Protein interactions cell surface

Ericsson, 1990), the synthesis of fluorescently labeled DNA probes (L. M. Smith et al., 19 8 5), as a label in homogeneous immunoassay systems (Nithipatikom and McGown, 1987), to investigate specific interactions of proteins with cells surfaces (Hochman et al., 1988), and as an important fluorescent tag of antibodies in immunohistochemical staining techniques (Davidson and Hilchenbach, 1990). 

Most physiological processes are the consequences of an effector interaction with biomacromolecules (Harding and Chowdhry, 2001 Weber, 1992), such as interactions between enzymes and their substrates, between hormones and hormone receptors, between antigens and antibodies, between inducer and DNA, and so on. In addition, there are macromolecule-macromolecule interactions such as between proteins (Kleanthous, 2000), between protein and nucleic acid (Saenger and Heinemann, 1989), and between protein and cell-surface saccharide. The effector of small molecular weight is normally referred to as the ligand, and the macromolecular combinant is known as the receptor. 

INTERACTION OF PRION PROTEINS WITH CELL SURFACE RECEPTORS, MOLECULAR CHAPERONES, AND OTHER MOLECULES... 

HMW heparin will bind to plasma proteins and cell surfaces in addition to its prime target, ATIII. Becanse different individnals synthesize different levels of plasma proteins, the nse of this form of heparin as an anticoagulant requires constant monitoring of the patient to ensnre that the correct dosage has been given such that spontaneous thrombi do not develop, bnt not so mnch that spontaneous bleeding occnrs. FMW heparin has fewer nonspecific interactions than HMW heparin, and its effects are easier to predict on patients, so that constant monitoring is not reqnired. 

Barinaga, M. Forging a Path to Cell Death. Scimce 273, 735-737 (1996). [A Research News article describing a process apparently missing in cancer cells, and that depends on interactions among receptor proteins on cell surfaces.]... 

Study of glycomes. Because of the fact that carbohydrates bind to many disease markers in human blood, their characterization is a highly significant field of study. The type of carbohydrate on the surface of a cell can be related to disease. Carbohydrates exert their influence in the body via a selective interaction with proteins on cell surfaces. 

FRAP was used initially to smdy the dynamics of lateral diffusion of lipids and proteins on cell surfaces [159-163]. It was combined with total internal reflection (Box 3.2 and Sect. 5.10) to study interactions of immunoglobulin fragments with planar bUayer membranes supported on glass surfaces [164] and binding of ligands to immobilized receptors [165]. Its applications expanded rapidly with the development of confocal microscopy (Sect. 5.10) and GFP tags [147,166-168], and now include components of the nucleus [169, 170], mitochonrial matrix [171], endoplasmic reticulum [172], and Golgi apparatus [173]. 

Class 1 and class II MHC molecules bind peptide antigens and present them at the cell surface for interaction with receptors on T cells. The extracellular portion of these molecules consists of a peptide-binding domain formed by two helical regions on top of an eight-stranded antiparallel p sheet, separated from the membrane by two lower domains with immunoglobulin folds. These domains are differently disposed between the two protein subunits in class I and class II molecules. 

VEGF-Trap is a protein-based product candidate designed to bind all forms of VEGF and the related P1GF, and prevents their interaction with cell surface receptors. VEGF Trap is being pursued in phase II... 

Integrins constitute a large family of a (3 heterodimeric cell surface, transmembrane proteins that interact with a large number of extracellular matrix components through a metal ion-dependent interaction. The term integrin reflects their function in integrating cell adhesion and migration with the cystoskeleton. 

Muscarinic acetylcholine receptors (mAChRs) form a class of cell surface receptors that are activated upon binding of the neurotransmitter, acetylcholine. Structurally and functionally, mAChRs are prototypical members of the superfamily of G protein-coupled receptors. Following acetylcholine binding, the activated mAChRs interact with distinct classes of heterotrimeric G proteins resulting in the activation or inhibition of distinct downstream signaling cascades. 

---