Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01275 (glucagon)
 26,492 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In vitro glucagon (1-100 microgram/ml) has been shown to inhibit the degradation of bradykinin by kininases present in kidney microsomes and erythrocytes. Glucagon was less active on kininases present in plasma and was inactive on purified pancreatic carboxypeptidase B. In conscious dogs the intravenous infusion of glucagon (10 microgram/min) increased urine flow (160%) and urine kinin excretion (130%) and decreased urine kallikrein excretion (14%). It is suggested that in vivo inhibition of kininases might contribute to the biological effects of glucagon.
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PMID:Kininase inhibition by glucagon. 58 Jan 44

To evaluate the effects of protein loading on glomerular filtration rate (GFR), urinary excretion rate of albumin (AER), and plasma concentration of amino acids, 10 healthy volunteers and six diabetics were studied before and after eating tuna fish, egg white, cheese, or tofu. Furthermore, to study the possible role of glucagon, growth hormone (GH), atrial natriuretic peptide (ANP), or kallikrein in the responses of GFR, these substances were measured before and after protein loading. GFR increased significantly (p less than .001) after ingestion of tuna fish. No significant differences were seen between the GFR before and that after ingestion of the other foods. AER was unchanged following protein loading. Plasma concentrations of alanine, glycine, and arginine increased to a greater degree after ingestion of tuna fish than after digestion of the other foods. This result suggests that the response of GFR after protein loading may differ from one protein to another, and that these responses may not be directly mediated by glucagon, GH, ANP, or kallikrein.
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PMID:Acute loading with proteins from different sources in healthy volunteers and diabetic patients. 177 24

To evaluate the effects of acute protein loading on the glomerular filtration rate, albumin excretion rate and concentration of plasma amino acids, ten healthy volunteers and six type 2 diabetic patients with normoalbuminuria were studied before and after eating 0.7 g/kg body weight of tuna fish, boiled egg white, cheese or tofu (bean curd) on separate days. Furthermore, to study the possible role of glucagon, growth hormone, atrial natriuretic peptide and kallikrein in the responses of glomerular filtration rate to protein, these substances were measured before and after ingestion of tuna fish or egg white in six healthy volunteers. In healthy subjects, glomerular filtration rate increased significantly (p less than 0.01) from 98.1 +/- 4.2 ml/min during the baseline period to 129.9 +/- 6.6 ml/min after ingestion of tuna fish. No significant differences were seen between glomerular filtration rate before and after ingestion of egg white, cheese or bean curd. No significant differences were observed between the baseline albumin excretion rate and that after loading with any of the four kinds of protein. Plasma concentrations of alanine, glycine and arginine (amino acids known to induce glomerular hyperfiltration) increased to a greater degree after ingestion of tuna fish than after administration of the other meals. Diabetic subjects and healthy volunteers had similar responses. Plasma glucagon and growth hormone concentrations increased after ingestion of the tuna fish meal or egg white. Plasma atrial natriuretic peptide concentration and urinary kallikrein excretion were unaffected by ingestion of these two kinds of protein. These findings suggest that responses of glomerular filtration rate to acute protein loading may differ depending on the protein ingested, and that these responses may not be directly induced by glucagon, growth hormone, atrial natriuretic peptide or kallikrein.
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PMID:Glomerular filtration response to acute loading with protein from different sources in healthy volunteers and diabetic patients. 215 Oct 71

Regulation of endocrine pancreatic hormone gene expression by cholecystokinin (CCK) was examined in the rat using cloned cDNA probes to quantify changes in specific mRNAs (insulin, glucagon, pancreatic polypeptide and somatostatin). Plasma CCK levels were raised to concentrations comparable to physiologic postprandial values either by including soybean trypsin inhibitor (SBTI) in the intraduodenal perfusate of an elemental diet (6.9 +/- 1.0 pM, n = 6), or by intravenous infusion of CCK-8 (6.0 +/- 0.9 pM, n = 6). SBTI infusion for 48 h resulted in a three- to fourfold increase in procarboxypeptidase B and kallikrein mRNA levels. Similar increases were observed when CCK was infused intravenously for 24 h. In contrast, neither SBTI intraduodenally, nor intravenous CCK had any effects on mRNA levels of insulin, glucagon, PP or somatostatin. These data therefore indicate that CCK at physiologic postprandial plasma concentrations stimulates pancreatic protease gene expression but has no effects on gene expression of endocrine pancreatic hormones.
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PMID:Effects of CCK on gene expression of endocrine pancreatic hormones. 226 71

