China
Africa
Explore chapters and articles related to this topic
Osteoporosis
Published in Peter V. Giannoudis, Thomas A. Einhorn, Surgical and Medical Treatment of Osteoporosis, 2020
Ippokratis Pountos, Peter V. Giannoudis
Bone sialoprotein (BSP) is a phosphorylated glycoprotein that accounts for up to 10% of the noncollagenous proteins of the bone matrix. It is the product of osteoblasts and odontoblasts; hence, it is relatively limited to mineralized tissues. It is believed to be an adhesion molecule of cells to the extracellular matrix and facilitates the organization of the extracellular matrix.
The locomotor system
Published in C. Simon Herrington, Muir's Textbook of Pathology, 2020
The protein matrix of bone consists largely of type I collagen produced by osteoblasts. There are, in addition, small amounts of non-collagenous proteins including calcium-binding proteins such as osteonectin and bone sialoprotein and those involved in mineralization such as osteocalcin. Cell adhesion proteins, including osteopontin and growth factors including transforming growth factor (TGF), are also present.
Muscle, Bone, and Skin Disorders
Published in Victor A. Bernstam, Pocket Guide to GENE LEVEL DIAGNOSTICS in Clinical Practice, 2019
The elevated c-myc mRNA level in some tumors is accompanied by a low expression of osteopontin (bone sialoprotein) and of bone Gla protein, another marker of highly differentiated osteogenic cells.
Understanding collagen interactions and their targeted regulation by novel drugs
Published in Expert Opinion on Drug Discovery, 2021
Marialucia Gallorini, Simone Carradori
Vitronectin (VN) is a multifunctional glycoprotein which binds to different biological ligands and, by binding to different types of integrins, mostly via the RGD sequence, plays a key role in tissue remodeling by controlling cell adhesion. In addition to that, VN owns two domains for collagen-binding and interacts with collagens I, II, III, IV, V and VI. As for fibronectin (FN), its interactions with collagen are crucial during the genesis of fibrils. Fibronectin has also been discovered as a target protein for the diagnosis of high-risk micro-metastasis of breast cancer. A successful approach to prevent metastatic invasion could be the selective delivery of therapeutic drugs to highly fibronectin-expressing metastatic tumor sites [93]. Finally, the crosstalk between collagens and non-collagenous bone proteins, such as bone sialoprotein II (BSPII) and osteonectin (SPARC, secreted protein acidic and rich in cysteine), is involved in tissue remodeling and cancer-related metastases. The SPARC protein has furthermore been identified as a potential therapeutic target to prevent breast cancer bone metastasis [94].
Green nanotechnology-based drug delivery systems for osteogenic disorders
Published in Expert Opinion on Drug Delivery, 2020
David Medina-Cruz, Ebrahim Mostafavi, Ada Vernet-Crua, Junjiang Cheng, Veer Shah, Jorge Luis Cholula-Diaz, Gregory Guisbiers, Juan Tao, José Miguel García-Martín, Thomas J. Webster
Oligopeptides are small sequences of amino acids, naturally present in the human body, which have the ability to link to HA when aspartic acid (Asp) and glutamic acid (Glu) residues are present in their structure, preventing bone resorption [32,33]. Osteopontin and bone sialoprotein are two major noncollagenous proteins in bone, which have both L-Asp and L-Glu repetitive sequences in their structure, respectively, aiding the process of rapid binding to HA once secreted in osteoblastic cell culture. Thus, these oligopeptides are suitable candidates as bone-targeting agents that can be combined with different drugs (Figure 1(b)). For instance, after systemic administration, a drug tagged with an oligopeptide can be selectively delivered to bind with bone, acting as the active drug which is gradually released during the bone remodeling process [34–36].
Colorectal carcinoma screening: Established methods and emerging technology
Published in Critical Reviews in Clinical Laboratory Sciences, 2020
Erika Hissong, Meredith E. Pittman
Emerging technologies that utilize alterations identified in peripheral blood are currently being explored to develop serum-based screening tests. Peripheral blood samples are easier to handle and store than stool samples, and a serum sample may be more appealing to patients, despite the need for phlebotomy, simply because phlebotomy has become a routine part of medical care [100–102]. Various circulating markers have been considered including proteins (i.e. cancer antigen (CA) 19–9, carcinoembryonic antigen (CEA), urokinase-type plasminogen activator (u-PA), soluble CD26 (sCD26)), DNA markers, and mRNA markers [103–110]. Sensitivities among different protein markers can vary widely, but some studies show high sensitivities and specificities for markers such as serum CD26, bone sialoprotein, and prolactin [111–113]. In addition, proteomic profiling using surface enhanced laser desorption/ionization time-of-flight mass spectrometry (SELDI-TOF-MS) has demonstrated the ability to detect candidate tumor derived serum markers in small study populations; however, reproducibility and validation of SELDI-TOF results have so far been limited [114–117].