Hepatocyte growth factor activator inhibitor-1 has a complex subcellular itinerary.

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Hepatocyte growth factor activator inhibitor-1 has a complex subcellular itinerary. / Godiksen, Sine; Selzer-Plon, Joanna; Pedersen, Esben D K; Abell, Kathrine; Rasmussen, Hanne B; Szabo, Roman; Bugge, Thomas H; Vogel, Lotte K.

In: Biochemical Journal, Vol. 413, No. 2, 2008, p. 251-9.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Godiksen, S, Selzer-Plon, J, Pedersen, EDK, Abell, K, Rasmussen, HB, Szabo, R, Bugge, TH & Vogel, LK 2008, 'Hepatocyte growth factor activator inhibitor-1 has a complex subcellular itinerary.', Biochemical Journal, vol. 413, no. 2, pp. 251-9. https://doi.org/10.1042/BJ20071496

APA

Godiksen, S., Selzer-Plon, J., Pedersen, E. D. K., Abell, K., Rasmussen, H. B., Szabo, R., ... Vogel, L. K. (2008). Hepatocyte growth factor activator inhibitor-1 has a complex subcellular itinerary. Biochemical Journal, 413(2), 251-9. https://doi.org/10.1042/BJ20071496

Vancouver

Godiksen S, Selzer-Plon J, Pedersen EDK, Abell K, Rasmussen HB, Szabo R et al. Hepatocyte growth factor activator inhibitor-1 has a complex subcellular itinerary. Biochemical Journal. 2008;413(2):251-9. https://doi.org/10.1042/BJ20071496

Author

Godiksen, Sine ; Selzer-Plon, Joanna ; Pedersen, Esben D K ; Abell, Kathrine ; Rasmussen, Hanne B ; Szabo, Roman ; Bugge, Thomas H ; Vogel, Lotte K. / Hepatocyte growth factor activator inhibitor-1 has a complex subcellular itinerary. In: Biochemical Journal. 2008 ; Vol. 413, No. 2. pp. 251-9.

Bibtex

@article{713de4f084bd11dd81b0000ea68e967b,
title = "Hepatocyte growth factor activator inhibitor-1 has a complex subcellular itinerary.",
abstract = "HAI-1 [HGF (hepatocyte growth factor) activator inhibitor-1] is a Kunitz-type transmembrane serine protease inhibitor that forms inhibitor complexes with the trypsin-like serine protease, matriptase. HAI-1 is essential for mouse placental development and embryo survival and together with matriptase it is a key regulator of carcinogenesis. HAI-1 is expressed in polarized epithelial cells, which have the plasma membrane divided by tight junctions into an apical and a basolateral domain. In the present study we show that HAI-1 at steady-state is mainly located on the basolateral membrane of both Madin-Darby canine kidney cells and mammary gland epithelial cells. After biosynthesis, HAI-1 is exocytosed mainly to the basolateral plasma membrane from where 15{\%} of the HAI-1 molecules are proteolytically cleaved and released into the basolateral medium. The remaining membrane-associated HAI-1 is endocytosed and then recycles between the basolateral plasma membrane and endosomes for hours until it is transcytosed to the apical plasma membrane. Minor amounts of HAI-1 present at the apical plasma membrane are proteolytically cleaved and released into the apical medium. Full-length membrane-bound HAI-1 has a half-life of 1.5 h and is eventually degraded in the lysosomes, whereas proteolytically released HAI-1 is more stable. HAI-1 is co-localized with its cognate protease, matriptase, at the basolateral plasma membrane. We suggest that HAI-1, in addition to its protease inhibitory function, plays a role in transporting matriptase as a matriptase-HAI-1 complex from the basolateral plama membrane to the apical plasma membrane, as matriptase is known to interact with prostasin, located at the apical plasma membrane.",
author = "Sine Godiksen and Joanna Selzer-Plon and Pedersen, {Esben D K} and Kathrine Abell and Rasmussen, {Hanne B} and Roman Szabo and Bugge, {Thomas H} and Vogel, {Lotte K.}",
note = "Keywords: Animals; Cell Line; Cell Membrane; Dogs; Endocytosis; Exocytosis; Gene Expression Regulation; Lysosomes; Mammary Glands, Animal; Membrane Glycoproteins; Mice; Models, Biological; Protein Transport; Serine Endopeptidases",
year = "2008",
doi = "10.1042/BJ20071496",
language = "English",
volume = "413",
pages = "251--9",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "2",

}

RIS

TY - JOUR

T1 - Hepatocyte growth factor activator inhibitor-1 has a complex subcellular itinerary.

