Secretin is a gastrointestinal hormone responsible for the regulation of bicarbonate, potassium ion and enzyme secretion from the pancreas. A cDNA encoding the human secretin receptor was isolated from a human pancreatic adenocarcinoma cell-line cDNA library using polymerase chain reaction and library screening techniques. The cDNA isolated is 1717 bp in length encoding a 440 amino acid long polypeptide. Computer analysis of the receptor indicated that it is a member of the glucagon-VIP-secretin receptor family and is a G-protein coupled receptor containing seven hydrophobic transmembrane domains. The receptor was subsequently expressed in COS-7 cells and was able to bind specifically to human secretin with high affinity as indicated by the competitive displacement assay. The human secretin receptor was found to be functionally coupled to the stimulation of adenylyl cyclase resulting in the accumulation of intracellular cAMP in a dose-dependent manner. By Northern blot analysis, a 1.8 Kb mRNA was detected in human pancreas and intestine, while weak hybridization signals were detected in human colon, kidney and lung. Functional characterization of this receptor should enhance our understanding of the physiology and pathophysiology of human secretin, its structure-function, receptor interaction and receptor tissue distribution.
The whole of the physical, chemical, and biochemical processes carried out by multicellular organisms to break down ingested nutrients into components that may be easily absorbed and directed into metabolism.
Secretin is a gastrointestinal hormone responsible for the regulation of bicarbonate, potassium ion and enzyme secretion from the pancreas. A cDNA encoding the human secretin receptor was isolated from a human pancreatic adenocarcinoma cell-line cDNA library using polymerase chain reaction and library screening techniques. The cDNA isolated is 1717 bp in length encoding a 440 amino acid long polypeptide. Computer analysis of the receptor indicated that it is a member of the glucagon-VIP-secretin receptor family and is a G-protein coupled receptor containing seven hydrophobic transmembrane domains. The receptor was subsequently expressed in COS-7 cells and was able to bind specifically to human secretin with high affinity as indicated by the competitive displacement assay. The human secretin receptor was found to be functionally coupled to the stimulation of adenylyl cyclase resulting in the accumulation of intracellular cAMP in a dose-dependent manner. By Northern blot analysis, a 1.8 Kb mRNA was detected in human pancreas and intestine, while weak hybridization signals were detected in human colon, kidney and lung. Functional characterization of this receptor should enhance our understanding of the physiology and pathophysiology of human secretin, its structure-function, receptor interaction and receptor tissue distribution.
The elimination by an organism of the waste products that arise as a result of metabolic activity. These products include water, carbon dioxide (CO2), and nitrogenous compounds.
Secretin is a gastrointestinal hormone responsible for the regulation of bicarbonate, potassium ion and enzyme secretion from the pancreas. A cDNA encoding the human secretin receptor was isolated from a human pancreatic adenocarcinoma cell-line cDNA library using polymerase chain reaction and library screening techniques. The cDNA isolated is 1717 bp in length encoding a 440 amino acid long polypeptide. Computer analysis of the receptor indicated that it is a member of the glucagon-VIP-secretin receptor family and is a G-protein coupled receptor containing seven hydrophobic transmembrane domains. The receptor was subsequently expressed in COS-7 cells and was able to bind specifically to human secretin with high affinity as indicated by the competitive displacement assay. The human secretin receptor was found to be functionally coupled to the stimulation of adenylyl cyclase resulting in the accumulation of intracellular cAMP in a dose-dependent manner. By Northern blot analysis, a 1.8 Kb mRNA was detected in human pancreas and intestine, while weak hybridization signals were detected in human colon, kidney and lung. Functional characterization of this receptor should enhance our understanding of the physiology and pathophysiology of human secretin, its structure-function, receptor interaction and receptor tissue distribution.
A series of molecular signals that proceeds with an activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, or for basal GPCR signaling the pathway begins with the receptor activating its G protein in the absence of an agonist, and ends with regulation of a downstream cellular process, e.g. transcription.
Secretin is a gastrointestinal hormone responsible for the regulation of bicarbonate, potassium ion and enzyme secretion from the pancreas. A cDNA encoding the human secretin receptor was isolated from a human pancreatic adenocarcinoma cell-line cDNA library using polymerase chain reaction and library screening techniques. The cDNA isolated is 1717 bp in length encoding a 440 amino acid long polypeptide. Computer analysis of the receptor indicated that it is a member of the glucagon-VIP-secretin receptor family and is a G-protein coupled receptor containing seven hydrophobic transmembrane domains. The receptor was subsequently expressed in COS-7 cells and was able to bind specifically to human secretin with high affinity as indicated by the competitive displacement assay. The human secretin receptor was found to be functionally coupled to the stimulation of adenylyl cyclase resulting in the accumulation of intracellular cAMP in a dose-dependent manner. By Northern blot analysis, a 1.8 Kb mRNA was detected in human pancreas and intestine, while weak hybridization signals were detected in human colon, kidney and lung. Functional characterization of this receptor should enhance our understanding of the physiology and pathophysiology of human secretin, its structure-function, receptor interaction and receptor tissue distribution.
Receptors which transduce extracellular signals across the cell membrane. At the external side they receive a ligand (a photon in case of opsins), and at the cytosolic side they activate a guanine nucleotide-binding (G) protein. These receptors are hydrophobic proteins that cross the membrane seven times.
A reference proteome is a set of protein sequences derived from a complete proteome which constitutes a defined standard for a particular user community. Reference proteomes are manually defined according to a number of criteria. They cover the proteomes of well- studied model organisms and other proteomes of interest for biomedical and biotechnological research. Reference proteomes have been selected to provide broad coverage of the tree of life, and constitute a representative cross-section of the taxonomic diversity to be found within UniProtKB.
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