Effect of premolar extraction and anchorage type for orthodontic space closure on upper airway dimensions and position of hyoid bone in adults: a retrospective cephalometric assessment

Background. This study aimed to assess the effect of premolar extraction and anchorage type for orthodontic space closure on upper airway dimensions and position of hyoid bone in adults by cephalometric assessment. Methods. This retrospective study was conducted on 142 cephalograms of patients who underwent orthodontic treatment with premolar extraction in four groups of (I) 40 class I patients with bimaxillary protrusion and maximum anchorage, (II) 40 class I patients with moderate crowding and anchorage, (III) 40 class II patients with maximum anchorage, and (IV) 22 skeletal class III patients with maximum anchorage. The dimensions of the nasopharynx, velopharynx, oropharynx, and hypopharynx, and hyoid bone position were assessed on pre- and postoperative lateral cephalograms using AudaxCeph v6.1.4.3951 software. Data were analyzed by the Chi-square test, paired t-test, and Pearson's correlation test (alpha D 0.05). Results. A significant reduction in oropharyngeal, velopharyngeal, and hypopharyngeal airway dimensions was noted in groups I, III, and IV (P <0:001), which was correlated with the magnitude of retraction of upper and lower incisors (r =0:6-0:8). In group II, a significant increase was observed in oropharyngeal and velopharyngeal dimensions (P < 0:001). A significant increase in nasopharyngeal dimensions occurred in all groups (P < 0:001). Also, in groups I and III, the position of hyoid bone changed downwards and backwards, which was correlated with reduction in airway dimensions (r =0:4-0:6). Conclusion. According to the present results, extraction orthodontic treatment affects upper airway dimensions and hyoid bone position. Maximum anchorage decreases airway dimensions while moderate anchorage increases airway dimensions

Sensing Tissue Damage by Myeloid C-Type Lectin Receptors

After both sterile and infectious insults, damage is inflicted on tissues leading to accidental or programmed cell death. In addition, events of programmed cell death also take place under homeostatic conditions, such as in embryo development or in the turnover of hematopoietic cells. Mammalian tissues are seeded with myeloid immune cells, which harbor a plethora of receptors that allow the detection of cell death, modulating immune responses. The myeloid C-type lectin receptors (CLRs) are one of the most prominent families of receptors involved in tailoring immunity after sensing dead cells. In this chapter, we will cover a diversity of signals arising from different forms of cell death and how they are recognized by myeloid CLRs. We will also explore how myeloid cells develop their sentinel function, exploring how some of these CLRs identify cell death and the type of responses triggered thereof. In particular, we will focus on DNGR-1 (CLEC9A), Mincle (CLEC4E), CLL-1 (CLEC12A), LOX-1 (OLR1), CD301 (CLEC10A) and DEC-205 (LY75) as paradigmatic death-sensing CLRs expressed by myeloid cells. The molecular processes triggered after cell death recognition by myeloid CLRs contribute to the regulation of immune responses in pathologies associated with tissue damage, such as infection, autoimmunity and cancer. A better understanding of these processes may help to improve the current approaches for therapeutic intervention.Carlos Del Fresno is supported by AECC Foundation (INVES192DELF). Francisco Javier Cueto is the recipient of a Ph.D. “La Caixa” fellowship (LCF/BQ/ES14/10320011). Work in the DS laboratory is funded by the CNIC; by the European Research Council (ERC-2016-Consolidator Grant 725091); by the European Commission (635122-PROCROP H2020); by Ministerio de Ciencia, Innovación e Universidades (MICINN), Agencia Estatal de Investigación and Fondo Europeo de Desarrollo Regional (FEDER) (SAF2016-79040-R); by Comunidad de Madrid (B2017/BMD-3733 Immunothercan-CM); by FIS-Instituto de Salud Carlos III, MICINN and FEDER (RD16/0015/0018-REEM); by Acteria Foundation; by Atresmedia (Constantes y Vitales prize) and by Fundació La Marató de TV3 (201723). The CNIC is supported by the Instituto de Salud Carlos III (ISCIII), the MICINN and the Pro-CNIC Foundation and is a Severo Ochoa Center of Excellence (SEV-2015-0505).S

The Breast Cancer-Associated Glycoforms of MUC1, MUC1-Tn and sialyl-Tn, Are Expressed in COSMC Wild-Type Cells and Bind the C-Type Lectin MGL

<div><p>Aberrant glycosylation occurs in the majority of human cancers and changes in mucin-type O-glycosylation are key events that play a role in the induction of invasion and metastases. These changes generate novel cancer-specific glyco-antigens that can interact with cells of the immune system through carbohydrate binding lectins. Two glyco-epitopes that are found expressed by many carcinomas are Tn (GalNAc-Ser/Thr) and STn (NeuAc<b>α</b>2,6GalNAc-Ser/Thr). These glycans can be carried on many mucin-type glycoproteins including MUC1. We show that the majority of breast cancers carry Tn within the same cell and in close proximity to extended glycan T (Gal<b>β</b>1,3GalNAc) the addition of Gal to the GalNAc being catalysed by the T synthase. The presence of active T synthase suggests that loss of the private chaperone for T synthase, COSMC, does not explain the expression of Tn and STn in breast cancer cells. We show that MUC1 carrying both Tn or STn can bind to the C-type lectin MGL and using atomic force microscopy show that they bind to MGL with a similar deadadhesion force. Tumour associated STn is associated with poor prognosis and resistance to chemotherapy in breast carcinomas, inhibition of DC maturation, DC apoptosis and inhibition of NK activity. As engagement of MGL in the absence of TLR triggering may lead to anergy, the binding of MUC1-STn to MGL may be in part responsible for some of the characteristics of STn expressing tumours.</p></div