Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UMLS:C0011570 (
depression
)
172,036
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Ileal absorption of nitrogen was determined for feather meal (FM) samples, using magnesium ferrite as a marker. Diets containing 15% FM were balanced by linear programming, using two nitrogen absorption values for FM: 55%, as found, or 85%, an average value for standard feeds. When nitrogen absorption of FM was calculated as 55%, the growth of chicks from one to three weeks of age was similar to that of the control chicks.
Depression
of growth occurred when the diet composition was calculated using 85% nitrogen absorption for FM. The official method of
pepsin
digestibility in vitro, using 0.2%
pepsin
, did not reflect the nutritive value of FM protein. Results similar to those of nitrogen absorption in vivo were obtained with 0.002%
pepsin
. The total cystine content of FM and the rate of its liberation by pancreatin may also seve as an indication of the nutritive value of FM protein.
...
PMID:Nutritional value of feather-meal protein for chicks. 617 71
Rats with chronic gastric fistula were used to study gastric and duodenal/pancreatic secretory changes evoked by chemical duodenal ulcerogens. Although the data demonstrate stimulation of gastric output of acid and
pepsin
by certain doses of cysteamine or propionitrile, cysteamine produced dose-response increases in acid secretion only during the 1st hour following administration. The base output was also elevated at most of the time intervals after cysteamine. Decreased alkaline secretion was only seen following propionitrile injection. Although hyperacidity at the ulcer site may occur during duodenal ulcerogenesis, these results suggest that direct stimulation of acid-
pepsin
secretion or
depression
of pancreatic alkaline output are not the primary mechanisms explaining the ulcerogenic action of cysteamine and propionitrile.
...
PMID:Secretory changes associated with chemically-induced duodenal ulceration: simultaneous measurements of acid, pepsin, base and pancreatic enzymes in rats with chronic gastric fistula. 620 1
A rice bran protein concentrate (RBPC) was prepared from de-fatted rice bran by extraction with a 1% sodium chloride solution and by acetone-precipitation. This protein concentrate contained 45% protein, which was as good as casein in terms of protein quality being judged from the results of amino acid analysis. On the other hand, RBPC possessed the trypsin inhibitor activity corresponding to the complete inhibition of about 6 mg of bovine trypsin per 1 g of dry material. The activity was, however, completely destroyed by autoclaving RBPC for 30 min at 121 degrees C. In vitro digestion tests showed that RBPC was easily digested by
pepsin
but was resistant to the attack by trypsin, compared with autoclaved RBPC. Concerning in vivo digestion, however, there was no significant difference in apparent nitrogen digestibility between RBPC and the heated RBPC. In growth experiments with weanling rats fed a 10% level of protein diet, growth
depression
and the tendency of slight pancreatic hypertrophy were observed in rats receiving a RBPC diet. It is presumed that one of the reasons which explains these phenomena is the presence of trypsin inhibitor in RBPC.
...
PMID:Nutritional significance of a rice bran concentrate with trypsin inhibitor activity. 661 92
In eight volunteers the effect of pentagastrin (0.15, 1.0 and 6.0 microgram/kg body weight/h), secretin (0.5 and 1.0 clinical units/kg b.w./h), and cholecystokinin (CCK) (0.5 and 1.0 Ivy dog units/kg b.w./h) on the gastric secretion of
pepsin
was investigated to ascertain whether interaction occurred. A high intraindividual variation was found, and also a significant washout of
pepsin
in the initial period after stimulation. Pepsin secretion was stimulated after pentagastrin (50% above basal level) and even more after secretin (75%-200% above basal level), whereas no stimulation but a tendency for
depression
was seen after CCK. With the doses of gastrointestinal hormones used in this investigation, no interaction between secretin and CCK on gastric secretion of
pepsin
in man was demonstrated.
...
PMID:Effect of Pentagastrin, secretin, and cholecystokinin on gastric secretion of pepsin in man. 679 45
1 Pilocarpine (40 microgram/min i.v.) stimulated acid and
pepsin
secretion from Heidenhain pouches but did not stimulate secretion from the innervated stomach. 2 Pilocarpine significantly increased acid secretion from the innervated main stomach after the vagal nerves were bilaterally blocked with lidocaine. 3 The effect of pilocarpine on secretion from the Heidenhain puch was depressed by ganglionic blockade (hexamethonium), by dopamine and by isoprenaline. 4 The stimulatory action of histamine on gastric secretion from either pouch or gastric fistulae was uninfluenced by dopamine. 5 The action of pilocarpine was augmented by the muscarinic ganglionic stimulant AHR 602. Considering this effect, as well as the secretory
depression
of isoprenaline, pilocarpine resembles pentagastrin rather than methacholine in its action.
...
PMID:A study of gastric secretion in dogs using pilocarpine. 680 52
To investigate the mechanism of the anti-peptic action of ecabet sodium (TA-2711) observed in pylorous-ligated rats, effects of this drug on the peptic activity of rat gastric juice, purified hog
pepsin
and pepsinogen were studied in vitro. After incubation with or without ecabet at acidic pH, the reaction mixture was centrifuged, and the peptic activity of the supernatant was measured. Ecabet depressed the peptic activity of
pepsin
and pepsinogen in parallel with a decrease in the protein concentration of the respective supernatant.
Depression
was greatest with pepsinogen (97% at 2.5 mg/ml of the drug) followed by gastric juice (about 60% at 10 mg/ml), and inhibition of the peptic activity of
pepsin
was weakest (about 10% at 10 mg/ml). When a fraction of the rat gastric juice containing substances with molecular weights below 10,000 was added to the
pepsin
solution, the anti-peptic activity of ecabet was potentiated. These results suggest that oral dosing of ecabet reduces the peptic activity of gastric juice by precipitating
pepsin
, which is facilitated by an unknown component(s) of gastric juice, and that the inactivation of pepsinogen may also contribute to the anti-peptic activity of ecabet.
