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Serum

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.

MMP-9 // Active and Pro-Matrix Metalloproteinase 9

The MMPs family comprises at least 24 different MMPs with high sequence similarity in their catalytic domains. MMPs are synthetized as pro-enzymes which are inactive until removal of their pro-domain (Löffek et al., 2011; Nagase and Woessner, 1999). MMP-9 is also called gelatinase B and its expression is induced by numerous factors including TGF-β, TNF-α and VEGF. MMP-9 degrades denatured collagens, matrix associated substrate, aggrecan and can also convert some cytokines into more active or inactive immune signals (Vandooren et al., 2013).

MMP-3 // Active and Pro-Matrix Metalloproteinase 3

The MMPs family comprises at least 24 different MMPs with high sequence similarity in their catalytic domains. MMPs are synthetized as pro-enzymes which are inactive until removal of their pro-domain (Löffek et al., 2011; Nagase and Woessner, 1999). Matrix metalloproteinase 3 (MMP-3, also known as stromelysin-1), secreted by chondrocytes and synovial cells, activates other proteases and has a broad substrate specificity for degrading extracellular matrix components (fibronectin, laminin, elastin, collagen IV, and proteoglycans)(Kim and Hwang, 2011; Murphy et al., 1991).

MMP-1 // Pro-Matrix Metalloproteinase 1

The MMPs family comprises at least 24 different MMPs with high sequence similarity in their catalytic domains. MMPs are synthetized as pro-enzymes which are inactive until removal of their pro-domain (Löffek et al., 2011; Nagase and Woessner, 1999). MMP-1 is also called Collagenase 1 or Fibroblast collagenase and is believed to degrade type I, II and III fibrillary collagens in the extracellular matrix. MMP-1 is implicated in different remodeling process in connective tissues as well as in inflammation and immunity (Parks et al., 2004).

IL-18 // Interleukin 18

Interleukin 18 (IL-18) belongs to the IL-1 family and is produced by macrophages, dendritic cells and epithelial cells (keratinocytes). Pro-IL-18 is expressed constitutively and is then activated by caspase 1. Its receptor is IL-18R and the pro-inflammatory signaling requires the formation of a complex containing IL18, IL18R and IL-18RAP (Sims and Smith, 2010). In normal condition, IL-18 activity is lowered by high levels of IL-18 Binding Protein (IL-18BP). Binding of IL-18BP to IL-18 prevents its interaction with IL-18R.

IL-6 // Interleukin 6

Interleukin 6 (IL-6) was initially identified as a differentiation factor for B-cells and was then named: B-cell stimulatory factor 2 (Naka et al., 2002). IL-6 is a pleiotropic cytokine produced by different types of cells (T cells, B cells, monocytes, fibroblasts, keratinocytes, endothelial cells, mesangial cells and some tumor cells). This cytokine has also a wide range of effect on different target through trans- or classical signaling with the IL-6R system (Calabrese and Rose-John, 2014).

IL-1β // Interleukin 1 beta

Interleukin 1β (IL-1β) belongs to the IL-1 family. In this family IL-1α and IL-1β bind to the same receptor and have identical biological activity. IL-1β is secreted, circulate in the bloodstream, and have a systemic activity, when IL-1α is generally associated with the producing cells plasma membrane and acts more locally (Sims and Smith, 2010). Active Il-1β is produced by cleavage ofpro-IL-1β by caspase-1 or neutrophil protease.

IGFBP-3 // Insulin-Like Growth Factor Binding Protein 3

The majority of Insulin Like Growth Factors (IGFs) in serum is complexed with IGF Binding Proteins (IGFBP) and acid-labile subunit (ALS). Six IGFBPs have been cloned and identified. IGFBP3 has the highest binding capacity for IGF-1 and it prolonged its high life in serum. GFBPs in serum regulate the endocrine actions of IGFs by modulating bioavailable IGF (Mohan and Baylink, 2002). IGFBPs constitute a "buffer" capable of limiting the effect of a rise in IGF concentration (which could result in hypoglycemia) (Ranke, 2015).

IGF-1 // Insulin-Like Growth Factor I or Somatomedin C

Insulin Like Growth Factor 1 (IGF-1) and 2 (IGF-2) are produced mainly by hepatocytes, and to a lesser extent in other tissues (Ranke, 2015). IGF-1 and IGF-2 have structural and sequence homology with insulin and also shared some biological functions. These hormone were assigned in 1978 to the family of somatomedins (Rinderknecht and Humbel, 1978a, 1978b). Higher risks of cancer were found to be associated with high IGF-1 levels in serum. This can be the result of IGF-1 influence on epithelial-cell population renewal rates and of its anti-apoptotic effect (Pollak et al., 2004).

ICTP // C-Terminal 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). Degradation of collagen Type I in bone is mediated by two types of proteinases: cysteine proteinases and Matrix Metalloproteinases (MMPs). ICTP is the product of collagen I degradation by MMPs in opposition to CTX-I which is produced through the cysteine proteinase Cathepsin K action (Garnero et al., 2003).

HA // Hyaluronic Acid

Hyaluronic acid (HA) is also known as hyaluronate or hyaluronan. This macromolecule is a ubiquitous linear polymer, especially abundant in connective tissues. HA is synthetized in the plasma membrane by a membrane-bound protein by addition of sugar units (D-glucuronic acid and D-N-acetylglucosamine, linked via alternating β-1,4 and β-1,3 glycosidic bonds) from a nucleotide precursor and followed by translocation to the extracellular space (Fraser et al., 1997).

FSH // Follico-Stimulating Hormone

Follicle-Stimulating Hormone is one of the four glycoprotein hormones. Proteins of this family share a common α subunit and have a specific β subunit. They present structural features of the superfamily of cysteine knot protein (this superfamily contain the TGFβ family, bone morphogenetic proteins, …) (Fan and Hendrickson, 2005; Grossmann et al., 1997; Vitt et al., 2001).

Fetuin-A

Fetuin A, also known as α-2-HS glycoprotein (AHSG) is a well conserved glycoprotein implicated in the regulation of phosphorus and calcium homeostasis. Fetuin-A has also a role in inflammation and metabolic disease as it binds to minerals, lipids, lectins, proteases and has TGF-β antagonist and insulin receptor antagonist action. Fetuin A is synthetized by the liver and circulates in blood at high concentrations. For example, fetal calf serum contains less albumin than fetuin-A (Jahnen-Dechent et al., 2011).

DKK-1 // Dickkopf Related Protein-1

Dickkopf family members are involved in the modulation of Wnt signaling. DKK1, the first member of this family (which comprises at least 4 cystein-rich protein), is an inhibitor of Wnt signaling. DKK1 has been found to not only promote bone resorption in a mouse model of arthritis but also to block bone formation and repair of diseased joint (Diarra et al., 2007). DKK1 appeared as a central player in bone homeostasis with implication in bone development and maintenance of bone mass as well as in formation of bone metastases (Pinzone et al., 2009).

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