Cancer

Phosphoserine, the phosphorylated modification of the amino acid serine, is a central post-translational modification within a cell for many biological and biomedical processes. The phosphorylation of specifically four residue types - histidine, serine, threonine, and tyrosine occurs both within the cell as well as at the cell surface. This exquisitely controlled regulatory system controls a vast number of intertwined and interconnected downstream signaling pathways and cascades.

The thymidine analogue bromodeoxyuridine (BrdU) has a long, colorful history of heavy use in molecular and cytokinetic studies (1, 2). BrDU is incorporated into newly synthesized DNA only in S-phase cells, and then immunocytochemically detected with BrDU antibodies. This method allows for extremely accurate and comprehensive comparative studies of a variety of cells ranging from normal to neoplastic.

Toll-like receptors (TLRs) play an essential role in the activation of innate immunity, and TLRs are expressed in a large number of immune cells like B-lymphocytes, monocytes, plasmacytoid dendritic cells and at low levels in human respiratory cells as well as in epithelial cells.

 Perforin is a calcium-dependent pore forming cytolytic protein. Perforin is partially homologous to the terminal components of the membrane attack complex of complement and produces pores of up to 20nm in diameter on target membranes.

Over the past two decades, it has become clear that tyrosine phosphorylation plays a pivotal role in a variety of important signaling pathways in multicellular organisms. In the typical vertebrate cell, phosphotyrosine represents only a tiny fraction of total protein phosphorylation. Yet it is sufficient enough to induce malignant transformation (1), as unregulated phosphotyrosine signaling causes a breakdown in the normal regulation of cellular processes leading to several human diseases (2).

Phosphoserine is an ester of serine and phosphoric acid which results from posttranslational modifications. Phosphorylation is a key post-translational modification necessary for normal cellular signaling.

Myosin is a super family of actin based molecular motors that hydrolyze ATP and generate physical force to move specific molecules inside the cell. This super family, divided into at least twenty four classes based on head domain sequence similarity and domain organization^. The processivity of myosins along an actin filament and transport of intracellular ‘cargo’ are achieved by generating physical force from chemical energy of ATP followed by appropriate conformational changes (1).

Myeloid differentiation primary response gene 88 (MYD88) encodes a cytosolic adapter protein that plays an essential role in innate and adaptive immune responses.

Monocyte Chemoattractant Protein (MCP1) is a potent monocyte attractant, is a member of the CC chemokine subfamily. MCP1 exerts its effects through binding to G-protein-coupled receptors on the surface of leukocytes targeted for activation and migration. The role of MCP1 and its receptor, chemokine receptor-2 (CCR2), in monocyte recruitment during infection or under other inflammatory conditions is well known. Recent studies indicate that MCP-1 may play an important role in pulmonary inflammation.

The polycomb group (PcG) protein, enhancer of zeste homolog 2 (EZH2) is a methyl-transferase that plays a key role in transcriptional gene repression. EZH2 is frequently overexpressed in several malignant tumors, and is often associated with advanced disease stage in many solid tumors.