Please Wait...

Musculoskeletal

sRANKL (Total) // Total Soluble Receptor Activator of Nuclear Factor Kappa B Ligand

Formerly known as TNF-related activation-induced cytokine (TRANCE), the receptor activator of Nf-κB ligand (RANKL) was initially identified as an osteoprotegerin ligand (Lacey et al., 2012). RANKL is a member of the TNF superfamily and exists as a transmembrane protein and in a soluble form (after proteolytic cleavage or alternative mRNA splicing). There are three known spliced variants in human and the smallest of these three variants lacks the transmembrane and the intracellular domain and is directly secreted.

UcOC // Undercarboxylated Osteocalcin

Osteocalcin (OC), also called bone γ-carboxyglutamic acid protein (BGP), is a 49 residues containing non-collagenous protein found in bone and dental tissues. OC is produced by osteoblasts and is a vitamin K dependent protein implicated in bone formation. Initially identified as a protein limiting bone formation, new functions such as implication in glucose metabolism, reproduction and cognition have been identified since (Ducy et al., 1996; Zoch et al., 2016). OC binds to hydroxyapatite and a fraction of the newly synthetized protein is then released in blood circulation.

SOST // Sclerostin

Scleroteosis is a genetic disorder caused by the loss of the SOST gen product. Studies of this disease characterized, among other clinical features, by progressive bone overgrowth, facial distortion, entrapment of cranial nerves and high intracranial pressure have allowed the identification of the Sclerostin (SOST) protein, which is implicated in the regulation of bone mass (Balemans et al., 2001). SOST is a glycoprotein with a cysteine-knot motif which belongs to the DAN/Cerberus family and is secreted mainly by bone dwelling osteocytes (Veverka et al., 2009).

sRANKL // Free Soluble Receptor Activator of Nuclear Factor Kappa B Ligand

Formerly known as TNF-related activation-induced cytokine (TRANCE), the receptor activator of Nf-κB ligand (RANKL) was initially identified as an osteoprotegerin ligand (Lacey et al., 2012). RANKL is a member of the TNF superfamily and exists as a transmembrane protein and in a soluble form (after proteolytic cleavage or alternative mRNA splicing). There are three known spliced variants in human and the smallest of these three variants lacks the transmembrane and the intracellular domain and is directly secreted.

PYD // Pyridinium Crosslinks

Pyridinium Crosslinks (PYD) or Pyridinoline is a non-reducible crosslinks of collagen formed during collagen maturation. High levels of PYD are found in cartilage, in comparison with bone levels. PYD crosslinks measured in urine reflect bone resorption (Seibel et al., 1992). In bone, the crosslinks of mature collagen are: PYD and deoxypyridinoline, they are released in circulation and urine during bone resorption (Delmas, 1993).

PTH, Whole // Whole Parathyroid Hormone

PTH is produced in the parathyroid gland and is a key regulator in skeletal and mineral homeostasis. PTH is a 84 amino-acid peptide, with an helical conformation in the 1-34 portion of its binding domain to its receptor of type 1 (PTH1R) (Jin et al., 2000). PTH and PTH-related peptide (PTHrP) have highly conserved sequences and activates PTH1R. The C terminal fragments of the intact PTH, PTH(39-84) or PTH(53-84) bind another receptor CPTHR, expressed on bone cells (Divieti et al., 2001).

PTH, Intact // Intact Parathyroid Hormone

PTH is produced in the parathyroid gland and is a key regulator in skeletal and mineral homeostasis. PTH is a 84 amino-acid peptide, with an helical conformation in the 1-34 portion of its binding domain to its receptor of type 1 (PTH1R) (Jin et al., 2000). PTH and PTH-related peptide (PTHrP) have highly conserved sequences and activates PTH1R. The C terminal fragments of the intact PTH, PTH(39-84) or PTH(53-84) bind another receptor CPTHR, expressed on bone cells (Divieti et al., 2001).

PINP // Procollagen Type I N-Propeptide

In bone, type I collagen constitute 90% of the organic matrix. Type I collagen is first synthetized as a type I procollagen and then cleaved at its two extremities. The two cleavage fragments, named N-terminal propeptide of type I collagen (PINP) and carboxy-terminal pro-peptide (PICP) are released and are measurable in blood. Their presence in the peripheral circulation is indicative of bone formation (but not specific)(Garnero et al., 2008; Naylor and Eastell, 2012).

