What is Function
TRPM8 is an ion channel, upon activation it allows the entry of Na+ (sodium) and Ca2+ (calcium) ions to the cell that leads to depolarization and the generation of action potential. This eventually leads to the feeling of cold.
The TRPM8 protein is expresed in sensory neurons, and it is activated by cold temperatures and cooling agents, such as menthol and icilin where as WS-12 and CPS-369 are the most selective agonist of TRPM8.
Tags: Integral membrane proteins, Ion channels, Membrane proteins, Proteins, Transmembrane proteins
This entry was posted
on Thursday, December 25th, 2008 at 12:39 am and is filed under Nutrients.
You can follow any responses to this entry through the RSS 2.0 feed.
You can leave a response, or trackback from your own site.
The main function of crystallins at least in the lens of the eye is probably to increase the refractive index while not obstructing light. However, this is not their only function. It is becoming increasingly clear that crystallins may have a several metabolic and regulatory functions, both within the lens and in other parts of the body [5].
The protein has no known natural ligand[2] and its function is unclear. It is suspected that it acts as a calcium channel in the cell membran
SAP97 is expressed throughout the body in epithelial cells, including the kidney and brain[1]. There is some evidence that SAP97 regulates cell-to-cell adhesion during cell death, and may interact with HPV. In the brain, SAP97's function is involved in the trafficking of transmembrane receptors from the ER to the plasma membrane[2].
SAP97's function has been investigated by reducing its expression by knockout or increasing its expression heterologously. Mice in which the SAP97 gene has been knocked out die perinatally, have a cleft palate, and deficiencies in renal function.[3][4] Overexpression of SAP97 in mammalian neurons leads to increased synaptic strength. [5]
ER-? may have anti-proliferative effects and therefore oppose the actions of ER-? in reproductive tissue.[4] ER-? may also have an important role in adpative function of the lung during pregnancy.[5]
There is a vast array of studies investingating the function of "membrane channels", these frequently combine the patch clamp technique with pharmacology. The process by which membrane channel function is altered by drugs and biochemicals is termed "channel modulation". Functional channelomic studies also includes study of diseases resulting from their mis-function. Such a disease is termed a channelopathy.
The precise function of the prion protein is not known, but there is substantial evidence that it serves as a copper-dependent antioxidant.[
Functional gum is the name given to types of chewing gum which impart some practical function instead of, or in addition to, the usual enjoyment provided by a traditional chewing gum as a confectionery product. Examples of this include Nicotine gum which is used to aid smoking cessation, so-called "dental gum" made by toothpaste manufacturers that provide some of the benefits of tooth brushing, caffeinated gum to help alertness and even Think Gum which designers say they believe may enhance mental functioning. It could be argued that most gum (at least the mint varieties) provides some function in that they
SNARE proteins are the key components of the molecular machinery that drives fusion of membranes in exocytosis. Their function however is subject to fine tuning by various regulatory protein collectively referred to as SNARE masters.
The function of sphingomyelin remained unclear until recently when it was found to have a function in signal transduction.
The plasma membrane of cells is highly enriched in sphingomyelin and is considered largely to be found in the exoplasmic leaflet of the cell membrane. However, there is some evidence that there may also be a sphingomyelin pool in the inner leaflet of the membrane [1] [2]. Moreover, neutral sphingomyelinase-2 - an enzyme that breaks down sphingomyelin into ceramide has been found to localise exclusively to the inner leaflet further suggesting that there may be sphingomyelin present there.
The key requirement in understanding protein function is to learn to correlate the vast array of potential protein modifications to particular phenotypic settings, and then determine if a particular post-translational modification is required for a function to occur
Recent evidence suggests RRF may accomplish the recycling of ribosomes by splitting ribosomes into subunits, thereby releasing the bound mRNA[5].
Loss of RRF Function:
In Bacteria (specifically Escherichia coli), loss of the gene encoding RRF is deleterious [6]. This makes RRF a possible target for new antibacterial drugs.
Yeast mitochondrial RRF (mtRRF) is encoded by a gene in the cell nucleus. Loss of function of this gene leads to mitochondrial genome instability and respiratory incompetence [7].
Centrin is required for duplication of centrioles.[2] It may also play a role in severing of microtubules by causing calcium-mediated contraction.[3] The majority of centrin in the cell is non-centrosomal whose function is not yet clear.[4]
The function of Thy-1 has not yet been fully elucidated. It has speculated roles in cell-cell and cell-matrix interactions, with implication in neurite outgrowth, nerve regeneration, apoptosis, metastasis, inflammation, and fibrosis.
Scientist believe that calcineurin might prove to be one of the two keys, along with NFAT, in improving the function of diabetics' pancreatic beta cells.[4][5]
Calcineurin/Nfat signaling is required for perinatal lung maturation and function:[6]
The amount of BSP in bone and dentin is roughly equal,[16] however the function of BSP in these mineralized tissues is not known. One possibility is that BSP acts as a nucleus for the formation of the first apatite crystals.[17].As the apatite forms along the collagen fibres with in the extracellular matrix, BSP could then help direct, redirect or inhibit the crystal growth.
Leave a Reply