Breast carcinoma epithelial cells express a very low-density lipoprotein receptor variant lacking the O-linked glycosylation domain encoded by exon 16, but with full binding activity for serine proteinase/serpin complexes and Mr-40,000 receptor-associated protein

P M Martensen; K Oka; L Christensen; P M Rettenberger; H H Petersen; A Christensen; L Chan; C W Heegaard; P A Andreasen

Breast carcinoma epithelial cells express a very low-density lipoprotein receptor variant lacking the O-linked glycosylation domain encoded by exon 16, but with full binding activity for serine proteinase/serpin complexes and Mr-40,000 receptor-associated protein

P M Martensen, K Oka, L Christensen, P M Rettenberger, H H Petersen, A Christensen, L Chan, C W Heegaard, P A Andreasen

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

32 Citationer (Scopus)

Abstract

Very-low density lipoprotein receptor (VLDLR) belongs to the low-density lipoprotein receptor family of endocytosis receptors. It binds a variety of different ligands, including apolipoprotein E, Mr-40,000 receptor-associated-protein (RAP), and some serine proteinase/serpin complexes. We previously demonstrated the occurrence of two forms of VLDLR in SDS/PAGE, migrating with Mr 105,000 and Mr 130,000, respectively [Heegaard, C. W., Simonsen, A. C. W., Oka, K., Kjøller, L., Christensen, A., Madsen, B., Ellgaard, L., Chan, L. & Andreasen, P. A. (1995) J. Biol. Chem. 270, 20,855-20,869]. We now demonstrate that these two forms correspond to forms with the absence (type-II) and presence (type-I) of the O-linked glycosylation domain encoded by exon 16, respectively. We show that the two forms have the same binding affinity to RAP and serine proteinase/serpin complexes. Using reverse transcription and PCR, we demonstrate that the splice variation giving rise to the two forms is highly cell specific. In particular, we demonstrate that human breast carcinomas express predominantly or exclusively the variant lacking exon 16. By immunohistochemistry, we demonstrate that VLDLR is mainly expressed by the epithelial cancer cells in these carcinomas. The VLDLR variant expressed by epithelial cancer cells could function in the clearance of cell-surface-associated serine proteinase/serpin complexes in breast carcinomas.

Originalsprog	Engelsk
Tidsskrift	European Journal of Biochemistry
Vol/bind	248
Nummer	2
Sider (fra-til)	583-91
Antal sider	9
ISSN	0014-2956
Status	Udgivet - 1 sep. 1997

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Citationsformater

Martensen, P. M., Oka, K., Christensen, L., Rettenberger, P. M., Petersen, H. H., Christensen, A., Chan, L., Heegaard, C. W., & Andreasen, P. A. (1997). Breast carcinoma epithelial cells express a very low-density lipoprotein receptor variant lacking the O-linked glycosylation domain encoded by exon 16, but with full binding activity for serine proteinase/serpin complexes and Mr-40,000 receptor-associated protein. European Journal of Biochemistry, 248(2), 583-91.

Martensen, P M ; Oka, K ; Christensen, L et al. / Breast carcinoma epithelial cells express a very low-density lipoprotein receptor variant lacking the O-linked glycosylation domain encoded by exon 16, but with full binding activity for serine proteinase/serpin complexes and Mr-40,000 receptor-associated protein. I: European Journal of Biochemistry. 1997 ; Bind 248, Nr. 2. s. 583-91.