AU - Godiksen, Sine

AU - Selzer-Plon, Joanna

AU - Pedersen, Esben D K

AU - Abell, Kathrine

AU - Rasmussen, Hanne B

AU - Szabo, Roman

AU - Bugge, Thomas H

AU - Vogel, Lotte K.

N1 - Keywords: Animals; Cell Line; Cell Membrane; Dogs; Endocytosis; Exocytosis; Gene Expression Regulation; Lysosomes; Mammary Glands, Animal; Membrane Glycoproteins; Mice; Models, Biological; Protein Transport; Serine Endopeptidases

PY - 2008

Y1 - 2008

N2 - HAI-1 [HGF (hepatocyte growth factor) activator inhibitor-1] is a Kunitz-type transmembrane serine protease inhibitor that forms inhibitor complexes with the trypsin-like serine protease, matriptase. HAI-1 is essential for mouse placental development and embryo survival and together with matriptase it is a key regulator of carcinogenesis. HAI-1 is expressed in polarized epithelial cells, which have the plasma membrane divided by tight junctions into an apical and a basolateral domain. In the present study we show that HAI-1 at steady-state is mainly located on the basolateral membrane of both Madin-Darby canine kidney cells and mammary gland epithelial cells. After biosynthesis, HAI-1 is exocytosed mainly to the basolateral plasma membrane from where 15% of the HAI-1 molecules are proteolytically cleaved and released into the basolateral medium. The remaining membrane-associated HAI-1 is endocytosed and then recycles between the basolateral plasma membrane and endosomes for hours until it is transcytosed to the apical plasma membrane. Minor amounts of HAI-1 present at the apical plasma membrane are proteolytically cleaved and released into the apical medium. Full-length membrane-bound HAI-1 has a half-life of 1.5 h and is eventually degraded in the lysosomes, whereas proteolytically released HAI-1 is more stable. HAI-1 is co-localized with its cognate protease, matriptase, at the basolateral plasma membrane. We suggest that HAI-1, in addition to its protease inhibitory function, plays a role in transporting matriptase as a matriptase-HAI-1 complex from the basolateral plama membrane to the apical plasma membrane, as matriptase is known to interact with prostasin, located at the apical plasma membrane.

AB - HAI-1 [HGF (hepatocyte growth factor) activator inhibitor-1] is a Kunitz-type transmembrane serine protease inhibitor that forms inhibitor complexes with the trypsin-like serine protease, matriptase. HAI-1 is essential for mouse placental development and embryo survival and together with matriptase it is a key regulator of carcinogenesis. HAI-1 is expressed in polarized epithelial cells, which have the plasma membrane divided by tight junctions into an apical and a basolateral domain. In the present study we show that HAI-1 at steady-state is mainly located on the basolateral membrane of both Madin-Darby canine kidney cells and mammary gland epithelial cells. After biosynthesis, HAI-1 is exocytosed mainly to the basolateral plasma membrane from where 15% of the HAI-1 molecules are proteolytically cleaved and released into the basolateral medium. The remaining membrane-associated HAI-1 is endocytosed and then recycles between the basolateral plasma membrane and endosomes for hours until it is transcytosed to the apical plasma membrane. Minor amounts of HAI-1 present at the apical plasma membrane are proteolytically cleaved and released into the apical medium. Full-length membrane-bound HAI-1 has a half-life of 1.5 h and is eventually degraded in the lysosomes, whereas proteolytically released HAI-1 is more stable. HAI-1 is co-localized with its cognate protease, matriptase, at the basolateral plasma membrane. We suggest that HAI-1, in addition to its protease inhibitory function, plays a role in transporting matriptase as a matriptase-HAI-1 complex from the basolateral plama membrane to the apical plasma membrane, as matriptase is known to interact with prostasin, located at the apical plasma membrane.

U2 - 10.1042/BJ20071496

DO - 10.1042/BJ20071496

M3 - Journal article

C2 - 18402552

VL - 413

SP - 251

EP - 259

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 2

ER -

ID: 6093317