The glycosylation profile of osteoadherin alters during endochondral bone formation.

Endochondral bone formation involves the dynamic interplay between the cells and their extracellular environment to facilitate the deposition of a calcified matrix. Numerous molecules are involved within this process, including collagens and non-collagenous proteins, and their post-translational modifications have been shown to effect their biomolecular interactions. Osteoadherin (OSAD), a keratin sulfate (KS)-substituted small leucine-rich proteoglycan has been isolated from mineralized tissues and is considered to be a mineralized tissue-specific protein.

Low-dose radiation with 80-kVp computed tomography to diagnose pulmonary embolism: a feasibility study.

Background: Mounting collective radiation doses from computed tomography (CT) implies an increased risk of radiation-induced cancer in exposed populations, especially in the young.

Purpose: To evaluate radiation dose and image quality at 80-kVp CT to diagnose acute pulmonary embolism (PE) compared with a previous study at 100 and 120 kVp with all other scanning parameters unchanged.

Material And Methods: A custom-made chest phantom with a 12 mg I/mL-syringe was scanned at 80/100/120 kVp to evaluate relative changes in computed tomographic dose index (CTDI(vol)), attenuation, image noise, and contrast-to-noise ratio (CNR).

Osteoadherin accumulates in the predentin towards the mineralization front in the developing tooth.

Background: Proteoglycans (PG) are known to be involved in the organization and assembly of the extracellular matrix (ECM) prior to mineral deposition. Osteoadherin (OSAD), a keratan sulphate PG is a member of the small leucine-rich (SLRP) family of PGs and unlike other SLRPs, OSAD expression is restricted to mineralized tissues. It is proposed to have a high affinity for hydroxyapatite and has been shown to be expressed by mature osteoblasts but its exact role remains to be elucidated.

Substitution of bovine dentine sialoprotein with chondroitin sulfate glycosaminoglycan chains.

Dentine sialoprotein (DSP) represents 5-8% of all non-collagenous proteins present in the tooth, but, together with dentine phosphoprotein, has been shown to be vital for correct tooth formation. Recently, the existence of a highly glycosylated form of porcine DSP has been reported and it was shown to possess glycosaminoglycan (GAG) chains. The current investigation confirms that this is also the case for bovine DSP and has further characterized these carbohydrates.