Jens Christian Jensenius

Assay for the pattern recognition molecule collectin liver 1 (CL-L1)

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Assay for the pattern recognition molecule collectin liver 1 (CL-L1). / Axelgaard, Esben; Jensenius, Jens Christian; Jensen, Lisbeth; Thiel, Steffen.

2012. Abstract from XXIV International Complement Workshop, Chania, Greece.

Research output: Contribution to conferenceConference abstract for conferenceResearchpeer-review

Harvard

Axelgaard, E, Jensenius, JC, Jensen, L & Thiel, S 2012, 'Assay for the pattern recognition molecule collectin liver 1 (CL-L1)', XXIV International Complement Workshop, Chania, Greece, 10/10/2012 - 15/10/2012.

APA

CBE

Axelgaard E, Jensenius JC, Jensen L, Thiel S. 2012. Assay for the pattern recognition molecule collectin liver 1 (CL-L1). Abstract from XXIV International Complement Workshop, Chania, Greece.

MLA

Axelgaard, Esben et al. Assay for the pattern recognition molecule collectin liver 1 (CL-L1). XXIV International Complement Workshop, 10 Oct 2012, Chania, Greece, Conference abstract for conference, 2012. 1 p.

Vancouver

Axelgaard E, Jensenius JC, Jensen L, Thiel S. Assay for the pattern recognition molecule collectin liver 1 (CL-L1). 2012. Abstract from XXIV International Complement Workshop, Chania, Greece.

Author

Bibtex

@conference{0953c0bcb96a487288c650ccb2418eef,
title = "Assay for the pattern recognition molecule collectin liver 1 (CL-L1)",
abstract = "Collectin liver 1 (also termed collectin 10 and CL-L1) is a C-type lectin that functions as a pattern recognition molecule (PRM) in the innate immune system1. We have produced antibodies against CL-L1 and have developed a sandwich-type time-resolved immuno-fluorometric assay (TRIFMA) for the measurement of CL-L1 in serum. High oligomeric forms of CL-L1 could be found in plasma and serum. Ontogeny studies revealed that CL-L1 is present a birth at near adult levels. During acute-phase responses we observe an initial decrease in CL-L1 levels followed by a recovery to initial levels. CL-L1 was found to co-purify with MASPs, possibly rendering it a role in complement. CL-L1 showed binding activity towards mannose-TSK beads in a Ca2+-dependent manner. This binding could be inhibited by mannose and glucose, but not by galactose, indicating that CL-L1 binds via its carbohydrate-recognition domain (CRD).",
author = "Esben Axelgaard and Jensenius, {Jens Christian} and Lisbeth Jensen and Steffen Thiel",
year = "2012",
month = oct,
day = "2",
language = "Dansk",
note = "XXIV International Complement Workshop, ICW ; Conference date: 10-10-2012 Through 15-10-2012",

}

RIS

TY - ABST

T1 - Assay for the pattern recognition molecule collectin liver 1 (CL-L1)

AU - Axelgaard, Esben

AU - Jensenius, Jens Christian

AU - Jensen, Lisbeth

AU - Thiel, Steffen

N1 - Conference code: XXIV

PY - 2012/10/2

Y1 - 2012/10/2

N2 - Collectin liver 1 (also termed collectin 10 and CL-L1) is a C-type lectin that functions as a pattern recognition molecule (PRM) in the innate immune system1. We have produced antibodies against CL-L1 and have developed a sandwich-type time-resolved immuno-fluorometric assay (TRIFMA) for the measurement of CL-L1 in serum. High oligomeric forms of CL-L1 could be found in plasma and serum. Ontogeny studies revealed that CL-L1 is present a birth at near adult levels. During acute-phase responses we observe an initial decrease in CL-L1 levels followed by a recovery to initial levels. CL-L1 was found to co-purify with MASPs, possibly rendering it a role in complement. CL-L1 showed binding activity towards mannose-TSK beads in a Ca2+-dependent manner. This binding could be inhibited by mannose and glucose, but not by galactose, indicating that CL-L1 binds via its carbohydrate-recognition domain (CRD).

AB - Collectin liver 1 (also termed collectin 10 and CL-L1) is a C-type lectin that functions as a pattern recognition molecule (PRM) in the innate immune system1. We have produced antibodies against CL-L1 and have developed a sandwich-type time-resolved immuno-fluorometric assay (TRIFMA) for the measurement of CL-L1 in serum. High oligomeric forms of CL-L1 could be found in plasma and serum. Ontogeny studies revealed that CL-L1 is present a birth at near adult levels. During acute-phase responses we observe an initial decrease in CL-L1 levels followed by a recovery to initial levels. CL-L1 was found to co-purify with MASPs, possibly rendering it a role in complement. CL-L1 showed binding activity towards mannose-TSK beads in a Ca2+-dependent manner. This binding could be inhibited by mannose and glucose, but not by galactose, indicating that CL-L1 binds via its carbohydrate-recognition domain (CRD).

M3 - Konferenceabstrakt til konference

T2 - XXIV International Complement Workshop

Y2 - 10 October 2012 through 15 October 2012

ER -