PIIANP // Procollagen Type IIA N-Propeptide

Type II collagen constitute 60% of cartilage weight and is found exclusively in cartilaginous tissues. Type II pro-collagen is subjected to differential splicing and produces two forms of amino-pro-peptide: PIIANP and PIIBNP, containing respectively the type IIA and type IIB exons (Rousseau, 2004). The IIB form is lacking the domain codded by exon 2: a 69-amino-acid cysteine-rich globular domain (Garnero et al., 2002). PIIANP can be specifically measured and is a biomarker for a collagen type II synthesis (Elsaid and Chichester, 2006; Rousseau, 2004).

Phosphorus

Phosphorus is present in the organism under different forms and, as a key element, is indispensable in cell processes and metabolism. In soft tissues, phosphorus exists as inorganic and organic forms (incorporated in macromolecules). Bones and teeth contain more than 80% of total phosphorus. Inorganic phosphorus is also present in serum and higher levels may reflect increased bone resorption (Takeda et al., 2012). Higher serum levels are also associated with higher risk of cardiovascular diseases (Menon and Ix, 2013).

OPN / / Osteopontin

Identified in bone calcified matrix, Osteopontin (OPN) is also called Bone Sialoprotein I and belongs to the Small Integrin-Binding Ligand, N-linked Glycoprotein (SIBLING) family of protein (Franzen and Heinegard, 1985). OPN contain an RGD motif which allow interaction with integrins and cell surface receptors (Oldberg et al., 1986). OPN interacts with various other partners, can be cleaved by thrombin and in some conditions also by MMP-3 and MMP-7. The resulting fragments have then specific properties which result in modulation of cell migration and adhesion (Bellahcène et al., 2008).

OPG // Osteoprotegerin

Osteoprotegerin (OPG) is a secretory glycoprotein composed of 401 amino acids (mature form with 380 amino acids) and seven structural domains. OPG exists as a disulfide-linked homodimer or as a monomer (Simonet et al., 1997). OPG belongs to the TNF receptor superfamily and was initially described as a cytokine, binding essentially the Receptor Activator of Nuclear Factor κβ Ligand (RANKL).Since, OPG have been found to be implicated in other pathways (Baud’huin et al., 2013).

OC // Osteocalcin

Osteocalcin (OC), also called bone γ-carboxyglutamic acid protein (BGP), is a 49 residues containing non-collagenous protein found in bone and dental tissues. OC is produced by osteoblasts and is a vitamin K dependent protein implicated in bone formation. Initially identified as a protein limiting bone formation, new functions such as implication in glucose metabolism, reproduction and cognition have been identified since (Ducy et al., 1996; Zoch et al., 2016). OC binds to hydroxyapatite and a fraction of the newly synthetized protein is then released in blood circulation.

NTX-I // N-Terminal Crosslinked Telopeptide of Type I Collagen

In bone, type I collagen constitute 90% of the organic matrix. Markers of bone resorption in serum or urine can be used to assess changes in bone resorption in various bone diseases or under treatment (Naylor and Eastell, 2012). Cross linked amino-terminal collagen (NTx-I) are peptides derived from the degradation of collagen I. Measurement of these peptides in urine or serum provide information about the bone resorption rate.

Pages

LEARN MORE OR SPEAK WITH OUR EXPERTS

CONTACT US
Leader in Clinical Trial
Management Solutions

Successful clinical trials require the ability to see key details and uncover hidden insights. Bioclinica utilizes science and technology to bring clarity to clinical trials, helping companies to develop new life-improving therapies more efficiently and safely.

With many clinical trials slowed or terminated, investments in new technologies are difficult. Yet, a #CTMS with a… https://t.co/VRIhWWf4tE
Bioclinica (5 days ago)
With Bioclinica #CTMS, sponsors & CROs have access to a full-featured, scalable system - a single, centralized sour… https://t.co/7ACrv8cvuF
Bioclinica (1 week ago)
Now available: a DIY #EDC solution. From study start-up to close-out, Bioclinica EDC Solo is an efficient, cost-eff… https://t.co/vFhC7ITfZV
Bioclinica (2 weeks ago)
Reduce the number of user requirement iterations and UAT findings during the #IRT build process. With the agile app… https://t.co/TJt2sZlrFP
Bioclinica (2 weeks ago)
Don't compromise with manual systems and spreadsheets. As an entry-level system with phased implementation, Bioclin… https://t.co/qIpi1MESXw
Bioclinica (3 weeks ago)
According to our recent poll, 45% of respondents had neither a #CTMS nor an #eTMF system, while only 24% had both.… https://t.co/l4dKC7pBQo
Bioclinica (3 weeks ago)