| BML | bone marrow lymphocytosis |
|---|---|
| BMN | bone marrow necrosis |
| BMT | Bachelor of Medical Technology; basement membrane thickening; benign mesenchymal tumor; bone marrow ... |
| BRA | bilateral renal agenesis; bone-resorbing activity; brain-reactive antibody |
| BRF | bone-resorbing factor |
| receptors, peptide | Cell surface receptors that bind peptide messengers with high affinity and regulate intracellular signals which influence the behaviour of cells. (12 Dec 1998) |
|---|---|
| receptors, phencyclidine | Specific sites or molecular structures on cell membranes or in cells with which phencyclidine reacts or to which it binds to elicit the specific response of the cell to phencyclidine. Studies have demonstrated the presence of multiple receptor sites for pcp. These are the pcp/sigma site, which binds both pcp and psychotomimetic opiates but not certain antipsychotics, and the pcp site, which selectively binds pcp analogs. (12 Dec 1998) |
| receptors, pituitary hormone | Cell surface proteins that bind pituitary hormones with high affinity and trigger intracellular changes influencing the behaviour of cells. Since many pituitary hormones are also released by neurons as neurotransmitters, these receptors are also found in the nervous system. (12 Dec 1998) |
| receptors, pituitary hormone-regulating hormone | Cell surface receptors that bind the hypothalamic hormones regulating pituitary cell differentiation, proliferation, and hormone synthesis and release, including the pituitary-releasing and release-inhibiting hormones. The pituitary hormone-regulating hormones are also released by cells other than hypothalamic neurons, and their receptors also occur on non-pituitary cells, especially brain neurons, where their role is less well understood. Receptors for dopamine, which is a prolactin release-inhibiting hormone as well as a common neurotransmitter, are not included here. (12 Dec 1998) |
| receptors, platelet-derived growth factor | Specific molecular sites or structures on cell membranes that react with platelet-derived growth factor, its analogs, or antagonists, to elicit or to inhibit the specific response of the cell to this factor. Pdgf binds with different affinities and specificities to two structurally related receptors, the alpha-receptor and the beta-receptor. Both of these receptors are transmembrane proteins with an intracellular, ligand-stimulatable protein kinase domain. (12 Dec 1998) |
| receptors, polymeric immunoglobulin | Specialised fc receptors (receptors, fc) for polymeric immunoglobulins, which mediate transcytosis of polymeric IgA and IgM into external secretions. They are found on the surfaces of epithelial cells and hepatocytes. After binding to IgA, the receptor-ligand complex undergoes endocytosis, transport by vesicle, and secretion into the lumen by exocytosis. Before release, the part of the receptor (secretory component) that is bound to IgA is proteolytically cleaved from its transmembrane tail. (12 Dec 1998) |
| receptors, presynaptic | Neurotransmitter receptors located on or near presynaptic terminals or varicosities. Presynaptic receptors which bind transmitter molecules released by the terminal itself are termed autoreceptors. (12 Dec 1998) |
| receptors, progesterone | Specific proteins found in or on cells of progesterone target tissues that specifically combine with progesterone. The cytosol progesterone-receptor complex then associates with the nucleic acids to initiate protein synthesis. There are two kinds of progesterone receptors, a and b. Both are induced by oestrogen and have short half-lives. (12 Dec 1998) |
| receptors, prolactin | Labile proteins on or in prolactin-sensitive cells that bind prolactin initiating the cells' physiological response to that hormone. Mammary casein synthesis is one of the responses. The receptors are also found in placenta, liver, testes, kidneys, ovaries, and other organs and bind and respond to certain other hormones and their analogs and antagonists. This receptor is related to the growth hormone receptor. (12 Dec 1998) |
| receptors, prostaglandin | Cell surface receptors that bind prostaglandins with high affinity and trigger intracellular changes which influence the behaviour of cells. Prostaglandin receptor subtypes have been tentatively named according to their relative affinities for the endogenous prostaglandins. They include those which prefer prostaglandin d2 (dp receptors), prostaglandin e2 (ep1, ep2, and ep3 receptors), prostaglandin f2-alpha (fp receptors), and prostacyclin (ip receptors). (12 Dec 1998) |
| receptors, prostaglandin e | Cell surface receptors which bind prostaglandins with a high affinity and trigger intracellular changes which influence the behaviour of cells. Prostaglandin e receptors prefer prostaglandin e2 to other endogenous prostaglandins. They are subdivided into ep1, ep2, and ep3 types based on their effects and their pharmacology. (12 Dec 1998) |
| receptors, purinergic | Cell surface proteins that bind purines with high affinity and trigger intracellular changes which influence the behaviour of cells. The best characterised classes of purinergic receptors in mammals are the p1 receptors, which prefer adenosine, and the p2 receptors, which prefer ATP or ADP. (12 Dec 1998) |
| receptors, purinergic p1 | A class of cell surface receptors that prefers adenosine to other endogenous purines. Purinergic p1 receptors are widespread in the body including the cardiovascular, respiratory, immune, and nervous systems. There are at least two pharmacologically distinguishable types (a1 and a2, or ri and ra). The methylxanthines, e.g., caffeine, bind to these receptors, but also have other unrelated effects. (12 Dec 1998) |
| receptors, purinergic p2 | A class of cell surface receptors for purines that prefer ATP or ADP over adenosine. P2 purinergic receptors are widespread in the periphery and in the central and peripheral nervous system. Subtypes have been proposed, usually designated p2 x, y, z, and t. P2x receptors may mediate fast synaptic transmission by ATP. The ADP-preferring p2t receptors in platelets stimulate aggregation. (12 Dec 1998) |
| receptors, retinoic acid | Proteins in the nucleus or cytoplasm that specifically bind retinoic acid or retinol and trigger changes in the behaviour of cells. Retinoic acid receptors, like steroid receptors, are ligand-activated transcription regulators. Several types have been recognised. (12 Dec 1998) |