The Functional Polymorphism Ala258Ser in the Innate Receptor Gene Ficolin-2 in the Donor Predicts Improved Renal Transplant Outcome

Eikmans, Michael; Canck, I. De; Pol, Pieter van der; Baan, Carla C.; Haasnoot, Geert W.; Mallat, M.; Vergunst, Manon; Meester, Els de; Roodnat, Joke I.; Anholts, J.; Thielen, M Van; Doxiadis, Ilias I.N.; Fijter, Johan W. de; Linden, Pieter J.E. van der; Beelen, Els van; Kooten, Cees van; Gestel, Judith A. Kal-van; Peeters, Annemiek M.A.; Weimar, Willem; Roelen, Dave L.; Rossau, R.; Claas, Frans H.J.

doi:10.1097/tp.0b013e31825c5967

Cited by 23 publications

(13 citation statements)

References 53 publications

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“…Ala258Ser, which represents decreased ficolin-2 concentration and increased binding capacity of ficolin-2 to GLcNAc, is associated with chronic Chagas disease (Luz et al, 2013) and leprosy . Furthermore, in renal transplantation, this SNP in the donor predicts improved outcome with lower incidence of severe rejection (Eikmans et al, 2012). In contrast, it was reported that three promoter SNPs (-986, -602, and -4) and two nonsynonymous SNPs (Thr236Met and Ala258Ser) are not associated with invasive pneumococcal disease (Chapman et al, 2007), respiratory tract infection (Ruskamp et al, 2009), or Behcet's disease (Chen et al, 2006).…”

Section: Gene Polymorphisms Serum Concentrations Of Ficolins and Thementioning

confidence: 92%

New Insights into the Role of Ficolins in the Lectin Pathway of Innate Immunity

Endo

Matsushita

Fujita

2015

International Review of Cell and Molecular Biology

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Section: Gene Polymorphisms Serum Concentrations Of Ficolins and Thementioning

confidence: 92%

New Insights into the Role of Ficolins in the Lectin Pathway of Innate Immunity

Endo

Matsushita

Fujita

2015

International Review of Cell and Molecular Biology

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“…63 However, another study of common functional polymorphisms in the ficolin-2 gene revealed an association between this polymorphism and lower incidence of renal transplant rejection. 64 Furthermore, high pretransplant levels of ficolin-3, the most abundant ficolin in serum, showed strong association with poor allograft survival after renal transplantation. 65,66…”

Section: Role Of Ficolins In Tissue Injurymentioning

confidence: 99%

Complement Recognition Pathways in Renal Transplantation

Nauser

Farrar

Sacks

2017

JASN

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The complement system, consisting of soluble and cell membrane-bound components of the innate immune system, has defined roles in the pathophysiology of renal allograft rejection. Notably, the unavoidable ischemia-reperfusion injury inherent to transplantation is mediated through the terminal complement activation products C5a and C5b-9. Furthermore, biologically active fragments C3a and C5a, produced during complement activation, can modulate both antigen presentation and T cell priming, ultimately leading to allograft rejection. Earlier work identified renal tubule cell synthesis of C3, rather than hepatic synthesis of C3, as the primary source of C3 driving these effects. Recent efforts have focused on identifying the local triggers of complement activation. Collectin-11, a soluble C-type lectin expressed in renal tissue, has been implicated as an important trigger of complement activation in renal tissue. In particular, collectin-11 has been shown to engage L-fucose at sites of ischemic stress, activating the lectin complement pathway and directing the innate immune response to the distressed renal tubule. The interface between collectin-11 and L-fucose, in both the recipient and the allograft, is an attractive target for therapies intended to curtail renal inflammation in the acute phase.

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“…138 Moreover, if the donor carries this SNP, an improved outcome of renal transplantation has been reported. 139 Only a few variations in FCN3 have been detected and these are present in low frequencies. 107 A few cases of ficolin-3 deficiency have been reported to date.…”

Section: Genetic Variations and Their Association With Diseasementioning

confidence: 99%

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

Garred

Genster

Pilely

et al. 2016

Immunological Reviews

323

302

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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.

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The Functional Polymorphism Ala258Ser in the Innate Receptor Gene Ficolin-2 in the Donor Predicts Improved Renal Transplant Outcome

Cited by 23 publications

References 53 publications

New Insights into the Role of Ficolins in the Lectin Pathway of Innate Immunity

New Insights into the Role of Ficolins in the Lectin Pathway of Innate Immunity

Complement Recognition Pathways in Renal Transplantation

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

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