Attachment to Caregivers and Type 1 Diabetes in Children

Attachment is a behavioral and physiological system, which enables individual’s dynamic adaptation to its environment. Attachment develops in close interaction between an infant and his/her mother, plays an important role in the development of the infant’s brain, and influences the quality of interpersonal relationships throughout life.Security of attachment is believed to influence individual response to stress, exposing insecurely organized individuals to deregulated autonomic nervous system and exaggerated hypothalamic-pituitary-adrenal activity, which, in turn, produces increased and prolonged exposure to stress-hormones. Such stress responses may have considerable implications for the development of diverse health-risk conditions, such as insulin resistance and hyperlipidemia, shown by numerous studies.Although the mechanisms are not yet fully understood, there is compelling evidence highlighting the role of psychological stress in the development of type 1 diabetes (T1D). One of the possible contributing factors for the development of T1D may be the influence of attachment security on individual stress reactivity. Thus, the suggestion is that insecurely attached individuals are more prone to experience increased and prolonged influence of stress hormones and other mechanisms causing pancreatic beta-cell destruction.The present paper opens with a short overview of the field of attachment in children, the principal attachment classifications and their historic development, describes the influence of attachment security on individual stress-reactivity and the role of the latter in the development of T1D. Following is a review of recent literature on the attachment in patients with T1D with a conclusion of a proposed role of attachment organization in the etiology of T1D.     

Effects of non-thermal atmospheric plasma treatment on dentin wetting and surface free energy for application of universal adhesives

Objectives

The study aims to evaluate the effects of non-thermal atmospheric plasma (NTAP) treatments on dentin wetting and surface free energy (SFE) and compare the effects of NTAP treatment, etch-and-rinse, and self-etch protocols for application of universal adhesives.

Materials and methods

Mid-coronal dentin of intact third molars was used to measure contact angles of distilled water, ethylene-glycol, and diiodomethane and calculate SFE following different NTAP preset treatments (feeding gas consisting of pure He, He + 1% O₂, He + 1.5% O₂), power input (1 or 3 W), and tip-to-surface distance (2, 4, or 8 mm). Contact angles of reference liquids and SFE of dentin following He + 1.5% O₂ at 3-W and 4-mm treatment was compared to phosphoric acid etching. Contact angles of Single Bond Universal (SBU; 3M ESPE) and Clearfil Universal Bond (CUB; Kuraray Noritake) were measured following NTAP, etch-and-rinse, and self-etch protocols.

Results

NTAP significantly reduced contact angles of reference liquids and increased dentin SFE compared to untreated dentin (p < 0.05). O₂ intensified the effect of He NTAP (p < 0.05). NTAP and phosphoric acid increased dentin polarity and Lewis base surface characteristics. Phosphoric acid increased contact angles of adhesives compared to the self-etch protocol (p < 0.05). NTAP resulted in lower adhesive contact angles than phosphoric acid, the difference being statistically significant for CUB (p < 0.05). Compared to the self-etch protocol, NTAP slightly reduced CUB contact angle but not that of SBU (p > 0.05).

Conclusions

He NTAP with and without O₂ increased dentin wetting and SFE, surpassing the effect of phosphoric acid and lowering adhesive contact angles. NTAP produced no apparent micro-morphological changes on dentin surface comparable to acid etching.

Clinical significance

NTAP treatment of dentin prior to adhesive application increases dentin wetting and surface free energy facilitating better adhesive distribution on dentin surface compared to phosphoric acid etching and similar to the “self-etch” application protocol.

     

Elastofibroma dorsi has distinct cytomorphologic features, making diagnostic surgical biopsy unnecessary: cytomorphologic study with clinical, radiologic, and electron microscopic correlations

Elastofibroma dorsi (EFD) is a relatively rare soft tissue mass, probably of reactive nature. The lesion is typically located near the inferior margin of the scapula or between the inferior part of scapula and the chest wall in elderly women. Although location of the tumor together with the age/sex of the patients and radiologic findings is often suggestive of the diagnosis, tissue examination has been considered necessary to confirm the diagnosis. Although the histologic features of EFD are well known, there are only four single case reports of the cytologic findings in the English language literature. We describe the cytologic features of EFD in five patients with correlations to clinical, radiologic, histologic, and electron microscopic findings. The current study suggests that the fine-needle aspiration (FNA) features are highly diagnostic, permitting a firm diagnosis of EFD in a typical clinical setting and eliminating the need for preoperative histologic examination.     

Anti-beta(2)-glycoprotein I antibodies in children with atopic dermatitis

beta(2)-Glycoprotein I (beta(2)GPI) appears to be the major antigen for antiphospholipid antibodies (aPL) in patients with antiphospholipid syndrome (APS). In early infancy, virtually all children initiate transient immune response to non-pathogenic nutritional antigens, which fails to terminate in children with atopic diseases. To examine the possibility that a prolonged immune response to beta(2)GPI could also spread to the human protein, antibodies against human beta(2)GPI (anti-beta(2)GPI) were determined in 93 randomly selected children with different allergic diseases. A high frequency (42%) of IgG anti-beta(2)GPI was found in children with atopic dermatitis (AD), but not in those with other allergic diseases. Anti-beta(2)GPI in children with AD were exclusively of the IgG1 subclass and bound to bovine beta(2)GPI as well, but not to either beta(2)GPI combined with the phospholipid cardiolipin. The epitopes were identified in domain V of beta(2)GPI and the antibody binding was abolished upon the specific proteolytic cleavage of the phospholipid-binding C-terminal loop in domain V of beta(2)GPI. These results indicated that the epitopes for anti-beta(2)GPI in children with AD most likely resided in close vicinity of the phospholipid-binding site of beta(2)GPI. The epitopic difference from anti-beta(2)GPI in APS may explain presumed non-thrombogenicity of anti-beta(2)GPI in children with AD.