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A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

Calcium-activated nucleotidase 1 (CANT1) is a member of the apyrase family. The CANT1 protein is calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is as follows: UDP > GDP > UTP > GTP. Moreover, CANT1 has a very low activity towards ADP and an even lower activity towards ATP. As well as it doesn’t hydrolyze AMP and GMP. CANT1’s specific function is yet unknown, nevertheless its substrates are involved in several key signaling functions, including Ca2+ release, through activation of pyrimidinergic signaling. Mutations in the CANT1 gene are linked with Desbuquois dysplasia with hand anomalies.

Galectins are a family of animal lectins with an affinity for beta-galactosides. This family has at least 14 identified members. Galectins share similarities in the CRD (the carbohydrate recognition domain). Galectins are synthesized as cytosolic proteins. Though localized principally in the cytoplasm and lacking a classical signal peptide, galectins can also be stimulated to secretion by non-classical pathways or alternatively targeted to the nucleus. Galectins are involved in modulating cell-cell and cell-matrix interactions. Galectin-8 is a tandem-repeat-type member of the galectin family, consisting of 2 CRDs attached by a linker peptide. Galectin-8 is greatly expressed in lung carcinomas, a number of forms of prostate carcinomas, in addition to other tumor cells. Galectin-8 attaches to a subset of cell surface integrins to modulate ECM-integrin interactions. Once immobilized, Galectin-8 promotes cell adhesion by ligation and clustering of cell surface integrin receptors. On the other hand, as a soluble ligand, Galectin-8 can inhibit cell adhesion.

RAN Binding Protein 3, also known as RANBP3, is found in the nucleus and cytoplasm. RANBP3 which owns RanBD1 domain participates in nuclear export as part of a heteromeric complex. RANBP3 is also negatively regulates TGF-beta signaling by interacting with the R-SMAD proteins, SMAD2 and SMAD3.

Cellular Repressor of E1A-Stimulated Genes 1 (CREG1) both activates and inhibits gene expression to stimulate cellular proliferation and hinder differentiation. CREG1 antagonizes transcriptional activation and cellular transformation by E1A. CREG1 shares partial sequence similarity with E1A and binds both the general transcription factor TBP and the tumor suppressor pRb in vitro. CREG1 contributes to the transcriptional control of cell growth and differentiation.

Pancreatitis-associated protein (PAP) is a secretory protein not normally expressed in healthy pancreas but highly induced during acute pancreatitis. While PAP has been shown to be anti-bacterial and antiapoptotic in vitro, its definitive biological function in vivo is not clear. Using antisepse oligonucleotides, inhibition of PAP expression significantly worsened pancreatitis in a rat model. During pancreatitis, PAP released by the pancreas could mediate lung inflammation through induction of hepatic TNF- alpha expression and subsequent increase in circulating TNF-alpha.
PAP is activated in primary liver cancers. In normal liver, the protein is undetectable in normal mature hepatocytes and found only in some ductular cells, representing potential hepatic progenitor cells. PAP can be considered hepatic cytokine that combines mitogenic and anti-apoptotic functions regarding hepatocytes, and consequently acts as a growth factor in vivo to enhance liver regeneration. In pancreatic cancor, PAP was overexpressed in 79% (30 of 38) of pancreatic ductal adenocarcinoma, 19% (7 of 36) of chronic pancreatitis, and 29% (2 of 7) of mucinous cystadenoma. PAP was found in malignant ductular structures in pancreatic carcinomas as well as in benign proliferating ductules and acinar cells in chronic pancreatitis. Elevation of PAP in patients with pancreatic cancer is not merely explainable by concomitant pancreatitis, but seems to be due to increased PAP production by the cancer cells and is also correlated to tumour load as expressed by the UICC stages.
Epithelial expression of PAP was induced under intestinal mucosal inflammation initiated by exposure to commensal bacteria or DSS as well as inflamed IBD colon. Increased serum level of PAP diagnosed ileal location in active Crohn disease with a sensitivity of 60%, a specificity of 94%, a positive predictive value of 84% and a negative predictive value of 81%. Elevated serum PAP (> 50 ng/mL) is significantly associated with disease activity and ileal location of Crohn disease.

S100A4 is part of the S100 super-family of proteins containing 2 EF-hand calcium binding domains. S100A4 is ubiquitously overexpressed and is localized in the cytoplasm and/or nucleus. S100A4 is involved in motility, invasion, and tubulin polymerization. Chromosomal rearrangements and altered expression of the S100A4 gene have been implicated in tumor metastasis.

Fibrinogen silencer-binding protein (FSBP), interacts with X11alpha. The X11alpha/FSBP complex send signals to the nucleus in order to repress glycogen synthase kinase-3beta promoter activity. X11alpha is a neuronal adaptor protein that interacts with the amyloid precursor protein (APP) via a centrally located phosphotyrosine binding domain to inhibit the production of Abeta peptide that is deposited in Alzheimer's diseased brains.

ITGB4 (integrin beta-4 isoform 1) belongs to the Integrin beta family. ITGB4 forms noncovalent heterodimers with Integrin alpha 6 and takes part in the formation of epithelial hemidesmosomes. ITGB4 has a vital structural role in the hemidesmosome of epithelial cells and is needed for the regulation of keratinocyte motility & polarity. ITGB4 leans towards the association with alpha 6 subunit and is expected to take a key role in the biology of invasive carcinoma.

