PubMed · 13793741
The source did not provide an abstract. Follow the original record for more information.
Explore connections, maps & timelines
H ANNAMUNTHODO. 1960. Calcinosis.. https://doi.org/10.1016/0002-9610(60)90496-7
Cite the original work for its findings. Save a collection to share your selection of sources.
KEEP EXPLORING
Bone and dentin biomineralization are well-regulated processes mediated by extracellular matrix proteins. It is widely believed that specific matrix proteins in these tissues modulate nucleation of apatite nanoparticles and their growth into micrometer-sized crystals via molecular recognition at the protein-mineral interface. However, this assumption has been supported only circumstantially, and the exact mechanism remains unknown. Dentin matrix protein 1 (DMP1) is an acidic matrix protein, present in the mineralized matrix of bone and dentin. In this study, we have demonstrated using synchrotron small-angle X-ray scattering that DMP1 in solution can undergo oligomerization and temporarily stabilize the newly formed calcium phosphate nanoparticle precursors by sequestering them and preventing their further aggregation and precipitation. The solution structure represents the first low-resolution structural information for DMP1. Atomic force microscopy and transmission electron microscopy studies further confirmed that the nascent calcium phosphate nuclei formed in solution were assembled into ordered protein-mineral complexes with the aid of oligomerized DMP1, recombinant and native. This study reveals a novel mechanism by which DMP1 might facilitate initiation of mineral nucleation at specific sites during bone and dentin mineralization and prevent spontaneous calcium phosphate precipitation in areas in which mineralization is not desirable.
This paper presents a 3D localization method to register clustered microcalcifications on mammograms from cranio-caudal (CC) and medio-lateral oblique (MLO) views. The method consists of three major components: registration of clustered microcalcifications in CC and MLO views, 3D localization of clustered microcalcifications and 3D visualization of clustered microcalcifications. The registration is performed based on three features, gradient, energy and local entropy codes that are independent of spatial locations of microcalcifications in two different views and are prioritized by discriminability in a binary decision tree. The 3D localization is determined by a sequence of coordinate corrections of calcified pixels using the breast nipple as a controlling point. Finally, the 3D visualization implements a virtual reality modeling language viewer (VRMLV) to view the exact location of the lesion as a guide for needle biopsy. In order to validate our proposed 3D localization system, a set of breast lesions, which appear both in mammograms and in MR Images is used for experiments where the depth of clustered microcalcifications can be verified by the MR images.
X-linked hypophosphatemia (XLH), the most common form of hereditary rickets, is caused by loss-of-function mutations of PHEX gene in osteoblast cells, leading to rachitic bone disease and hypophosphatemia. Available evidence today indicates that the bone defect in XLH is caused not only by hypophosphatemia and altered vitamin D metabolism, but also by locally released osteoblastic mineralization inhibitory factor(s), referred to as minhibin. In our present study, we found that suppression of PHEX expression by PHEX antisense in human osteoblast cells caused an increase in cathepsin D expression at protein, but not mRNA, levels. This was associated with a decrease in cathepsin D degradation and an increased cathepsin D release into culture media. Our results also showed that lowering cathepsin D activity in antisense cell conditioned media abolished their inhibitory effect on osteoblast cell calcification, suggesting the involvement of cathepsin D in mediating the minhibin activity of the antisense cell conditioned media.