| POLIP | polyneuropathy-ophthalmoplegia-leukoencephalopathy-intestinal pseudoobstruction [syndrome] |
|---|---|
| RBPI | intestinal retinol-binding protein |
| CGRP | Calcitonin Gene Related Peptide(Protein) |
| CLIP | Corticotropin-Like Intermediate Peptide |
| DSIP | Delta Sleep Inducing Peptide |
| receptors, adrenergic, alpha-2 | A subclass of alpha-adrenergic receptors (receptors, adrenergic, alpha). Alpha-2 adrenergic receptors can be pharmacologically discriminated, e.g., by their high affinity for the agonist clonidine and the antagonist yohimbine. They are found on pancreatic beta cells, platelets, and vascular smooth muscle, as well as both pre- and postsynaptically in the central and peripheral nervous systems. (12 Dec 1998) |
|---|---|
| receptors, adrenergic, beta | One of the two major pharmacologically defined classes of adrenergic receptors. The alpha-beta distinction was originally based on the cellular effects of receptor activation but now relies on the relative affinities for characteristic synthetic ligands. Beta adrenergic receptors are further subdivided based on information from endogenous and cloned receptors. (12 Dec 1998) |
| receptors, adrenergic, beta-1 | A subclass of beta-adrenergic receptors (receptors, adrenergic, beta). Beta-1 adrenergic receptors are equally sensitive to epinephrine and norepinephrine and bind the agonist dobutamine and the antagonist metoprolol with high affinity. They are found in the heart, juxtaglomerular cells, and in the central and peripheral nervous systems. (12 Dec 1998) |
| receptors, adrenergic, beta-2 | A subclass of beta-adrenergic receptors (receptors, adrenergic, beta). Beta-2 adrenergic receptors are more sensitive to epinephrine than to norepinephrine and have a high affinity for the agonist terbutaline. They are widespread, with clinically important roles in skeletal muscle, liver, and vascular, bronchial, gastrointestinal, and genitourinary smooth muscle. (12 Dec 1998) |
| receptors, albumin | Cell surface proteins that bind albumin with high affinity and trigger intracellular changes influencing the behaviour of cells. (12 Dec 1998) |
| receptors, aldosterone | Cytoplasmic proteins that specifically bind aldosterone and mediate its cellular effects. The aldosterone-bound receptor acts in the nucleus to regulate the transcription of specific segments of DNA. (12 Dec 1998) |
| receptors, amino acid | Cell surface proteins that bind amino acids and trigger changes which influence the behaviour of cells. Glutamate receptors are the most common receptors for fast excitatory synaptic transmission in the vertebrate central nervous system, and gaba and glycine receptors are the most common receptors for fast inhibition. (12 Dec 1998) |
| receptors, ampa | Cell surface proteins that bind glutamate and directly gate ion channels in cell membranes. Ampa receptors were originally discriminated from other glutamate receptors by their affinity for the agonist ampa (alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid). They are probably the most common mediators of fast excitatory synaptic transmission in the central nervous system. Several subtypes have been cloned, and for some types the traditional distinction from kainate receptors may not apply. (12 Dec 1998) |
| receptors, androgen | Proteins, generally found in the cytoplasm, that specifically bind androgens and mediate their cellular actions. The complex of the androgen and receptor migrates to the nucleus where it induces transcription of specific segments of DNA. (12 Dec 1998) |
| receptors, angiotensin | Cell surface proteins that bind angiotensins and trigger intracellular changes influencing the behaviour of cells. (12 Dec 1998) |
| receptors, antigen | Molecules on the surface of b- and T-lymphocytes that recognise and combine with specific antigens. (12 Dec 1998) |
| receptors, antigen, B-cell | Immunoglobulin molecules on the surface of B-lymphocytes that recognise and bind antigen. (12 Dec 1998) |
| receptors, antigen, T-cell | Molecules on the surface of T-lymphocytes that recognise and combine with antigens. The receptors are non-covalently associated with a complex of several polypeptides collectively called CD3 antigens (antigens, CD3). Recognition of foreign antigen and the major histocompatibility complex is accomplished by a single heterodimeric antigen-receptor structure, composed of either alpha-beta (receptors, antigen, T-cell, alpha-beta) or gamma-delta (receptors, antigen, T-cell, gamma-delta) chains. (12 Dec 1998) |
| receptors, antigen, T-cell, alpha-beta | T-cell receptors composed of CD3-associated alpha and beta polypeptide chains and expressed primarily in CD4+ or CD8+ T-cells. Unlike immunoglobulins, the alpha-beta T-cell receptors recognise antigens only when presented in association with major histocompatibility (MHC) molecules. (12 Dec 1998) |
| receptors, antigen, T-cell, gamma-delta | T-cell receptors composed of CD3-associated gamma and delta polypeptide chains and expressed primarily in CD4-/CD8- T-cells. The receptors appear to be preferentially located in epithelial sites and probably play a role in the recognition of bacterial antigens. The T-cell receptor gamma/delta chains are separate and not related to the gamma and delta chains which are subunits of CD3 (see antigens, CD3). (12 Dec 1998) |