CLEC2A: a novel, alternatively spliced and skin-associated member of the NKC-encoded AICL–CD69–LLT1 family

Spreu, Jessica; Kienle, Eike; Schrage, Birgit; Steinle, Alexander

doi:10.1007/s00251-007-0263-1

Cited by 31 publications

(42 citation statements)

References 19 publications

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“…This result suggested that the 20 N-terminal aa prevented efficient production of soluble CLEC2D protein isoforms. Interestingly, a similar observation has been made for CLEC2A (11). It is therefore unlikely that a soluble LLT1 generated from alternative splicing could compete with membrane-bound LLT1.…”

Section: Discussionsupporting

confidence: 73%

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Characterization of Alternatively Spliced Transcript Variants of CLEC2D Gene

Germain

Bihl²,

Zahn³

et al. 2010

Journal of Biological Chemistry

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Lectin-like transcript 1 (LLT1) encoded by CLEC2D gene is a C-type lectin-like molecule interacting with human CD161 (NKR-P1A) receptor expressed by natural killer cells and subsets of T cells. Using RT-PCR and sequencing, we identified several CLEC2D alternatively spliced transcript variants generated by exon skipping. In addition to the reported transcript variants 1 (LLT1) and 2, we identified a novel splice variant 4 and transcripts coding for putative soluble proteins. CLEC2D transcripts were detected primarily in hematopoietic cell lines and were found to be co-induced by the same activation signals. Although very low amounts of putative soluble CLEC2D protein isoforms could be produced by transfectants, CLEC2D isoforms 2 and 4 were efficiently expressed. By contrast to LLT1, which was detected on the cell surface, isoform 2 and 4 remained in the endoplasmic reticulum where they formed homodimers or heterodimers with LLT1. They failed to interact with CD161, leaving LLT1 as the sole ligand for this receptor. CLEC2D therefore uses gene splicing to generate protein isoforms that are structurally distinct and that have different biological activities.

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Section: Discussionsupporting

confidence: 73%

“…This vector and control RSV5-CLEC2A were generously provided by A. Steinle and described previously (11). Transient expression was obtained by electroporation of 293T and 293T-LLT1 cells (250 V, 500 microfarads).…”

Section: Cloning Of Clec2d Alternatively Spliced Transcript Variants:mentioning

confidence: 99%

Characterization of Alternatively Spliced Transcript Variants of CLEC2D Gene

Germain

Bihl²,

Zahn³

et al. 2010

Journal of Biological Chemistry

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“…35 It has been reported that gut-resident Th17 cells express CD161. 36 Our present study shows most decidual Th17 cells express CD161.…”

Section: Discussionmentioning

confidence: 99%

Decidual stromal cells recruit Th17 cells into decidua to promote proliferation and invasion of human trophoblast cells by secreting IL-17

Jin

et al. 2014

Cell Mol Immunol

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T helper 17 (Th17) cells have both regulatory and protective roles in physiological conditions. The Th17 subset and the cytokine interleukin-17A (IL-17A) have been implicated in the pathogenesis of certain autoimmune diseases, several types of cancer and allograft rejection. However, the role of Th17 cells at the maternal/fetal interface remains unknown. Here, we demonstrate that Th17 cells are present in decidua and are increased in the peripheral blood of 10 clinically normal pregnancies based on intracellular cytokine analysis. Our results suggest a potential role of Th17 cells in sustaining pregnancy in humans. Furthermore, we demonstrate that decidual stromal cells (DSCs) but not trophoblast cells recruit peripheral Th17 cells into the decidua by secreting CCL2. The recruited Th17 cells promote proliferation and invasion and inhibit the apoptosis of human trophoblast cells by secreting IL-17 during the first trimester of pregnancy. These findings indicate a novel role for Th17 cells in controlling the maternal-fetal relationship and placenta development.

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“…The cellular distribution of NKp65 receptors in vivo remains to be shown. NKp65 tightly binds to the C-type lectin-like glycoprotein KACL, which is encoded adjacently to KLRF2 in the NKC and restricted to keratinocytes (28,81). The exceptionally high affinity of the NKp65-KACL interaction (28, 82) is due to high shape complementary and a few "hotspot" amino acid residues, providing a high number of hydrogen bonds (29,82).…”

Section: Nkp65mentioning

confidence: 99%