE

Jensen PH, Davidsen O, Gliemann J, Petersen CM. 1988. Cell association and degradation of pregnancy zone protein-chymotrypsin complex in cultured human monocytes. Scandinavian Journal of Clinical & Laboratory Investigation. 48(2):165-76.

MLA

Jensen, Poul Henning et al. "Cell association and degradation of pregnancy zone protein-chymotrypsin complex in cultured human monocytes". Scandinavian Journal of Clinical & Laboratory Investigation. 1988, 48(2). 165-76.

Vancouver

Jensen PH, Davidsen O, Gliemann J, Petersen CM. Cell association and degradation of pregnancy zone protein-chymotrypsin complex in cultured human monocytes. Scandinavian Journal of Clinical & Laboratory Investigation. 1988;48(2):165-76.

Author

Jensen, Poul Henning ; Davidsen, O ; Gliemann, J ; Petersen, C M. / Cell association and degradation of pregnancy zone protein-chymotrypsin complex in cultured human monocytes. In: Scandinavian Journal of Clinical & Laboratory Investigation. 1988 ; Vol. 48, No. 2. pp. 165-76.

Bibtex

@article{22b62107a10444c7840626b1d76d8a44,
title = "Cell association and degradation of pregnancy zone protein-chymotrypsin complex in cultured human monocytes",
abstract = "125I-labelled pregnancy zone protein complexed with chymotrypsin (PZP-ct) bound to freshly isolated and to cultured human monocytes. Binding of uncomplexed 125I-pregnancy zone protein (PZP) was less than 20{\%} of complex binding. At 4 degrees C, labelled PZP-ct complex bound to cultured monocytes with a half-time of about 4 h. Dissociation at 4 degrees C was slow at low receptor occupancies (t 1/2 greater than 24 h). At high receptor occupancies, dissociation was biphasic (initial k-1 = 8 X 10(-3) min-1) and 85{\%} of the cell-associated label had dissociated within 24 h. At near equilibrium, binding of 20 pmol/l 125I-PZP-ct was half maximally inhibited at a ligand concentration of about 450 pmol/l. The Scatchard plot was linear giving an estimated concentration of 2 X 10(4) receptors/cell. Ligand bound at 4 degrees C was rapidly internalized at 37 degrees C (half-time = 0.5 min) and after a 5-10 min lag time, radioactivity comprising monoiodotyrosine was released into the medium following a sigmoidal curve. At 37 degrees C the uptake of 125I-PZP-ct complex was initially linear and within 15 min internalized label accumulated, reaching a steady state at about 85{\%} of the cell-associated radioactivity. Following a lag time of 15 min, radioactivity soluble in trichloroacetic acid appeared in the medium. Similar results were obtained with 125I-alpha 2-macroglobulin-trypsin complex (alpha 2M-T). It is concluded that high affinity receptors mediate binding, uptake and degradation of pregnancy zone protein--and alpha 2-macroglobulin-proteinase complex in human monocyte-macrophages.",
keywords = "Cells, Cultured, Chromatography, Gel, Chymotrypsin, Endocytosis, Humans, Low Density Lipoprotein Receptor-Related Protein-1, Monocytes, Pregnancy Proteins, Receptors, Immunologic, Trypsin, alpha-Macroglobulins",
author = "Jensen, {Poul Henning} and O Davidsen and J Gliemann and Petersen, {C M}",
year = "1988",
language = "English",
volume = "48",
pages = "165--76",
journal = "Scandinavian Journal of Clinical & Laboratory Investigation",
issn = "0036-5513",
publisher = "Taylor & francis",
number = "2",

}

RIS

TY - JOUR

T1 - Cell association and degradation of pregnancy zone protein-chymotrypsin complex in cultured human monocytes