The serine proteinase glandular kallikrein has been demonstrated in the gastrointestinal tract, although there is some doubt as to whether it is synthesized there or derives from exocrine-gland secretions. Using a rat pancreatic kallikrein cRNA probe we have demonstrated kallikrein-like gene expression in the corpus, duodenum, jejunum, ileum, caecum and colon, and compared the pattern of expression with that of the gastrointestinal peptides somatostatin, gastrin and glucagon. In addition, using a panel of oligonucleotide probes specific for various members of the rat kallikrein-gene family, we have shown that the kallikrein-like gene expressed appears to be expressed as true kallikrein.
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PMID:Kallikrein-gene expression in the rat gastrointestinal tract. 260 9

We have investigated in stimulated human pancreatic juice the presence of the following peptides: insulin, glucagon, gastrin, somatostatin, VIP and secretin. Collection of pancreatic juice (3 periods: 20 min each) was completed by endoscopic cannulation of the pancreatic duct during the infusion of secretin (0.5 U/kg/h) and cerulein (75 ng/kg/h) in 6 healthy volunteers. Pure pancreatic juice was recovered in the presence of kallikrein inhibitor (iniprol 8,000 U/ml) in refrigerated collection tubes (4 degrees C). The material was acidified, boiled for 5 min and centrifuged. Radioimmunoassays were performed on the supernatant solutions. The elution profiles on Sephadex G 25 gel filtration of the immunoreactivities were compared with standard samples of hormones, immuno-reactive insulin, glucagon and somatostatin were found in every sample: insulin was present at a constant level (50 microU/ml) during the three periods of collection; glucagon was encountered in large amounts in the first sample and decreased significantly during the subsequent periods; somatostatin which occurred at a low level during the first period was significantly increased in the following periods. Gastrin, VIP and secretin were undetectable or only inconstantly found in very small amounts. These results are in agreement with a two-directional secretion of the human pancreatic endocrine cells. The cellular origin and function of these exocrine secreted peptides need further studies.
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PMID:[Presence of hormonal polypeptides in the pure pancreatic secretion in man under stimulation by cerulein and secretin]. 286 46

The submandibular glands of mice and rats are not fully developed at birth. In early postnatal life, differentiation of acini takes place before that of granular convoluted tubule (GCT) cells. The latter develop from striated duct cells, and first appear in both species around 15 days of age. In mice their full development gets under way by 20 days of age and is rapid in males and slow in females, resulting in a clear sexual dimorphism in adults. In rats, GCT development is more protracted, and accelerates around 40 days of age, with no sexual dimorphism seen at any time. The course of postnatal development of several GCT cell products is correlated with the cytodifferentiation of these cells. Reliable data are available for the development of amylase, proteases (including kallikrein), renin, epidermal growth factor, and nerve growth factor. Preliminary information exists for a glucagon-like substance. Cytodifferentiation of GCT cells is under hormonal control. Androgens alone can not precociously induce GCT cells, but thyroid hormones can do so, acting either alone or synergistically with androgens.
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PMID:Postnatal developmental changes in submandibular glands of rats and mice. 616 Jan 81