@article{660a832ea6664e56a4df9a94116eb0bb,

title = "Breast carcinoma epithelial cells express a very low-density lipoprotein receptor variant lacking the O-linked glycosylation domain encoded by exon 16, but with full binding activity for serine proteinase/serpin complexes and Mr-40,000 receptor-associated protein",

abstract = "Very-low density lipoprotein receptor (VLDLR) belongs to the low-density lipoprotein receptor family of endocytosis receptors. It binds a variety of different ligands, including apolipoprotein E, Mr-40,000 receptor-associated-protein (RAP), and some serine proteinase/serpin complexes. We previously demonstrated the occurrence of two forms of VLDLR in SDS/PAGE, migrating with Mr 105,000 and Mr 130,000, respectively [Heegaard, C. W., Simonsen, A. C. W., Oka, K., Kj{\o}ller, L., Christensen, A., Madsen, B., Ellgaard, L., Chan, L. & Andreasen, P. A. (1995) J. Biol. Chem. 270, 20,855-20,869]. We now demonstrate that these two forms correspond to forms with the absence (type-II) and presence (type-I) of the O-linked glycosylation domain encoded by exon 16, respectively. We show that the two forms have the same binding affinity to RAP and serine proteinase/serpin complexes. Using reverse transcription and PCR, we demonstrate that the splice variation giving rise to the two forms is highly cell specific. In particular, we demonstrate that human breast carcinomas express predominantly or exclusively the variant lacking exon 16. By immunohistochemistry, we demonstrate that VLDLR is mainly expressed by the epithelial cancer cells in these carcinomas. The VLDLR variant expressed by epithelial cancer cells could function in the clearance of cell-surface-associated serine proteinase/serpin complexes in breast carcinomas.",

keywords = "Amino Acid Sequence, Animals, Base Sequence, Breast Neoplasms/metabolism, Carbohydrate Conformation, Carcinoma/metabolism, Endocytosis, Epithelium, Exons, Glycosylation, Humans, Immunohistochemistry, Mammary Neoplasms, Animal/metabolism, Membrane Proteins/metabolism, Molecular Sequence Data, Rabbits, Receptors, LDL/chemistry, Serine Endopeptidases/metabolism, Serpins/metabolism, Tumor Cells, Cultured",

author = "Martensen, {P M} and K Oka and L Christensen and Rettenberger, {P M} and Petersen, {H H} and A Christensen and L Chan and Heegaard, {C W} and Andreasen, {P A}",

year = "1997",

month = sep,

day = "1",

language = "English",

volume = "248",

pages = "583--91",

journal = "European Journal of Biochemistry",

issn = "0014-2956",

publisher = "Wiley-Blackwell Publishing Ltd",

number = "2",

}

Martensen, PM, Oka, K, Christensen, L, Rettenberger, PM, Petersen, HH, Christensen, A, Chan, L, Heegaard, CW & Andreasen, PA 1997, 'Breast carcinoma epithelial cells express a very low-density lipoprotein receptor variant lacking the O-linked glycosylation domain encoded by exon 16, but with full binding activity for serine proteinase/serpin complexes and Mr-40,000 receptor-associated protein', European Journal of Biochemistry, bind 248, nr. 2, s. 583-91.

Breast carcinoma epithelial cells express a very low-density lipoprotein receptor variant lacking the O-linked glycosylation domain encoded by exon 16, but with full binding activity for serine proteinase/serpin complexes and Mr-40,000 receptor-associated protein. / Martensen, P M; Oka, K; Christensen, L et al.
I: European Journal of Biochemistry, Bind 248, Nr. 2, 01.09.1997, s. 583-91.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

TY - JOUR

T1 - Breast carcinoma epithelial cells express a very low-density lipoprotein receptor variant lacking the O-linked glycosylation domain encoded by exon 16, but with full binding activity for serine proteinase/serpin complexes and Mr-40,000 receptor-associated protein