...
PMID:Effects of the new anti-ulcer drug ecabet sodium (TA-2711) on pepsin activity. I. Inactivation of enzyme protein. 837 15
The purpose of this study was to investigate the effects of gastric freezing on the chief and parietal cells of the stomach. To carry this out six Heidenhain pouch dogs were prepared. The secretions of these pouches were studied, both for HCl levels and
pepsin
activity, for 30 days before and 30 days after the freezing of the pouch. Freezing was carried out for one hour at -17 to -20 degrees C. The results show that no essential
depression
of either the HCl levels or the
pepsin
activity of the juice was effected by freezing. Therefore, it is deduced that freezing does not affect the functional activity of either the chief or the parietal cells. Complications such as ulceration and fistula formation into adjacent organs occurred as a result of freezing in certain pouch dogs.
...
PMID:EFFECTS OF GASTRIC FREEZING ON THE ISOLATED DENERVATED GASTRIC POUCH IN DOGS. 1415 26
107 patients with myocardial infarction and ulcer recurrence were examined. It was revealed that the ulcerous process proceeded with focal trombohemorragic disorders of local microcirculation in the gastroduodenal mucous coat in severe cases of myocardial infarction and with tromboischemic disorders of terminal blood flow in extremely severe cases. It was accompanied by the activation of acid and
pepsin
production,
depression
of mucopolysaccharides production and hypermotor gastric dyskinesis in patients with severe coronary pathology, in patients with the extremely severe pathology--by the
depression
of all functions of the stomach, except for normal acid production. The administration of an antiulcerous therapy helped to reduce the period of elimination of ulcer recurrence symptoms, liquidated microcirculatory and gastric functional disorders, and promoted the healing of ulcers. The therapy included omeprazole, sucralfate, long-term form of nifedipine for patients with severe myocardial infarction, and ranitidine, sucralfate and doxazosin in common doses for 20-25 days for patients with extremely severe cases.
...
PMID:[Particular features of the treatment of ulcer recurrence in patients with myocardial infarction]. 1625 36
Cbln1 (a.k.a. precerebellin) is secreted from cerebellar granule cells as homohexamer or in heteromeric complexes with Cbln3. Cbln1 plays crucial roles in regulating morphological integrity of parallel fiber (PF)-Purkinje cell (PC) synapses and synaptic plasticity. Cbln1-knockout mice display severe cerebellar phenotypes that are essentially indistinguishable from those in glutamate receptor GluRdelta2-null mice, and include severe reduction in the number of PF-PC synapses and loss of long-term
depression
of synaptic transmission. To understand better the relationship between Cbln1, Cbln3 and GluRdelta2, we performed light and electron microscopic immunohistochemical analyses using highly specific antibodies and antigen-exposing methods, i.e.
pepsin
pretreatment for light microscopy and postembedding immunogold for electron microscopy. In conventional immunohistochemistry, Cbln1 was preferentially associated with non-terminal portions of PF axons in the molecular layer but rarely overlapped with Cbln3. In contrast, antigen-exposing methods not only greatly intensified Cbln1 immunoreactivity in the molecular layer, but also revealed its high accumulation in the synaptic cleft of PF-PC synapses. No such synaptic accumulation was evident at other PC synapses. Furthermore, Cbln1 now came to overlap almost completely with Cbln3 and GluRdelta2 at PF-PC synapses. Therefore, the convergence of all three molecules provides the anatomical basis for a common signaling pathway regulating circuit development and synaptic plasticity in the cerebellum.
...
PMID:Cbln1 accumulates and colocalizes with Cbln3 and GluRdelta2 at parallel fiber-Purkinje cell synapses in the mouse cerebellum. 1925 Apr 38
In this study, the binding and enzyme activity inhibitory effect of nano-TiO(2) on
pepsin
was explored compared with micro-TiO(2). Nano-TiO(2) was about 60 nm and micro-TiO(2) was about 200 nm, both round in shape. The activity of
pepsin
was depressed significantly by nano-TiO(2) comparing to micro-ones. The results of UV spectrometry, HPLC, SDS-PAGE and CD assay proved that micro-TiO(2) has only physical absorption effect on
pepsin
, but no impairment on primary sequences or secondary structure. However, nano-TiO(2) had coordination interaction with
pepsin
besides physical binding effect. The secondary structure of
pepsin
was unfolded with the treatment of nano-TiO(2) at pH 6.5 and pH 3.53, which might consequently affect the beta-hairpin loop that protects the active center of
pepsin
, and then reduce the enzyme activity. Furthermore, the thermodynamic mechanisms of interaction between nano-TiO(2) and
pepsin
were explored by fluorescence spectrum and ITC analysis. According to the results of thermodynamic analysis, the K value was 3.64x10(6), stoichiometry (N(
pepsin
:nano-TiO2)) was 3.04x10(3), the total DeltaH was -2277 cal/mol, DeltaS was 22.7 cal/(K mol), therefore the nano-TiO(2)-
pepsin
interaction is spontaneous. The
depression
of activity and the unfolding of secondary structure of
pepsin
were resulted from non-covalent reactions, including electrostatic force and hydrophobic binding. This work studied the different inhibitory effects and revealed mechanisms of the interaction between micro/nano-TiO(2) and
pepsin
, and provided a useful approach for evaluating the health risk of nano-materials on level of proteins.
...
PMID:Enzyme activity inhibition and secondary structure disruption of nano-TiO2 on pepsin. 2054
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