Jens Christian Jensenius

Recombinant expression of human mannan-binding lectin

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

Standard

Recombinant expression of human mannan-binding lectin. / Vorup-Jensen, T; Sørensen, Esben Skipper; Jensen, Uffe Birk; Schwaeble, W; Kawasaki, T; Ma, Yong; Uemura, K; Wakamiya, N; Suzuki, Y; Jensen, T G; Takahashi, K; Ezekowitz, R A; Thiel, S; Jensenius, J C.

In: International Immunopharmacology, Vol. 1, No. 4, 01.04.2001, p. 677-87.

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

Harvard

Vorup-Jensen, T, Sørensen, ES, Jensen, UB, Schwaeble, W, Kawasaki, T, Ma, Y, Uemura, K, Wakamiya, N, Suzuki, Y, Jensen, TG, Takahashi, K, Ezekowitz, RA, Thiel, S & Jensenius, JC 2001, 'Recombinant expression of human mannan-binding lectin', International Immunopharmacology, vol. 1, no. 4, pp. 677-87.

APA

Vorup-Jensen, T., Sørensen, E. S., Jensen, U. B., Schwaeble, W., Kawasaki, T., Ma, Y., Uemura, K., Wakamiya, N., Suzuki, Y., Jensen, T. G., Takahashi, K., Ezekowitz, R. A., Thiel, S., & Jensenius, J. C. (2001). Recombinant expression of human mannan-binding lectin. International Immunopharmacology, 1(4), 677-87.

CBE

Vorup-Jensen T, Sørensen ES, Jensen UB, Schwaeble W, Kawasaki T, Ma Y, Uemura K, Wakamiya N, Suzuki Y, Jensen TG, Takahashi K, Ezekowitz RA, Thiel S, Jensenius JC. 2001. Recombinant expression of human mannan-binding lectin. International Immunopharmacology. 1(4):677-87.

MLA

Vorup-Jensen, T et al. "Recombinant expression of human mannan-binding lectin". International Immunopharmacology. 2001, 1(4). 677-87.

Vancouver

Vorup-Jensen T, Sørensen ES, Jensen UB, Schwaeble W, Kawasaki T, Ma Y et al. Recombinant expression of human mannan-binding lectin. International Immunopharmacology. 2001 Apr 1;1(4):677-87.

Author

Vorup-Jensen, T ; Sørensen, Esben Skipper ; Jensen, Uffe Birk ; Schwaeble, W ; Kawasaki, T ; Ma, Yong ; Uemura, K ; Wakamiya, N ; Suzuki, Y ; Jensen, T G ; Takahashi, K ; Ezekowitz, R A ; Thiel, S ; Jensenius, J C. / Recombinant expression of human mannan-binding lectin. In: International Immunopharmacology. 2001 ; Vol. 1, No. 4. pp. 677-87.

Bibtex

@article{7de3786348ef42d9b5edb1eb9940be09,
title = "Recombinant expression of human mannan-binding lectin",
abstract = "Mannan-binding lectin (MBL) constitutes an important part of the innate immune defence by effecting the deposition of complement on microbial surfaces. MBL deficiency is among the most common primary immunodeficiencies and is associated with recurrent infections and symptoms of poor immune complex clearance. Plasma-derived MBL has been used in reconstitution therapy but concerns over viral contamination and production capacity point to recombinant MBL (rMBL) as a future source of this protein for clinical use. Natural human MBL is an oligomer of up to 18 identical polypeptide chains. The synthesis of rMBL has been accomplished in several mammalian cell lines, however, the recombinant protein differed structurally from natural MBL. In this, study we compare rMBL produced in myeloma cells, Chinese hamster ovary (CHO) cells, human hepatocytes, and human embryonic kidney (HEK) cells. We report that rMBL structurally and functionally similar to natural MBL can be obtained through synthesis in the human embryonic kidney cells followed by selective carbohydrate affinity chromatography.",
keywords = "Carrier Proteins, Collectins, Humans, Recombinant Proteins",
author = "T Vorup-Jensen and S{\o}rensen, {Esben Skipper} and Jensen, {Uffe Birk} and W Schwaeble and T Kawasaki and Yong Ma and K Uemura and N Wakamiya and Y Suzuki and Jensen, {T G} and K Takahashi and Ezekowitz, {R A} and S Thiel and Jensenius, {J C}",
year = "2001",
month = apr,
day = "1",
language = "English",
volume = "1",
pages = "677--87",
journal = "International Immunopharmacology",
issn = "1567-5769",
publisher = "Elsevier Ltd",
number = "4",

}

RIS

TY - JOUR

T1 - Recombinant expression of human mannan-binding lectin

AU - Vorup-Jensen, T

AU - Sørensen, Esben Skipper

AU - Jensen, Uffe Birk

AU - Schwaeble, W

AU - Kawasaki, T

AU - Ma, Yong

AU - Uemura, K

AU - Wakamiya, N

AU - Suzuki, Y

AU - Jensen, T G

AU - Takahashi, K

AU - Ezekowitz, R A

AU - Thiel, S

AU - Jensenius, J C

PY - 2001/4/1

Y1 - 2001/4/1

N2 - Mannan-binding lectin (MBL) constitutes an important part of the innate immune defence by effecting the deposition of complement on microbial surfaces. MBL deficiency is among the most common primary immunodeficiencies and is associated with recurrent infections and symptoms of poor immune complex clearance. Plasma-derived MBL has been used in reconstitution therapy but concerns over viral contamination and production capacity point to recombinant MBL (rMBL) as a future source of this protein for clinical use. Natural human MBL is an oligomer of up to 18 identical polypeptide chains. The synthesis of rMBL has been accomplished in several mammalian cell lines, however, the recombinant protein differed structurally from natural MBL. In this, study we compare rMBL produced in myeloma cells, Chinese hamster ovary (CHO) cells, human hepatocytes, and human embryonic kidney (HEK) cells. We report that rMBL structurally and functionally similar to natural MBL can be obtained through synthesis in the human embryonic kidney cells followed by selective carbohydrate affinity chromatography.

AB - Mannan-binding lectin (MBL) constitutes an important part of the innate immune defence by effecting the deposition of complement on microbial surfaces. MBL deficiency is among the most common primary immunodeficiencies and is associated with recurrent infections and symptoms of poor immune complex clearance. Plasma-derived MBL has been used in reconstitution therapy but concerns over viral contamination and production capacity point to recombinant MBL (rMBL) as a future source of this protein for clinical use. Natural human MBL is an oligomer of up to 18 identical polypeptide chains. The synthesis of rMBL has been accomplished in several mammalian cell lines, however, the recombinant protein differed structurally from natural MBL. In this, study we compare rMBL produced in myeloma cells, Chinese hamster ovary (CHO) cells, human hepatocytes, and human embryonic kidney (HEK) cells. We report that rMBL structurally and functionally similar to natural MBL can be obtained through synthesis in the human embryonic kidney cells followed by selective carbohydrate affinity chromatography.

KW - Carrier Proteins

KW - Collectins

KW - Humans

KW - Recombinant Proteins

M3 - Journal article

C2 - 11357880

VL - 1

SP - 677

EP - 687

JO - International Immunopharmacology

JF - International Immunopharmacology

SN - 1567-5769

IS - 4

ER -