Collectin liver 1 and collectin kidney 1 and other complement-associated pattern recognition molecules in systemic lupus erythematosus

Troldborg, Anne; Thiel, Steffen; Jensen, Lisbeth; Hansen, Søren; Laska, Magdalena Janina; Jensenius, Jens C.; Stengaard‐Pedersen, Kristian

doi:10.1111/cei.12678

Cited by 29 publications

(30 citation statements)

References 49 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The LP proteins are synthesized predominantly by the liver [34]; however, it has been described that H-ficolin is abundant in lung tissue [35], that M-ficolin is produced primarily by leucocytes [28] and that CL-K1 is also produced by kidney cells [36]. We confirmed that CL-L1 and CL-K1 concentrations correlate strongly, as we have reported previously [37]. These proteins have been found to exist primarily as heteromeric complexes in the circulation [4].…”

Section: Discussionsupporting

confidence: 89%

Lectin complement pathway proteins in healthy individuals

Troldborg

Hansen

et al. 2017

Clinical and Experimental Immunology

Self Cite

View full text Add to dashboard Cite

Since the discovery of the lectin pathway of complement activation, numerous clinical cohorts have been examined for one or more proteins, with the intention of uncovering the functions of the proteins or with the aim of discovering new biomarkers or diagnostic tools. To unveil the abnormal, it is pivotal to know the normal. Our aim was to describe the concentrations of the 11 known proteins of the lectin pathway in serum and plasma and to uncover possible gender differences, age and diurnal variations, which must be taken into account for investigation in different cohorts. We examined the concentrations of all lectin pathway proteins mannan-binding lectin (MBL), H-ficolin, L-ficolin, M-ficolin, collectin-K1, collectin-L1, MBL-associated serine protease 2 (MASP-2), MASP-3, MBL-associated protein of 44 kDa (MAp44) and MAp19 in 300 Danish blood donors in serum and ethylenediamine tetraacetic acid (EDTA) plasma in established assays, and we further developed a new assay to measure MASP-1 in the same samples. We found significant differences in concentrations between serum and plasma for all proteins except for MBL and MASP-3. H-ficolin, M-ficolin and MAp19 displayed convincing diurnal variation. H-ficolin, in particular, halved from morning to the middle of the night. There were gender differences for most proteins, whereas age did not seem to influence concentration. The present study underlines the necessity of considering which material to use, correct matching and a trial design that takes the nature of the protein into account in order for the outcome of cohort studies to have significant relevance.

show abstract

Section: Discussionsupporting

confidence: 89%

Lectin complement pathway proteins in healthy individuals

Troldborg

Hansen

et al. 2017

Clinical and Experimental Immunology

Self Cite

View full text Add to dashboard Cite

show abstract

“…Chinese hamster ovary (CHO) cells co‐transfected with both proteins were observed to synthesize such complexes with the same CL‐10:CL‐11 ratio. Finally, studies show that CL‐10 and CL‐11 serum levels are highly correlated, which further supports the idea of naturally occurring heteromeric CL‐10/11 (CL‐L/K) complexes . Until recently, human CL‐10 was considered as a cytoplasmic protein retained within the hepatocytes .…”

Section: Collectin‐10 and Collectin‐11supporting

confidence: 56%

“…Until recently, human CL‐10 was considered as a cytoplasmic protein retained within the hepatocytes . Nevertheless, CL‐10 on its own has now been defined as a serum protein with a median concentration of around 0.3 μg/ml (0.2–0.51 μg/ml) . How much of the CL‐10 content in serum that is a part of the CL‐10/11 heteromeric complex is still unknown.…”