It is well known that there are functional and morphological similarities between the salivary glands and the pancreas. Amylase, kallikrein and glucagon are present in both tissues. Morphological similarities of the two tissues have been observed by using a light and electron microscope. In order to examine the pathophysiological relationship between the pancreas and the salivary glands, an immunohistochemical study using antisera against proline-rich peptide P-C, which was recently isolated from human whole saliva, was carried out on the human salivary glands and the pancreas. Peptide P-C like immunoreactivity was found not only in the salivary glands but also in the pancreatic islets. Furthermore, observation of serial thin sections immunostained with insulin, glucagon, somatostatin, PP antisera and antisera against peptide P-C revealed that peptide P-C like immunoreactivity-containing cells were identical to insulin containing B-cells. As the antisera against peptide P-C did not have any cross-reactivity to other kinds of peptide including insulin, glucagon, somatostatin, pp, VIP, human C-peptide and kallikrein, the present finding suggests that peptide P-C like immunoreactivity is present in the B-cells independently of insulin and proinsulin. The finding seems to be a new addition to the lists of proof which support the presence of a pathophysiological relation between the salivary glands and the pancreas. Although it seems likely that peptide P-C like immunoreactivity in the pancreatic B-cells may play some role in the function of the B-cells, since this material was present only in the B-cells among four kinds of cells in the pancreatic islets, its exact pathophysiological role remains to be elucidated.
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PMID:[The presence of proline-rich peptide P-C like immunoreactivity in the human pancreatic B-cells]. 634 34

Antisera against proline rich peptide P-C, recently isolated from human whole saliva were raised in rabbits by injections of peptide P-C-BSA conjugates. Immunohistochemical study using the antisera was carried out on human salivary glands, gut and pancreas. The results showed that peptide P-C like immunoreactivity was present not only in the salivary glands but also in the pancreatic islets, though not in the gut. Furthermore, immunostaining of adjacent thin sections revealed that cells reacting with antisera against peptide P-C were identical to those reacting with insulin antisera. As the antisera against peptide P-C did not have any cross-reactivities to insulin, glucagon, somatostatin, pancreatic polypeptide, VIP and human C-peptide, the antisera were considered to recognize specifically either peptide P-C related antigen or peptide P-C itself in human pancreatic B-cells. A novel substance, peptide P-C like immunoreactivity, may be present in pancreatic B-cells independent of pro-insulin and insulin. Morphological similarity between the salivary glands and the pancreas has been reported, and amylase, kallikrein and glucagon are present in both. These findings seem to suggest some functional relation between the pancreas and salivary glands. Detection of peptide P-C like immunoreactivity in the pancreas and salivary glands would be a additional support for this idea. Although it is suggested that peptide P-C like immunoreactivity in pancreatic B-cells may play some role in the function of B-cells, its exact pathophysiological role remains obscure.
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PMID:Immunohistochemical demonstration of salivary proline rich peptide P-C like immunoreactivity in human pancreatic B-cells. 635 25

The symptoms which immediately follow envenomation by many crotalid snakes include hypotension, hypovolemia, hemoconcentration, and shock. We have isolated and characterized two proteases (EI and EII) from the venom of Crotalus atrox which may be involved in the onset of these symptoms. EI and EII have molecular weights of 27,500 and 29,200 and isoelectric points of 4.7 and 4.3, respectively. Specific esterolytic activities of EI and EII on N alpha-p-tosyl-L-arginine methyl ester are 51.5 mumol min-1mg-1 and 48.1 mumol min-1 mg-1, respectively. Both enzymes are rather specific in their substrate requirements in that neither was demonstrated to have any proteolytic activity against either of the oxidized chains of insulin, or glucagon. Neither enzyme was shown to have plasmin or fibrinolytic activity. Both enzymes are able to cleave a kininogen analog to release bradykinin. This proteolytic activity is inhibited by aprotinin and phenylmethanesulfonyl fluoride but not by ethylenediaminetetraacetate. The enzymes are active upon the kallikrein substrates S2666 and S2302. The Km values of the enzymes with these substrates are similar to those reported for kallikrein. Structural similarity between the two enzymes was demonstrated by ultraviolet and circular dichroic spectroscopy, and amino acid analysis. Tryptic peptide mapping of the two native enzymes also suggested a large degree of structural similarity. Furthermore, sequence studies on the NH2-terminal regions of the enzymes indicate that they share a significant degree of sequence homology with porcine kallikrein and crotalase, a kallikrein-like enzyme from Crotalus adamanteus. The main physical difference between the two kallikreins reported here appears to be due to the carbohydrate moieties on the enzymes. At present the in vivo role of venom kallikreins in envenomation pathology is uncertain; however, it is possible that they play an important part in giving rise to the initial symptoms of hypotension and shock.
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PMID:Kallikrein-like enzymes from Crotalus atrox venom. 635 88


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