Physiology of SK3
KCa2.3 channels play a major role in human physiology, particularly in smooth muscle relaxation. The expression level of KCa2.3 channels in the endothelium influences arterial tone by setting arterial smooth muscle membrane potential. The sustained activity of KCa2.3 channels induces a sustained hyperpolarisation of the endothelial cell membrane potential, which is then carried to nearby smooth muscle through gap junctions.[5] Blocking the KCa2.3 channel or suppressing KCa2.3 expression causes a greatly increased tone in resistance arteries, producing an increase in peripheral resistance and blood pressure.
Tags: Integral membrane proteins, Ion channels, Membrane proteins, Proteins, Transmembrane proteins
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SK3 is a small-conductance calcium-activated potassium channel partly responsible for the calcium-dependent after hyperpolarisation current (IAHP). It belongs to a family of channels known as small-conductance potassium channels, which consists of three members – SK1, SK2 and SK3 (KCNN1, 2 and 3 respectively), which share a 60-70% sequence identity.[1] These channels have acquired a number of alternative names, however a NC-IUPHAR has recently achieved consensus on the best names, KCa2.1 (SK1), KCa2.2 (SK2) and KCa2.3 (SK3).[2] Small conductance channels are responsible for the medium and possibly the slow components of the IAHP.
The SK channel family contains 4 members - SK1, SK2, SK3, and SK4.
Mutations in KCa2.3 are suspected to be a possible underlying cause for several neurological disorders, including schizophrenia, bipolar disorder, Alzheimer’s disease, anorexia nervosa and ataxia[6][7][8] as well as myotonic muscular dystrophy.
KCa2.3 contains 6 transmembrane domains, a pore-forming region, and intracellular N- and C- termini[3][1] and is readily blocked by apamin. The gene for KCa2.3, KCNN3, is located on chromosome 1q21.
All SK channels can be pharmacologically blocked by quaternary ammonium salts of a plant-derived neurotoxin bicuculline.[6] In addition, SK channels(SK1-SK3) are sensitive to blockade by the bee venom apamin, [7] but SK4 (IK) is not. and the scorpion venom tamapin.[8]
In plant physiology lovastatin has occasionally been used as inhibitor of cytokinin biosynthesis.[10]
The discovery of EGF won Dr. Stanley Cohen a Nobel Prize in Physiology and Medicine in 1986[2] and was patented for cosmetic use by Dr. Greg Brown in 1989[3].
Stanley Cohen and Rita Levi-Montalcini won the 1986 Nobel Prize in Physiology or Medicine for their discovery of NGF and other growth factors.[3][4][5]
Leland H. Hartwell, R. Timothy Hunt, and Paul M. Nurse won the 2001 Nobel Prize in Physiology or Medicine for their discovery of cyclin and cyclin-dependent kinase, central molecules in the regulation of the cell cycle.
C9ORF3 Messenger RNA has been detected in human pancreas, placenta, liver, testis, and heart. The expression in the heart suggests this enzyme may play a role in the regulating the physiology of cardiac muscle.[2]
Structure and functional studies of membrane channels are closely linked, but perhaps the most famous recent work studying the structure of ion channels is the paper by Doyle et al. 1998, which led to the Nobel Prize for physiology for Prof Roderick MacKinnon. A
Cortisone was first discovered by the American chemist Edward Calvin Kendall while a researcher at the Mayo Clinic. He was awarded the 1950 Nobel Prize for Physiology or Medicine along with Philip S. Hench and Tadeus Reichstein for the discovery of adrenal cortex hormones, their structures, and functions. Cortisone was first produced commercially by Merck & Co.
Although found in many tissues,amylase is most prominent in pancreatic juice and saliva which each have their own isoform of human ?-amylase. They behave differently on isoelectric focusing, and can also be separated in testing by using specific monoclonal antibodies. In humans, all amylase isoforms link to chromosome 1p21 (see AMY1A).
Leland H. Hartwell, R. Timothy Hunt, and Paul M. Nurse won the 2001 Nobel Prize in Physiology or Medicine for their complete description of cyclin and cyclin-dependent kinase mechanisms, central molecules in the regulation of the cell cycle.
Although found in many tissues,amylase is most prominent in pancreatic juice and saliva which each have their own isoform of human ?-amylase. They behave differently on isoelectric focusing, and can also be separated in testing by using specific monoclonal antibodies. In humans, all amylase isoforms link to chromosome 1p21 (see AMY1A).
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