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Oncology

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.

VEGF-A // Vascular Endothelial Growth Factor

Vascular Endothelial Growth Factor A (VEGF-A or VEGF) is a member of the Platelet-derived growth factor (PDGF) family and is implicated in embryogenic development, angiogenesis and vascular permeability (Coultas et al., 2005). Biological activities of VEGF-A are mediated through binding with VEGFR-1 and VEGFR-2, two related tyrosine kinases receptors (Ferrara et al., 2003). VEGF-A exist under several isoforms (at least 7 different spliced variants) which have different capacities to bind heparin and heparin-sulfate and are differentially expressed during development (Byrne et al., 2005).

TIMP-1 // Tissue Inhibitor of 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). Tissue Inhibitor of Metalloproteinase family comprises 4 members. They are two-domain proteins with a N-Terminal domain of approximately 125 residues and a C terminal domain of about 65 residues (Brew et al., 2000).

Survivin

Survivin is the smallest member of the Inhibitor of Apoptosis Protein (IAP) family. The eight members of the IAPs family contain Baculoviral IAP Repeat (BIR) motifs. Initially identified in bacculovirus, BIR motif is a sequence of approximately 70 amino acids that coordinates a zinc ion (through histidine and cystine residues)(Srinivasula and Ashwell, 2008). Survivin expression was detected in different solid cancers and lymphomas (Ambrosini et al., 1997).

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.

PSA // Prostate Specific Antigen

Prostate Specific Antigen (PSA) is a member of the Kallikrein related peptidase and is also known as Kallikrein-Related peptidase 3 (KLK3). Its major physiological function is the liquefaction of seminal fluid through its proteolysis activity against gel proteins. PSA is normally found in seminal fluid and only a small proportion is found in blood. The release of PSA in blood circulation is believed to be the result of architecture modification and alterations in the basement membrane when prostate tumors develop (Lilja et al., 2008).

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).

PIIINP // Intact N-Terminal Propeptide Of Type III Collagen

Type III collagen is present in many tissues, such as skin, vascular vessels, ligaments, skeletal muscles, synovial membrane and connective tissues. Type III collagen is an homotrimer of α1 chains encoded by a single gene (Wu et al., 2010). Collagen type III is synthetized as a large procollagen which is subjected to cleavage of its N-terminal peptide and this N-terminal propeptide of collagen type III (PIINP) is released in the blood circulation in direct proportion to newly formed type III collagen.

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).

MMP-13 // Pro-Matrix Metalloproteinase 13

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-13 is also called collagenase 3 and cleaves the interstitial collagens types I, II and III with a high potency against collagen of type II (the major component of cartilage)(Leeman et al., 2002).

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-8 // Total Matrix Metalloproteinase 8

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-8 is also known as collagenase-2 or neutrophil collagenase and is implicated in the degradation of a wide range of substrates: type I, II and III collagens, proteoglycans, fibronectin, fibrinogen, angiotensin I, substance P, Angiotensin, CXCL10 and many others (Lenglet et al., 2013; Van Lint and Libert, 2006).

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).

CTX-I // C-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). Collagen in bone can be isomerized with racemization of the aspartic residues in the CTX telopeptide. The newly formed collagen is α isomerized and β isomerization occurs with aging (Garnero, 2012). In urine, the ratio between native and isomerized CTX can give an estimate of the extent of type I collagen isomerization in bone tissue (Cloos and Fledelius, 2000).

COL4 // Type IV Collagen

Type Collagen IV is encoded by six genes: COL4A1, COL4A2, COL4A3, COL4A4, COL4A5, and COL4A6 for the six collagen chain implicated in its composition: α1(IV) through α6(IV). The assembly of collagen IV network is highly regulated. Each of the six chains present the same features with three domains: short 7S N-Terminal, collagenous domain and non-collagenous domain (NC1) in C-terminal and can form three sets of helical molecules. Depending on the tissues the set of collagen type IV molecules is different.

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