Notes

A total of 75 pre-demineralized coronal dentin specimens were randomly treated with one of the following test agents (n = 15 each): artificial saliva (AS), casein phosphopeptide-amorphous calcium phosphate (CPP-ACP), CEnHAp, PHS, and CEnHAp-PHS under pH cycling for 7, 14, and 28 days
Vickers microhardness indenter, HRSEM-EDX, and micro-Raman spectroscopy methods were used to assess the mineral changes in the treated dentin samples. Data were submitted to Kruskal-Wallis and Friedman's two-way analyses of variance (p < 05). HRSEM and TEM analysis depicted irregular spherical structure of the prepared CEnHAp with a particle size of 20-50 nm. The EDX analysis confirmed the presence of Ca, P, Na and Mg ions. The XRD pattern showed the characteristic crystalline peaks for hydroxyapatite and calcium carbonate that are present in the prepared CEnHAp. Dentin treated with CEnHAp-PHS revealed highest microhardness values along with complete tubular occlusion compared to other groups at all test time intervals (p < 05).

Specimens treated with CEnHAp showed increased remineralization than those treated with CPP-ACP followed by PHS and AS groups. ordinary cleanser of mineral peaks, as observed in the EDX and micro-Raman spectra, confirmed these findings. Further, the molecular conformation of the collagen's polypeptide chains, and amide-I and CH2 peaks attained peak intensities in dentin treated with CEnHAp-PHS and PHS whereas other groups revealed poor stability of collagen bands. Microhardness, surface topography, and micro-Raman spectroscopy analyses revealed that dentin treated with CEnHAp-PHS have an improved collagen structure and stability as well as highest mineralization and crystallinity.Conflict of interest statement: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this [Clinicopathologic features of collagenous spherulosis of the breast].OBJECTIVE: To investigate the morphological features, immunohistochemical phenotype, diagnosis and differential diagnosis of collagenous spherulosis of METHODS: Clinicopathologic observation, immunohistochemistry using EnVision method and histochemical staining were applied in 33 cases of collagenous RESULTS: Collagenous spherulosis of the breast was a benign lesion, consisting of proliferative myoepithelial and ductal epithelial cells. These cells were arranged in a cribriform pattern with esinophilic, round, oval or star-shaped fibrillary spherules in the lumen.

SMA, calponin and p63 by immunohistochemistry identified the proliferative myoepithelium, while E-cadherin identified the proliferative ductal epithelial cells. The esinophilic spherules were stained with collagen type IV, AB-PAS and reticulin. Collagenous spherulosis was often CONCLUSIONS: Collagenous spherulosis of the breast is often associated with other diseases. It has special morphological presentation and is easily confused with malignant tumors such as adenoid cystic carcinoma or cribriform carcinoma in situ, and needs to be differentiated from these disease entities.Interaction of the bullous pemphigoid antigen 1 (BP230) and desmoplakin with intermediate filaments is mediated by distinct sequences within their COOH The bullous pemphigoid antigen 1 (BP230) and desmoplakin (DP) are members of the plakin protein family of cytolinkers. Despite their homology, their COOH termini selectively bind distinct intermediate filaments (IFs). We studied sequences within their COOH termini required for their interaction with the epidermal keratins K5/K14, the simple epithelial keratins K8/K18, and type III IF vimentin by yeast three-hybrid, cell transfection, and overlay assays.

The results indicate that BP230 interacts with K5/K14 but not with K8/K18 or vimentin via a region encompassing both the B and C subdomains and the COOH extremity, including a COOH-terminal eight-amino-acid stretch. In contrast, the C subdomain with the COOH-terminal extremity of DP interacts with K5/K14 and K8/K18, and its linker region is able to associate with K8/K18 and vimentin. Furthermore, the potential of DP to interact with IF proteins in yeast seems to be regulated by phosphorylation of Ser 2849 within its COOH terminus. Strikingly, squalane cleanser the ordinary and DP interacted with cytokeratins only when both type I and type II keratins were present. The head and tail domains of K5/K14 keratins were dispensable for their interaction with BP230 or DP. On the basis of our findings, we postulate that linker region between the highly homologous B and C subdomains and their COOH keratins is critically affected by the tertiary structure induced by heterodimerization and involves recognition sites located primarily in the rod Chemistry of collagen cross-linking: biochemical changes in collagen during the partial mineralization of turkey leg tendon.With age, the proximal sections of turkey leg tendons become calcified, and this phenomenon has led to their use as a model for collagen mineralization.

Mineralizing turkey leg tendon was used in this study to characterize further the composition and cross-linking of collagen in calcified tissues.
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