Section: Collectin‐10 and Collectin‐11mentioning

confidence: 99%

A journey through the lectin pathway of complement—MBL and beyond

Garred

Genster

Pilely

et al. 2016

Immunological Reviews

323

302

View full text Add to dashboard Cite

Mannose-binding lectin (MBL), collectin-10, collectin-11, and the ficolins (ficolin-1, ficolin-2, and ficolin-3) are soluble pattern recognition molecules in the lectin complement pathway. These proteins act as mediators of host defense and participate in maintenance of tissue homeostasis. They bind to conserved pathogen-specific structures and altered self-antigens and form complexes with the pentraxins to modulate innate immune functions. All molecules exhibit distinct expression in different tissue compartments, but all are found to a varying degree in the circulation. A common feature of these molecules is their ability to interact with a set of serine proteases named MASPs (MASP-1, MASP-2, and MASP-3). MASP-1 and -2 trigger the activation of the lectin pathway and MASP-3 may be involved in the activation of the alternative pathway of complement. Furthermore, MASPs mediate processes related to coagulation, bradykinin release, and endothelial and platelet activation. Variant alleles affecting expression and structure of the proteins have been associated with a variety of infectious and non-infectious diseases, most commonly as disease modifiers. Notably, the severe 3MC (Malpuech, Michels, Mingarelli, and Carnevale) embryonic development syndrome originates from rare mutations affecting either collectin-11 or MASP-3, indicating a broader functionality of the complement system than previously anticipated. This review summarizes the characteristics of the molecules in the lectin pathway.

show abstract

“…The LPP patterns reported in SLE and RA differ from that found in our axSpA cohort. This possibly reflects that different parts of the innate immune system are involved in each of these diseases and might be due to that both SLE and RA are humoral‐associated autoimmune diseases, where autoantibodies precede the clinical presentation of the disease.…”

Section: Discussioncontrasting

confidence: 99%

Plasma levels of H- and L-ficolin are increased in axial spondyloarthritis: improvement of disease identification

Troldborg

Thiel

Mistegaard

et al. 2019

Clinical and Experimental Immunology

Self Cite

View full text Add to dashboard Cite

Summary Axial spondyloarthritis (axSpA) is a chronic inflammatory disease that primarily affects the axial skeleton. A predominance of innate versus adaptive immune responses have been reported in axSpA, indicating a prominent autoinflammatory component of the disease. Little is known about the lectin pathway proteins (LPPs) of the complement system in relation to axSpA. We have investigated LPPs in patients with axSpA and control individuals. Plasma samples were obtained from a cross‐sectional cohort of 120 patients with a clinical diagnosis of axSpA and from 144 age‐ and gender‐matched controls. The plasma concentrations of 11 LPPs were measured, using sandwich‐type time‐resolved immunofluorometric assays in patients and controls, and related to clinical diagnosis and disease activity. Three LPPs [H‐ficolin (ficolin‐3), L‐ficolin (ficolin‐2) and collectin liver 1 (CL‐L1)] were significantly higher in axSpA patients than in controls (P < 0·0001) and one LPP, collectin kidney 1 (CL‐K1), was significantly lower (P < 0·0001). Further, combining H‐ or L‐ficolin concentrations above the 75th percentile of the respective H‐ or L‐ficolin concentration measured in controls with human leucocyte antigen (HLA)‐B27 positivity yielded axSpA diagnostic specificities of 99/99% and positive likelihood ratios of 68/62, respectively. H‐ficolin and L‐ficolin plasma concentrations were found to be elevated in axSpA patients regardless of time since diagnosis. H‐ficolin and L‐ficolin may represent diagnostic biomarkers for patients with axSpA and should be further evaluated. Our results showed no association between disease activity and the measured LPP concentrations. This result might be due to the cross‐sectional design, and should be further investigated.

show abstract

Collectin liver 1 and collectin kidney 1 and other complement-associated pattern recognition molecules in systemic lupus erythematosus

Cited by 29 publications

References 49 publications

Lectin complement pathway proteins in healthy individuals

Lectin complement pathway proteins in healthy individuals

A journey through the lectin pathway of complement—MBL and beyond

Plasma levels of H- and L-ficolin are increased in axial spondyloarthritis: improvement of disease identification

Contact Info

Product

Resources

About