Intermediate Filament Proteins Expression and Carbohydrate Moieties in Trophoblast and Decidual Cells of Mature Cat Placenta

Abstract

The aim of this study was to characterize cytoskeletal intermediate filament proteins and glycoconjugates of syncytiotrophoblast, cytotrophoblast and decidual cells of feline endotheliochorial placenta. Samples from 12 normal pregnant female cats, after 45 ± 5 days of gestation, were obtained removing the uterine horns by hysterectomy. Sections were processed for routine observation and for immunohistochemistry using anticytokeratin, antivimentin and antidesmin antibodies. In addition, lectin histochemistry was performed using a panel of several biotinylated lectins to characterize glycosides expression profile. Cytotrophoblast and syncytiotrophoblast showed immunoreactivity only with acidic and basic cytokeratins. Decidual cells were only positive to vimentin, consistent with their origin from endometrial fibroblasts. Trophoblast expressed a broad population of glycans, highly exposing terminal N-acetyl glucosamine residues and non-sialylated galactose and N-acetyl galactosamine oligomers. Oligosaccharides bound by Phaseolus vulgaris erythroagglutinin were the only highly branched N-linked residues evidenced in cats, and they were restricted to the syncytium. Unlike results reported on humans, mice and rats on lectin affinity of decidual cells, sialid acids and complex N-linked oligosaccharides were not demonstrated in cats. Glycosylation of proteins determines many of their final properties, thus becoming essential for the embryo-maternal dialogue during implantation and placentation. Changes in glycosylation pattern have been related to pathological pregnancies in other species. Hence, the knowledge about glycosylation profile of the normal cat placenta may lead to a better understanding of both normal and pathological reproductive events.

Lectin binding patterns and immunohistochemical antigen detection in placenta and lungs of <i>Brucella abortus</i>-bovine infected fetuses

“…Controls for lectin staining included: exposure to horseradish-peroxidase and substrate medium without lectin and blocking by incubation with the appropriate blocking sugars (0.1 to 0.2M in PBS) for 1 h at room temperature before applying to the sections. The intensity of lectin binding was subjectively scored from (-) (none) to +++ (strongly positive) following the system used previously (Fernández et al, 2014;Díaz et al, 2017). The structures studied in the lungs were glycocalix and cytoplasm of the epithelium of bronchi, bronchioli and alveoli and vascular endothelium.…”

Functional glycosylation in the human and mammalian uterus

“…Jones et al recently employed a panel of twenty-four different lectins to investigate the glycosylation of the placenta and the uterus in a marsupial, the tammar wallaby Macropus eugenii [59]. Feline decidual cells displayed weak binding for GS-I, ConA, DBA, DSA, PNA, RCA-I, SBA and SJA in another study [60]. ConA, LCA, SNA, RCA-I, PNA, SBA and HPA were among the lectins that were shown to bind to normal rat endometrium [61].…”

Morphology of alpaca (Vicugna pacos) embryos in the first third of pregnancy

“…Some sections were used as negative controls by omitting the primary antibody and incubating with 1% BSA. Samples from previously published experiments (Fernández et al., ) with recognized positive reactivity were used as positive control. Other organs of alpaca (liver, intestine, tongue) were used to convalidate the specific distribution of the positive marcation.…”