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Jens Christian Jensenius

Investigations on Collectin Liver 1

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Investigations on Collectin Liver 1. / Axelgaard, Esben; Jensen, Lisbeth; Dyrlund, Thomas Franck; Nielsen, Hans J; Enghild, Jan J; Thiel, Steffen; Jensenius, Jens C.

In: Journal of Biological Chemistry, Vol. 288, No. 32, 09.08.2013, p. 23407-23420.

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

Harvard

Axelgaard, E, Jensen, L, Dyrlund, TF, Nielsen, HJ, Enghild, JJ, Thiel, S & Jensenius, JC 2013, 'Investigations on Collectin Liver 1', Journal of Biological Chemistry, vol. 288, no. 32, pp. 23407-23420. https://doi.org/10.1074/jbc.M113.492603

APA

Axelgaard, E., Jensen, L., Dyrlund, T. F., Nielsen, H. J., Enghild, J. J., Thiel, S., & Jensenius, J. C. (2013). Investigations on Collectin Liver 1. Journal of Biological Chemistry, 288(32), 23407-23420. https://doi.org/10.1074/jbc.M113.492603

CBE

Axelgaard E, Jensen L, Dyrlund TF, Nielsen HJ, Enghild JJ, Thiel S, Jensenius JC. 2013. Investigations on Collectin Liver 1. Journal of Biological Chemistry. 288(32):23407-23420. https://doi.org/10.1074/jbc.M113.492603

MLA

Axelgaard, Esben et al. "Investigations on Collectin Liver 1". Journal of Biological Chemistry. 2013, 288(32). 23407-23420. https://doi.org/10.1074/jbc.M113.492603

Vancouver

Axelgaard E, Jensen L, Dyrlund TF, Nielsen HJ, Enghild JJ, Thiel S et al. Investigations on Collectin Liver 1. Journal of Biological Chemistry. 2013 Aug 9;288(32):23407-23420. https://doi.org/10.1074/jbc.M113.492603

Author

Axelgaard, Esben ; Jensen, Lisbeth ; Dyrlund, Thomas Franck ; Nielsen, Hans J ; Enghild, Jan J ; Thiel, Steffen ; Jensenius, Jens C. / Investigations on Collectin Liver 1. In: Journal of Biological Chemistry. 2013 ; Vol. 288, No. 32. pp. 23407-23420.

Bibtex

@article{ca5f7710682648e685275d3f4affef42,
title = "Investigations on Collectin Liver 1",
abstract = "Collectins are pattern recognition molecules of the innate immune system showing binding to carbohydrate structures on microorganisms in a calcium-dependent manner. Recently, three novel collectins, collectin liver 1 (CL-L1), collectin kidney 1 (CL-K1 and CL-11), and collectin placenta 1 (CL-P1), were discovered. The roles of these three collectins remain largely unknown. Here, we present a time-resolved immunofluorometric assay for quantification of CL-L1. The concentration of CL-L1 in donor plasma (n = 210) was distributed log-normally with a median value of 3.0 μg/ml (range 1.5-5.5 μg/ml). We observed on average 30% higher concentrations of CL-L1 in plasma as compared with serum. Size analysis by gel-permeation chromatography showed CL-L1 in serum to elute as large 700-800-kDa complexes and smaller 200-300-kDa complexes. CL-L1 showed specific binding to mannose-TSK beads in a Ca(2+)-dependent manner. This binding could be inhibited by mannose and glucose, but not galactose, indicating that CL-L1 binds via its carbohydrate-recognition domain and has ligand specificity similar to that of mannan-binding lectin. Western blot analysis of CL-L1 showed the presence of several oligomeric forms in serum. Ontogeny studies showed CL-L1 to be present at birth at near adult levels. CL-L1 levels exhibit low variation in healthy adults over a 1-year period. During acute-phase responses, the CL-L1 levels display only minor variations. In serum, CL-L1 was found in complexes with mannan-binding lectin-associated serine proteases, suggesting a role in the lectin pathway of complement activation. The presented data establish a basis for future studies on the biological role of CL-L1.",
keywords = "Collectins, Complement System, Inflammation, Innate Immunity, Lectin",
author = "Esben Axelgaard and Lisbeth Jensen and Dyrlund, {Thomas Franck} and Nielsen, {Hans J} and Enghild, {Jan J} and Steffen Thiel and Jensenius, {Jens C}",
year = "2013",
month = aug,
day = "9",
doi = "10.1074/jbc.M113.492603",
language = "English",
volume = "288",
pages = "23407--23420",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "32",