AU - Jensen, Poul Henning

AU - Davidsen, O

AU - Gliemann, J

AU - Petersen, C M

PY - 1988

Y1 - 1988

N2 - 125I-labelled pregnancy zone protein complexed with chymotrypsin (PZP-ct) bound to freshly isolated and to cultured human monocytes. Binding of uncomplexed 125I-pregnancy zone protein (PZP) was less than 20% of complex binding. At 4 degrees C, labelled PZP-ct complex bound to cultured monocytes with a half-time of about 4 h. Dissociation at 4 degrees C was slow at low receptor occupancies (t 1/2 greater than 24 h). At high receptor occupancies, dissociation was biphasic (initial k-1 = 8 X 10(-3) min-1) and 85% of the cell-associated label had dissociated within 24 h. At near equilibrium, binding of 20 pmol/l 125I-PZP-ct was half maximally inhibited at a ligand concentration of about 450 pmol/l. The Scatchard plot was linear giving an estimated concentration of 2 X 10(4) receptors/cell. Ligand bound at 4 degrees C was rapidly internalized at 37 degrees C (half-time = 0.5 min) and after a 5-10 min lag time, radioactivity comprising monoiodotyrosine was released into the medium following a sigmoidal curve. At 37 degrees C the uptake of 125I-PZP-ct complex was initially linear and within 15 min internalized label accumulated, reaching a steady state at about 85% of the cell-associated radioactivity. Following a lag time of 15 min, radioactivity soluble in trichloroacetic acid appeared in the medium. Similar results were obtained with 125I-alpha 2-macroglobulin-trypsin complex (alpha 2M-T). It is concluded that high affinity receptors mediate binding, uptake and degradation of pregnancy zone protein--and alpha 2-macroglobulin-proteinase complex in human monocyte-macrophages.

AB - 125I-labelled pregnancy zone protein complexed with chymotrypsin (PZP-ct) bound to freshly isolated and to cultured human monocytes. Binding of uncomplexed 125I-pregnancy zone protein (PZP) was less than 20% of complex binding. At 4 degrees C, labelled PZP-ct complex bound to cultured monocytes with a half-time of about 4 h. Dissociation at 4 degrees C was slow at low receptor occupancies (t 1/2 greater than 24 h). At high receptor occupancies, dissociation was biphasic (initial k-1 = 8 X 10(-3) min-1) and 85% of the cell-associated label had dissociated within 24 h. At near equilibrium, binding of 20 pmol/l 125I-PZP-ct was half maximally inhibited at a ligand concentration of about 450 pmol/l. The Scatchard plot was linear giving an estimated concentration of 2 X 10(4) receptors/cell. Ligand bound at 4 degrees C was rapidly internalized at 37 degrees C (half-time = 0.5 min) and after a 5-10 min lag time, radioactivity comprising monoiodotyrosine was released into the medium following a sigmoidal curve. At 37 degrees C the uptake of 125I-PZP-ct complex was initially linear and within 15 min internalized label accumulated, reaching a steady state at about 85% of the cell-associated radioactivity. Following a lag time of 15 min, radioactivity soluble in trichloroacetic acid appeared in the medium. Similar results were obtained with 125I-alpha 2-macroglobulin-trypsin complex (alpha 2M-T). It is concluded that high affinity receptors mediate binding, uptake and degradation of pregnancy zone protein--and alpha 2-macroglobulin-proteinase complex in human monocyte-macrophages.

KW - Cells, Cultured

KW - Chromatography, Gel

KW - Chymotrypsin

KW - Endocytosis

KW - Humans

KW - Low Density Lipoprotein Receptor-Related Protein-1

KW - Monocytes

KW - Pregnancy Proteins

KW - Receptors, Immunologic

KW - Trypsin

KW - alpha-Macroglobulins

M3 - Journal article

C2 - 2451858

VL - 48

SP - 165

EP - 176

JO - Scandinavian Journal of Clinical & Laboratory Investigation

JF - Scandinavian Journal of Clinical & Laboratory Investigation

SN - 0036-5513

IS - 2

ER -