Protein Gcg

Name Gcg
Description glucagon
Notes GLP-1 and GLP-2 exhibit a diverse array of metabolic, proliferative and cytoprotective actions with important clinical implications for the treatment of diabetes and gastrointestinal disease--REVIEW GLP-1 and GLP-2 exhibit a diverse array of metabolic, proliferative and cytoprotective actions with important clinical implications for the treatment of diabetes and gastrointestinal disease--REVIEW. GLP-1 has to be present in blood to stimulate insluin or suppress glucagon. Human pancreatic beta cells do not appear to possess memory for insulinotropic stimuli. GLP-1 improves function and inhibit apoptosis in freshly isolated human islets. GLP-1 is preserved in type 2 diabetic patients, this peptide was a candidate as a therapeutic agent for this disease. (review). GLP-1 may be another important determiner of pancreatic endocrine differentiation as is pdx-1. GLP-1 protects against myocardial infarction in the isolated and intact rat heart. GLP-1, like insulin, stimulates glucose uptake in myocytes, and this involves activation of PI3K/PKB, p44/42 MAPKs, partially p70s6k, and possibly PKC. GLP-2 may prove to be important in the attempt to optimize remnant intestinal function thereby eliminating the need for parenteral support in short bowel syndrome. Glucagon inhibits ghrelin secretion in humans. In morbid obesity, accelerated inactivation of circulating GLP-1 could at least partially account for plasma peptide levels lower than normal, defective availability of such a satiety factor possibly contributing to eating behaviour abnormalities. Increased GLP-1 levels, which lead to decreased food intake, may also contribute to the weight loss that is associated with the use of this drug in obese diabetics. Reduced secretion or action of GLP-1 or GIP does not explain a relative reduced beta-cell responsiveness to glucose or the slightly elevated plasma glucose concentrations observed in young low birth weight men. Results demonstrate that glucagon like peptide-1 is capable of preserving beta-cell function and protecting cells from apoptotic cell death. Review article focuses on the complex integrative mechanisms that regulate the secretion of GLP-1 and GLP-2 from intestinal L cells, including both direct and indirect regulation by ingested nutrients. The glucose-lowering effect of GLP-1 is markedly reduced when the deceleration of gastric emptying is antagonized, illustrating the importance of this facet of the multiple antidiabetic actions of GLP-1. The isolated N-terminal domain of the glucagon-like peptide-1 (GLP-1) receptor binds exendin peptides with much higher affinity than GLP-1. The protein encoded by this gene is actually a preproprotein that is cleaved into four distinct mature peptides. One of these, glucagon, is a pancreatic hormone that counteracts the glucose-lowering action of insulin by stimulating glycogenolysis and gluconeogenesis. Glucagon is a ligand for a specific G-protein linked receptor whose signalling pathway controls cell proliferation. Two of the other peptides are secreted from gut endocrine cells and promote nutrient absorption through distinct mechanisms. Finally, the fourth peptide is similar to glicentin, an active enteroglucagon. There are interactions between this protein, specific NEFA and insulin secretion. Conclude that the elimination of GLP-1 is the same in obese type 2 diabetic petients and matched healthy subjects. Delayed elimination in renal insufficiency. Glicentin plays an important role in the regulating inhibition of the contraction reaction in normal human jejunum via NANC nerves, and has a direct action on the jejunal muscle receptor. Important role for the irregularities in glucagon response in the postprandial glucose excursion in glucose intolerance and type 2 diabetes. In overweight/obese subjects, glucagon-like peptide 1 concentrations after weight loss were decreased compared with before weight loss, and nutrient-related stimulation was abolished. Leptin stimulates GLP-1 secretion from rodent and human intestinal L cells; leptin resistance may account for the decreased levels of GLP-1 found in obese humans. Low secretion of GLP-1 in girls with obesity may seriously and negatively influence the course of this disease while low levels in girls with anorexia nervosa are beneficial and promote appetite. Present in human colorectal adenocarcinomas and liver metastases. Role of M1 and M2 muscarinic receptors expressed by human L cells in the control of GLP-1 secretion. Role of polarity at Asp198 in determining binding site for glucagon-like peptide-1 receptor. Single treatment of sensitized mice with GLP diminishes both immediate and late-phase hypersensitivity reactions characteristic of food allergy by inhibiting transepithelial uptake of antigen. Some of the events that lead to the differentiation of pancreatic ductal cells in response to treatment with human GLP-1.
Owner Public
URN urn:agi-llid:2641
Connectivity 1711

KEGG pathway Neuroactive ligand-receptor interaction

LocusLink ID 2641
14526
24952

OMIM ID 138030

GO ID 0005179
0007186
0008283
0007631
0007165
0005576
0005625
0050796
0005615
0031769
0007188
0019538
0006109
0019216

Hugo ID 4191

Human chromosome position 2q36-q37

GenBank ID NC_000002
NM_002054
NP_002045
NT_005403
NW_001838860
NW_921585
AC_000134
AC_000045
AC007750
AAY24204
CH471058
EAX11356
EAX11357
EAX11358
V01515
CAA24759
X03991
CAA27627
X05387
AI818268
BC005278
AAH05278
BT006813
AAP35459
J04040
AAA52567
X05388
P01275
DQ892521
ABM83447
DQ895732
ABM86658
NC_000068
NM_008100
NP_032126
NT_039207
NW_001030694
AC_000024
AL928576
CAM21612
CH466519
EDL26988
EDL26989
AF276754
AAK96898
AK007911
BAB25344
AK148544
BAE28612
BC012975
AAH12975
Z46845
CAA86902
P55095
NC_005102
NM_012707
NP_036839
NW_001084813
NW_047655
AC_000071
CH473949
EDL79008
EDL79009
K02808
K02809
AAA41235
K02810
K02811
K02812
K02813
U81517
P06883
NT_162142
Q53TP6
NW_000176

Unigene ID Hs.516494
Mm.45494
Rn.54383

KEGG ID hsa:2641
mmu:14526
rno:24952

Alias GLP1
GLP2
GRPP
glucagon
glucagon-like peptide 1
glucagon-like peptide 2
glicentin-related polypeptide
GLP-1
RP23-343C17.3
glucagon-like peptide I
GLP I
Gcg

Organism Homo sapiens
Mus musculus
Rattus norvegicus

Mouse chromosome position 2 36.0 cM

Rat chromosome position 3q22-q24

Cell Localization Extracellular

Homologene ID 1553

Pathway GlucagonR -> CREB/ELK-SRF/SP1 signaling
glucagon signaling pathway
glucagon signaling pathway - Copy
glucagon signaling pathway

MGI ID 95674

Ariadne Ontology Neuromodulator

RGD ID 2668

GO Molecular Function hormone activity
glucagon receptor binding

GO Cellular Component extracellular region
soluble fraction
extracellular space

GO Biological Process regulation of insulin secretion
regulation of carbohydrate metabolic process
regulation of lipid metabolic process
cell proliferation
signal transduction
G-protein coupled receptor protein signaling pathway
G-protein signaling, coupled to cAMP nucleotide second messenger
protein metabolic process
feeding behavior

Group extracellular region
soluble fraction
extracellular space
hormone activity
glucagon receptor binding
regulation of insulin secretion
regulation of carbohydrate metabolic process
regulation of lipid metabolic process
cell proliferation
signal transduction
G-protein coupled receptor protein signaling pathway
G-protein signaling, coupled to cAMP nucleotide second messenger
protein metabolic process
feeding behavior
Neuromodulator

Swiss-Prot Accession P01275
P06883
P55095
Q53TP6