Species-specific evolution of immune receptor tyrosine based activation motif-containing CEACAM1-related immune receptors in the dog

Kammerer, Robert; Popp, Tanja; Härtle, Stefan; Singer, Bernhard B.; Zimmermann, Wolfgang

doi:10.1186/1471-2148-7-196

Cited by 30 publications

(44 citation statements)

References 48 publications

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“…It is generally accepted that PSGs evolved exclusively in mammals with hemochorial placentation. In cattle (epitheliochorial placenta) and dogs (endotheliochorial placenta), PSGs did not evolve (Kammerer et al 2004, Kammerer et al 2007.…”

Section: Introductionmentioning

confidence: 95%

Convergent evolution of pregnancy-specific glycoproteins in human and horse

et al. 2016

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Pregnancy-specific glycoproteins (PSGs) are members of the carcinoembryonic antigen cell adhesion molecule (CEACAM) family that are secreted by trophoblast cells. PSGs may modulate immune, angiogenic and platelet responses during pregnancy. Until now, PSGs are only found in species that have a highly invasive (hemochorial) placentation including humans, mice and rats. Surprisingly, analyzing the CEACAM gene family of the horse, which has a non-invasive epitheliochorial placenta, with the exception of the transient endometrial cups, we identified equine CEACAM family members that seem to be related to PSGs of rodents and primates. We identified seven genes that encode secreted PSG-like CEACAMs. Phylogenetic analyses indicate that they evolved independently from an equine CEACAM1-like ancestor rather than from a common PSG-like ancestor with rodents and primates. Significantly, expression of PSG-like genes (CEACAM44, CEACAM48, CEACAM49 and CEACAM55) was found in non-invasive as well as invasive trophoblast cells such as purified chorionic girdle cells and endometrial cup cells. Chorionic girdle cells are highly invasive trophoblast cells that invade the endometrium of the mare where they form endometrial cups and are in close contact with maternal immune cells. Therefore, the microenvironment of invasive equine trophoblast cells has striking similarities to the microenvironment of trophoblast cells in hemochorial placentas, suggesting that equine PSG-like CEACAMs and rodent and primate PSGs have undergone convergent evolution. This is supported by our finding that equine PSG-like CEACAM49 exhibits similar activity to certain rodent and human PSGs in a functional assay of platelet-fibrinogen binding. Our results have implications for understanding the evolution of PSGs and their functions in maternal-fetal interactions. Reproduction (2016) 152

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Section: Introductionmentioning

confidence: 95%

Convergent evolution of pregnancy-specific glycoproteins in human and horse

et al. 2016

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“…All 12 expressed CEACAM genes and a number of derived pseudogenes cluster on chromosome 19q13 [3,4]. CEACAMs show distinct expression patterns on different cell types [1,5].…”

Section: Introductionmentioning

confidence: 99%

Signaling by epithelial members of the CEACAM family – mucosal docking sites for pathogenic bacteria

2014

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Carcinoembryonic antigen-related cell adhesion molecules (CEACAMs) comprise a group of immunoglobulin-related vertebrate glycoproteins. Several family members, including CEACAM1, CEA, and CEACAM6, are found on epithelial tissues throughout the human body. As they modulate diverse cellular functions, their signaling capacity is in the focus of current research. In this review we will summarize the knowledge about common signaling processes initiated by epithelial CEACAMs and suggest a model of signal transduction by CEACAM family members lacking significant cytoplasmic domains. As pathogenic and non-pathogenic bacteria exploit these receptors during mucosal colonization, we try to highlight the connection between CEACAMs, microbes, and cellular responses. Special emphasis in this context is placed on the functional interplay between CEACAMs and integrins that influences matrix adhesion of epithelial cells. The cooperation between these two receptor families provides an intriguing example of the fine tuning of cellular responses and their manipulation by specialized microorganisms.

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“…They have been extensively used to study the polarized organization of epithelial cells forming monolayers and the biosynthetic and recycling pathways for apical and basolateral plasma‐membrane proteins (Rodriguez‐Boulan et al ., 2005). It has been reported that most of the CEACAMs, identified in canine liver, bone marrow, spleen, peripheral blood monocytes and granulocytes, harboured immunoreceptor tyrosine‐based activation motifs, one of which, CEACAM28, exhibits nearly complete sequence identity with the ligand‐binding N domain of CEACAM1 (Kammerer et al ., 2007). In consequence, MDCK cells probably express canine CEACAMs.…”

Section: Introductionmentioning

confidence: 99%