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L-Selectin belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. The L-Selectin molecule is composed of various domains: one homologous to lectins, one to epidermal growth factor, and two to the consensus repeat units found in C3/C4 binding proteins.
L-selectin is expressed constitutively on lymphocytes, monocytes and granulocytes and interacts specifically with carbohydrate groups on activated endothelial cells. L-Selectin may be shed by proteolytic cleavage and circulating levels in biological fluids may be used as an indicator of various pathological conditions. L-Selectin is cleaved by ADAM17.
L-selectin works as a "homing receptor" for leukocytes to enter secondary lymphoid tissues via the high endothelial venules. Ligands present on endothelial cells will attach to leukocytes expressing L-selectin, which causes the leukocytes to become localized at that juncture. The receptor is also located on the cell surfaces of "naive" T cells, which have not yet encountered their particular antigen. This surface expression is lost following the cells activation.

Galectin 3, or LGALS3, is a protein which belongs to the animal lectins family, that binds betagalactoside residues selectively. LGALS3 is originated and leaves cells through ectocytosis. The protein is capable of inhibition apoptosis and the development of cancer. Galectin 3 is found in epithelial tissues in organisms, it can be located in dendritic cells, Kupffer cells, macrophages etc. LGALS3 levels elevated when inflammation is generating, cell proliferation, trans-activation by viral proteins and cell differentiation.

Hepatitis A virus cellular receptor 1 (HAVCR1) is a membrane receptor for both human hepatitis A virus (HHAV) and TIMD4. HAVCR1 is a type I trans-membrane structural glycoprotein located in the renal proximal tubule epithelial cells. HAVCR1 protein may be involved in the control of asthma and allergic diseases. The reference genome represents an allele which retains a MTTVP amino acid segment that presents defense against atopy in HHAV seropositive individuals.

CD200 is a type-1 membrane glycoprotein which is a part of the immunoglobulin superfamily due to its 2 immunoglobulin domains. CD200 regulates myeloid cell activity and delivers an inhibitory signal for the macrophage lineage in various tissues. CD200 is also Costimulates T-cell proliferation.

Hepatitis A virus cellular receptor 1 (HAVCR1) is a membrane receptor for both human hepatitis A virus (HHAV) and TIMD4. HAVCR1 is a type I trans-membrane structural glycoprotein located in the renal proximal tubule epithelial cells. HAVCR1 protein may be involved in the control of asthma and allergic diseases. The reference genome represents an allele which retains a MTTVP amino acid segment that presents defense against atopy in HHAV seropositive individuals.

Nectin Cell Adhesion Molecule 2, also known as NECTIN2, is a Ca(2+)-independent cell-cell adhesion molecule which is one of the plasma membrane components of adherens junctions. NECTIN2 takes a vital part in the establishment of homotypic as well as heterotypic cell to cell contacts. NECTIN2 is essential for resisting herpes simplex virus type 2 infection in transfected cells. NECTIN2 is also a possible target for antibody therapy of breast & ovarian cancers. NECTIN2 might be related with human longevity. Two diseases which have been associated with NECTIN2 are Herpes Simplex and Ovarian Cystic Teratoma.

Proteasomal ubiquitin receptor ADRM1 (ADRM1) functions as a proteasomal ubiquitin receptor. ADRM1 is an integral plasma membrane protein which promotes cell adhesion. ADRM1 is assumed to undergo O-linked glycosylation. ADRM1 gene expression is induced by gamma interferon in some cancer cells. ADRM1 employs the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity.

E-selectin which is also called Endothelial leukocyte adhesion molecule 1, ELAM1, ELAM belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. Eselectin is expressed on the surface of endothelial cells and mediates the interaction of leukocytes and platelets with endothelial cells during an inflammatory response. E-selectin is present in single copy in the human genome and contains 14 exons spanning about 13 kb of DNA.

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. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.

Cadherin-5, also known as CDH5 is a classical cadherin which belongs to the cadherin superfamily. The CDH5is located in a six-cadherin cluster in a region on the long arm of chromosome 16 which is involved in loss ofheterozygosity events in breast as well as prostate cancer. CDH5 is a calcium-dependent cell-celladhesion glycoprotein composed of five extracellular cadherin repeats, a transmembrane region and a highlyconserved cytoplasmic tail. Furthermore, CDH5 functions as a classic cadherin by passing on to cells the ability to adhere in ahomophilic manner, CDH5 plays a significant role in endothelial cell biology through control of the cohesion as well as organization of the intercellular junctions.

Carcinoembryonic Antigen-Related Cell Adhesion Molecule 7 (CEACAM7) is a member of the immunoglobulin superfamily, CEA family. CEACAM7 contains 1 Ig-like C2-type (immunoglobulin-like) domain and 1 Ig-like V-type (immunoglobulin-like) domain. CEACAM7 is intensely down-regulated in colonic adenocarcinomas.

The CTX family of proteins (including ASAM) are type I transmembrane proteins within the Ig superfamily, which localize to junctional complexes between endothelial and epithelial cells and may play a role in cell-cell adhesion. CLMP has a role in adipocyte differentiation and development of obesity. CLMP is required for normal small intestine development.

