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Epithelial glycoprotein-330 mediates endocytosis of plasminogen activator-plasminogen activator inhibitor type-1 complexes

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Epithelial glycoprotein-330 mediates endocytosis of plasminogen activator-plasminogen activator inhibitor type-1 complexes. / Moestrup, S K; Nielsen, Susanne; Andreasen, P; Jørgensen, K E; Nykjaer, A; Røigaard, H; Gliemann, J; Christensen, E I.

In: Journal of Biological Chemistry, Vol. 268, No. 22, 05.08.1993, p. 16564-16570.

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

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Moestrup SK, Nielsen S, Andreasen P, Jørgensen KE, Nykjaer A, Røigaard H et al. Epithelial glycoprotein-330 mediates endocytosis of plasminogen activator-plasminogen activator inhibitor type-1 complexes. Journal of Biological Chemistry. 1993 Aug 5;268(22):16564-16570.

Author

Moestrup, S K ; Nielsen, Susanne ; Andreasen, P ; Jørgensen, K E ; Nykjaer, A ; Røigaard, H ; Gliemann, J ; Christensen, E I. / Epithelial glycoprotein-330 mediates endocytosis of plasminogen activator-plasminogen activator inhibitor type-1 complexes. In: Journal of Biological Chemistry. 1993 ; Vol. 268, No. 22. pp. 16564-16570.

Bibtex

@article{b629980650fa41ab99446e922f32f54f,
title = "Epithelial glycoprotein-330 mediates endocytosis of plasminogen activator-plasminogen activator inhibitor type-1 complexes",
abstract = "Epithelial glycoprotein 330 (gp330) is structurally similar to the multifunctional alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein (alpha 2MR/LRP), gp330 and alpha 2MR/LRP bind Ca2+ with high affinity, and both receptors bind and mediate endocytosis of alpha 2MR-associated protein (RAP). In the present report, we describe that affinity-purified gp330 from rabbit renal cortex binds plasminogen activator inhibitor type-1 (PAI-1) complexed with urokinase-type plasminogen activator (uPA). alpha 2M-methylamine, which binds with high affinity to alpha 2MR/LRP, did not bind to gp330. The apparent Kd for binding of uPA.PAI-1 complexes was about 0.8 nM at 4 degrees C. The binding was calcium-dependent and inhibited by recombinant RAP (rRAP) and tissue type plasminogen activator-PAI-1 complexes. Thin sections of rabbit renal proximal tubules bound 125I-labeled uPA.PAI-1 and rRAP in the apical part of proximal tubules corresponding to the localization of gp330. The binding of 125I-uPA.PAI-1 complexes in tubules was abolished by excess unlabeled rRAP, and a rRAP-inhibitable endocytosis and degradation of labeled uPA.PAI-1 complexes was demonstrated by perfusion of isolated rabbit proximal tubules. The results establish an endocytotic function of gp330 and suggest that gp330 is an important component of the fibrinolytic system in gp330-containing epithelial as found in, for example, kidney and lung.",
keywords = "Amino Acid Sequence, Animals, Autoantigens, Calcium, Cell Line, Chromatography, High Pressure Liquid, Endocytosis, Epithelium, Heymann Nephritis Antigenic Complex, Humans, Kidney Glomerulus, Kidney Tubules, Proximal, Kinetics, Membrane Glycoproteins, Molecular Sequence Data, Nevirapine, Plasminogen Activator Inhibitor 1, Pyridines, Rabbits",
author = "Moestrup, {S K} and Susanne Nielsen and P Andreasen and J{\o}rgensen, {K E} and A Nykjaer and H R{\o}igaard and J Gliemann and Christensen, {E I}",
year = "1993",
month = aug,
day = "5",
language = "English",
volume = "268",
pages = "16564--16570",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "22",

}

RIS

TY - JOUR

T1 - Epithelial glycoprotein-330 mediates endocytosis of plasminogen activator-plasminogen activator inhibitor type-1 complexes