}

RIS

TY - JOUR

T1 - Investigations on Collectin Liver 1

AU - Axelgaard, Esben

AU - Jensen, Lisbeth

AU - Dyrlund, Thomas Franck

AU - Nielsen, Hans J

AU - Enghild, Jan J

AU - Thiel, Steffen

AU - Jensenius, Jens C

PY - 2013/8/9

Y1 - 2013/8/9

N2 - Collectins are pattern recognition molecules of the innate immune system showing binding to carbohydrate structures on microorganisms in a calcium-dependent manner. Recently, three novel collectins, collectin liver 1 (CL-L1), collectin kidney 1 (CL-K1 and CL-11), and collectin placenta 1 (CL-P1), were discovered. The roles of these three collectins remain largely unknown. Here, we present a time-resolved immunofluorometric assay for quantification of CL-L1. The concentration of CL-L1 in donor plasma (n = 210) was distributed log-normally with a median value of 3.0 μg/ml (range 1.5-5.5 μg/ml). We observed on average 30% higher concentrations of CL-L1 in plasma as compared with serum. Size analysis by gel-permeation chromatography showed CL-L1 in serum to elute as large 700-800-kDa complexes and smaller 200-300-kDa complexes. CL-L1 showed specific binding to mannose-TSK beads in a Ca(2+)-dependent manner. This binding could be inhibited by mannose and glucose, but not galactose, indicating that CL-L1 binds via its carbohydrate-recognition domain and has ligand specificity similar to that of mannan-binding lectin. Western blot analysis of CL-L1 showed the presence of several oligomeric forms in serum. Ontogeny studies showed CL-L1 to be present at birth at near adult levels. CL-L1 levels exhibit low variation in healthy adults over a 1-year period. During acute-phase responses, the CL-L1 levels display only minor variations. In serum, CL-L1 was found in complexes with mannan-binding lectin-associated serine proteases, suggesting a role in the lectin pathway of complement activation. The presented data establish a basis for future studies on the biological role of CL-L1.

AB - Collectins are pattern recognition molecules of the innate immune system showing binding to carbohydrate structures on microorganisms in a calcium-dependent manner. Recently, three novel collectins, collectin liver 1 (CL-L1), collectin kidney 1 (CL-K1 and CL-11), and collectin placenta 1 (CL-P1), were discovered. The roles of these three collectins remain largely unknown. Here, we present a time-resolved immunofluorometric assay for quantification of CL-L1. The concentration of CL-L1 in donor plasma (n = 210) was distributed log-normally with a median value of 3.0 μg/ml (range 1.5-5.5 μg/ml). We observed on average 30% higher concentrations of CL-L1 in plasma as compared with serum. Size analysis by gel-permeation chromatography showed CL-L1 in serum to elute as large 700-800-kDa complexes and smaller 200-300-kDa complexes. CL-L1 showed specific binding to mannose-TSK beads in a Ca(2+)-dependent manner. This binding could be inhibited by mannose and glucose, but not galactose, indicating that CL-L1 binds via its carbohydrate-recognition domain and has ligand specificity similar to that of mannan-binding lectin. Western blot analysis of CL-L1 showed the presence of several oligomeric forms in serum. Ontogeny studies showed CL-L1 to be present at birth at near adult levels. CL-L1 levels exhibit low variation in healthy adults over a 1-year period. During acute-phase responses, the CL-L1 levels display only minor variations. In serum, CL-L1 was found in complexes with mannan-binding lectin-associated serine proteases, suggesting a role in the lectin pathway of complement activation. The presented data establish a basis for future studies on the biological role of CL-L1.

KW - Collectins

KW - Complement System

KW - Inflammation

KW - Innate Immunity

KW - Lectin

U2 - 10.1074/jbc.M113.492603

DO - 10.1074/jbc.M113.492603

M3 - Journal article

C2 - 23814060

VL - 288

SP - 23407

EP - 23420

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 32

ER -