Adhesion Molecule with Ig-Like Domain 2, also known as AMIGO2 is a member of the leucine-rich repeat family. AMIGO2 arbitrates homophilic in addition to heterophilic cell-cell interaction with AMIGO1 or AMIGO3. Furthermore, AMIGO2 contributes to signal transduction via its intracellular domain and is also essential for tumorigenesis of a subset of gastric adenocarcinomas.

CFLAR contains two death effector domains (DEDs) and a caspase-like domain. CFLAR may play a critical role between cell survival and cell death pathway in mammalian cells. CFLAR also interacts with adapter protein FADD and caspase-8 and -10, and potently inhibits apoptosis induced by all known death receptors DR3 (death receptor 3), TRAIL-R (TNF-related apoptosis-inducing ligand receptor) and TNFR1 (tumor necrosis factor receptor 1).

CD34 is a single chain transmembrane glycoprotein which is selectively expressed on human lymphoid and myeloid hemapoietic progenitor cells. CD34 has been used to measure angiogenesis, which reportedly predicts tumor recurrence.

E-cadherin (uvomorulin, cell-CAM120/80) is a calcium dependent cell adhesion molecule expressed predominately in epithelial tissues. It plays an important role in the growth and development of cells via the mechanisms of control of tissue architecture and the maintenance of tissue integrity. Numerous studies have demonstrated that reduction and/or loss of Ecadherin expression in carcinomas correlates positively with the potential of these tumors for invasion and metastasis.

Sialic acid-binding Ig-like lectin 7 isoform 1, also known as SIGLEC7, is a newly discovered family of sialic acid-binding lectins of the immunoglobulin (Ig) superfamily. The extracellular portion has two Ig-like domains, with the amino-terminal V-set Ig domain containing amino acid residues which known to be implicated in sialic acid recognition by other Siglecs. The combination of an extracellular sialic acid binding site and an intracellular ITIM motif proposes that SIGLEC7 is involved in trans-membrane regulatory signaling reactions. Furthermore, on the cell surface SIGLEC7 exists as a monomer and is expressed on natural killer cells.

Jumonji Domain Containing 6, also known as JMJD6 performs as a lysyl-hydroxylase which catalyzes 5-hydroxylation on specific lysine residues of target proteins for instance U2AF2/U2AF65 and LUC7L2, as a regulator of RNA splicing by mediating 5-hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. Additionally to peptidyl-lysine 5-dioxygenase activity, JMJD6 performs as an RNA hydroxylase, as proposed by its ability to bind single strand RNA. Furthermore, it acts as an arginine demethylase which demethylates histone H3 at 'Arg-2' (H3R2me) as well as histone H4 at 'Arg-3' (H4R3me), thus taking a part in histone code.

C-JUN is a gene which, in combination with c-Fos, forms the AP-1early response transcription factor. C-JUN is activated by the JNKpathway. C-JUN is the putative transforming gene of avian sarcoma virus 17. C-JUN is a protein which is highly similar to the viral protein, and which interacts directly with specific target DNA sequences to regulate gene expression. The C-JUN gene is intronless and is mapped to 1p32-p31, a chromosomal region involved in both translocations and deletions in human malignancies.

CD5 antigen-like (CD5L) participates in the regulation of the immune system. CD5L functions as an inhibitor of apoptosis. CD5L is expressed in the spleen, lymph node, thymus and bone marrow.

Lymphocyte Antigen 9, also known as LY9 is a member of the SLAM family of immunomodulatory receptors, LY9 interacts with the adaptor molecule SAP . LY9 plays a part in adhesion reactions between T lymphocytes and accessory cells via homophilic interaction. LY9 promotes T-cell differentiation into a helper T-cell Th17 phenotype which leads to increased IL-17 secretion; the costimulatory activity requires SH2D1A. Furthermore it also promotes recruitment of RORC to the IL-17 promoter. LY9 is implicated in the maintenance of peripheral cell tolerance through serving as a negative regulator of the immune response. LY9 disables autoantibody responses as well as inhibits IFN-gamma secretion by CD4(+) T-cells. Moreover, LY9 negatively regulate the size of thymic innate CD8(+) T-cells and the development of invariant natural killer T (iNKT) cells. Systemic Lupus Erythematosus is one of the diseases which are associated with LY9.

Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines. Vimentin is the main intermediate filament protein in mesenchymal cells and is therefore of value in the differential diagnosis of undifferentiated neoplasms.

Cluster of Differentiation 244 (CD244/Natural Killer Cell Receptor 2B4) contains 2 Ig-like (immunoglobulin-like) domains. CD244 is a cell surface receptor expressed on natural killer (NK) cells (and some T cells) which mediate non-major histocompatibility complex (MHC) restricted killing. NK-cell and target cells interaction via the CD244 receptor is believed to modulate NK-cell cytolytic activity. CD244 molecules function in eosinophil adhesion and chemotaxis, and have a role in the pathophysiology of allergic rhinitis (AR).

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.