AU - Martensen, P M

AU - Oka, K

AU - Christensen, L

AU - Rettenberger, P M

AU - Petersen, H H

AU - Christensen, A

AU - Chan, L

AU - Heegaard, C W

AU - Andreasen, P A

PY - 1997/9/1

Y1 - 1997/9/1

N2 - Very-low density lipoprotein receptor (VLDLR) belongs to the low-density lipoprotein receptor family of endocytosis receptors. It binds a variety of different ligands, including apolipoprotein E, Mr-40,000 receptor-associated-protein (RAP), and some serine proteinase/serpin complexes. We previously demonstrated the occurrence of two forms of VLDLR in SDS/PAGE, migrating with Mr 105,000 and Mr 130,000, respectively [Heegaard, C. W., Simonsen, A. C. W., Oka, K., Kjøller, L., Christensen, A., Madsen, B., Ellgaard, L., Chan, L. & Andreasen, P. A. (1995) J. Biol. Chem. 270, 20,855-20,869]. We now demonstrate that these two forms correspond to forms with the absence (type-II) and presence (type-I) of the O-linked glycosylation domain encoded by exon 16, respectively. We show that the two forms have the same binding affinity to RAP and serine proteinase/serpin complexes. Using reverse transcription and PCR, we demonstrate that the splice variation giving rise to the two forms is highly cell specific. In particular, we demonstrate that human breast carcinomas express predominantly or exclusively the variant lacking exon 16. By immunohistochemistry, we demonstrate that VLDLR is mainly expressed by the epithelial cancer cells in these carcinomas. The VLDLR variant expressed by epithelial cancer cells could function in the clearance of cell-surface-associated serine proteinase/serpin complexes in breast carcinomas.

AB - Very-low density lipoprotein receptor (VLDLR) belongs to the low-density lipoprotein receptor family of endocytosis receptors. It binds a variety of different ligands, including apolipoprotein E, Mr-40,000 receptor-associated-protein (RAP), and some serine proteinase/serpin complexes. We previously demonstrated the occurrence of two forms of VLDLR in SDS/PAGE, migrating with Mr 105,000 and Mr 130,000, respectively [Heegaard, C. W., Simonsen, A. C. W., Oka, K., Kjøller, L., Christensen, A., Madsen, B., Ellgaard, L., Chan, L. & Andreasen, P. A. (1995) J. Biol. Chem. 270, 20,855-20,869]. We now demonstrate that these two forms correspond to forms with the absence (type-II) and presence (type-I) of the O-linked glycosylation domain encoded by exon 16, respectively. We show that the two forms have the same binding affinity to RAP and serine proteinase/serpin complexes. Using reverse transcription and PCR, we demonstrate that the splice variation giving rise to the two forms is highly cell specific. In particular, we demonstrate that human breast carcinomas express predominantly or exclusively the variant lacking exon 16. By immunohistochemistry, we demonstrate that VLDLR is mainly expressed by the epithelial cancer cells in these carcinomas. The VLDLR variant expressed by epithelial cancer cells could function in the clearance of cell-surface-associated serine proteinase/serpin complexes in breast carcinomas.

KW - Amino Acid Sequence

KW - Animals

KW - Base Sequence

KW - Breast Neoplasms/metabolism

KW - Carbohydrate Conformation

KW - Carcinoma/metabolism

KW - Endocytosis

KW - Epithelium

KW - Exons

KW - Glycosylation

KW - Humans

KW - Immunohistochemistry

KW - Mammary Neoplasms, Animal/metabolism

KW - Membrane Proteins/metabolism

KW - Molecular Sequence Data

KW - Rabbits

KW - Receptors, LDL/chemistry

KW - Serine Endopeptidases/metabolism

KW - Serpins/metabolism

KW - Tumor Cells, Cultured

M3 - Journal article

C2 - 9346319

SN - 0014-2956

VL - 248

SP - 583

EP - 591

JO - European Journal of Biochemistry

JF - European Journal of Biochemistry

IS - 2

ER -

Martensen PM, Oka K, Christensen L, Rettenberger PM, Petersen HH, Christensen A et al. Breast carcinoma epithelial cells express a very low-density lipoprotein receptor variant lacking the O-linked glycosylation domain encoded by exon 16, but with full binding activity for serine proteinase/serpin complexes and Mr-40,000 receptor-associated protein. European Journal of Biochemistry. 1997 sep. 1;248(2):583-91.