AU - Moestrup, S K

AU - Nielsen, Susanne

AU - Andreasen, P

AU - Jørgensen, K E

AU - Nykjaer, A

AU - Røigaard, H

AU - Gliemann, J

AU - Christensen, E I

PY - 1993/8/5

Y1 - 1993/8/5

N2 - Epithelial glycoprotein 330 (gp330) is structurally similar to the multifunctional alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein (alpha 2MR/LRP), gp330 and alpha 2MR/LRP bind Ca2+ with high affinity, and both receptors bind and mediate endocytosis of alpha 2MR-associated protein (RAP). In the present report, we describe that affinity-purified gp330 from rabbit renal cortex binds plasminogen activator inhibitor type-1 (PAI-1) complexed with urokinase-type plasminogen activator (uPA). alpha 2M-methylamine, which binds with high affinity to alpha 2MR/LRP, did not bind to gp330. The apparent Kd for binding of uPA.PAI-1 complexes was about 0.8 nM at 4 degrees C. The binding was calcium-dependent and inhibited by recombinant RAP (rRAP) and tissue type plasminogen activator-PAI-1 complexes. Thin sections of rabbit renal proximal tubules bound 125I-labeled uPA.PAI-1 and rRAP in the apical part of proximal tubules corresponding to the localization of gp330. The binding of 125I-uPA.PAI-1 complexes in tubules was abolished by excess unlabeled rRAP, and a rRAP-inhibitable endocytosis and degradation of labeled uPA.PAI-1 complexes was demonstrated by perfusion of isolated rabbit proximal tubules. The results establish an endocytotic function of gp330 and suggest that gp330 is an important component of the fibrinolytic system in gp330-containing epithelial as found in, for example, kidney and lung.

AB - Epithelial glycoprotein 330 (gp330) is structurally similar to the multifunctional alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein (alpha 2MR/LRP), gp330 and alpha 2MR/LRP bind Ca2+ with high affinity, and both receptors bind and mediate endocytosis of alpha 2MR-associated protein (RAP). In the present report, we describe that affinity-purified gp330 from rabbit renal cortex binds plasminogen activator inhibitor type-1 (PAI-1) complexed with urokinase-type plasminogen activator (uPA). alpha 2M-methylamine, which binds with high affinity to alpha 2MR/LRP, did not bind to gp330. The apparent Kd for binding of uPA.PAI-1 complexes was about 0.8 nM at 4 degrees C. The binding was calcium-dependent and inhibited by recombinant RAP (rRAP) and tissue type plasminogen activator-PAI-1 complexes. Thin sections of rabbit renal proximal tubules bound 125I-labeled uPA.PAI-1 and rRAP in the apical part of proximal tubules corresponding to the localization of gp330. The binding of 125I-uPA.PAI-1 complexes in tubules was abolished by excess unlabeled rRAP, and a rRAP-inhibitable endocytosis and degradation of labeled uPA.PAI-1 complexes was demonstrated by perfusion of isolated rabbit proximal tubules. The results establish an endocytotic function of gp330 and suggest that gp330 is an important component of the fibrinolytic system in gp330-containing epithelial as found in, for example, kidney and lung.

KW - Amino Acid Sequence

KW - Animals

KW - Autoantigens

KW - Calcium

KW - Cell Line

KW - Chromatography, High Pressure Liquid

KW - Endocytosis

KW - Epithelium

KW - Heymann Nephritis Antigenic Complex

KW - Humans

KW - Kidney Glomerulus

KW - Kidney Tubules, Proximal

KW - Kinetics

KW - Membrane Glycoproteins

KW - Molecular Sequence Data

KW - Nevirapine

KW - Plasminogen Activator Inhibitor 1

KW - Pyridines

KW - Rabbits

M3 - Journal article

C2 - 8344937

VL - 268

SP - 16564

EP - 16570

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 22

ER -