Prolactin-inducible protein (PIP) is a main protein component of benign breast gross cysts. PIP is a famous indicator of breast cancer, since it is found in around 50% of all breast cancer specimens. PIP is expressed in exocrine glands, in pathologic conditions, in breast cysts and breast cancers exhibiting apocrine features. PIP and prostate specific antigen are co-expressed in androgen receptor-positive breast tumours.

ACTN1 encodes a nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene. Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments.

S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.

C8, a component of the complement system consists of three polypeptides C8A, C8B and C8G and takes part in the formation of Membrane Attack Complex (MAC). Patients with C8 deficiency are exposed to several bacteria infections. C8G, a member of the lipocalin family and calycin superfamily, is a secreted protein that can bind retinol. C8G is created in the liver, monocytes and fibroblast and has a role in clearing pathogens from an infected host.

HMGB3 is a member of the high mobility group (HMG) protein superfamily. HMGB3 holds DNA-binding HMG box domains, as do HMG1 and HMG2, and like the rest of the HMG protein superfamily members has a vital part in DNA replication, transcription and nucleosome assembly.

SERPINI1 (Neuroserpin) is an inhibitory serpin which is expressed primarily in the central nervous system. Even though the physiological target of SERPINI1 is still vague, amassed evidence suggest that SERPINI1 has an imperative role in controlling proteolytic degradation of extracellular matrix (ECM) during synaptogenesis and the subsequent development of neuronal plasticity. The neuroprotective role of SERPINI1 has been demonstrated in transgenic mice lacking SERPINI1 expression. The deficiency of SERPINI1 in these mice is linked with motor neuron disease characterized by axonal degradation. In humans, defects in SERPINI1, caused by point mutations in the neuroserpin gene, trigger a hereditary disorder known as the familial encephalopathy with neuroserpin inclusion bodies (FENIB).

Uroplakin 2 (UPK2) is one of the proteins of the highly urothelium-specific integral membrane proteins of the asymmetric unit membrane which forms urothelium apical plaques in mammals. The asymmetric unit membrane is thought to strengthen the urothelium by preventing cell rupture during bladder distention. The UPK2 protein is expressed in the peripheral blood of bladder cancer patients with transitional cell carcinomas.

Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.

WIBG is a cooperateing partner of Mago-Y14. The Mago-Y14 heterodimer is a key protein of the EJC(exon junction complex) that is deposited on mRNAs as a consequence of splicing and influences postsplicing mRNA metabolism. WIBG is a cytoplasmic RNA-binding protein that is excluded from the nucleus by Crm1. WIBG relates directly with Mago-Y14 by means of its N-terminal domain.

TRIM21 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The 52 kDa Ro protein is part of the RoSSA ribonucleoprotein, which includes a single polypeptide and one of four small RNA molecules. The RoSSA particle localizes to both the cytoplasm and the nucleus. Ro/SSA interacts with autoantigens in patients with Sjogren syndrome and systemic lupus erythematosus. Ribonucleoprotein particle is composed of a single polypeptide and one of four small RNA molecules. The RoSSA is present in all mammalian cells studied but has no known function. At least 2 isoforms are present in nucleated and red blood cells, and tissue specific differences in Ro/SSA proteins were identified.

UPK3A is a member of the uroplakin-3 family. Uroplakins (UP) which are transmembrane proteins are important components of the urothelium that pass the lipid bilayer once (UPII, UPIIIa, and UPIIIb) or four times (UPIa and UPIb; both members of the "tetraspanin" family). All hold great luminal/extracellular domains, but only UPIIIa and UPIIIb have significant cytoplasmic shares in their C-termini. UPK3A is an extremely specific and moderately sensitive immunohistochemical marker for primary and metastatic urothelial carcinomas. Alterations in this gene are related to renal adysplasia.

COMP is a non-collagenous glycoprotein and is belongs to the thrombospondin family of extracellular proteins. COMP is a calcium-binding protein of high molecular weight (>500kDa) found in the extracellular matrix of articular, nasal and tracheal cartilage. COMP is not only cartilage-derived but is common in other tissues, such as synovium and tendon. Intact COMP is pentameric, with 5 equal subunits and the carboxy-terminal globular domain of native COMP binds to collagens I, II, and IX. COMP molecules are vital for conserving the properties and integrity of collagen network. Moreover, COMP has a storage and delivery function for hydrophobic cellsignaling molecules such as vitamin D. Mutations of the COMP gene cause Pseudoachondroplasia and some forms of multiple epiphyseal dysplasia which implicates that it is vital that COMP develops and functions normally.

CPPED1 which is a part of the metallophosphoesterase superfamily takes part in glucose uptake by adipocytes. CPPED1 binds two divalent metal cations and is transactivated by the great envelope protein of the hepatitis B virus.

N-Myc Downstream Regulated 3, also known as NDRG3, is a protein coding gene which is a part of the NDRG family and is expressed greatly in brain. NDRG2 is an important paralog of NDRG3.

Autophagy Related 3 (ATG3) is a conjugating enzyme essential for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. ATG3 is localizes to the cytoplasm and is expressed in tissues with predominant levels found in kidney, placenta, liver, heart and skeletal muscle. ATG3 catalyzes a reaction which is necessary for autophagy. That reaction is the formation of the Atg8-phosphatidylethanolamine (ATG-PE) conjugate.