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At least 325 records · Page 18Linked to original sources

PubMed1995

Chemical synthesis of phosphopeptides using the arylthio group for protection of phosphate: application to identification of cdc2 kinase phosphorylation sites.

Synthesis of two O-phosphorylated dipeptides, N-Boc-O[S,S-bis(p-methoxyphenyl)phosphorodithioyl] -serylproline and N-Boc-O-[S,S-bis(p-methoxyphenyl) phosphorodithioyl]threonylproline, as new O-phosphorylated dipeptide building blocks for the synthesis of O-phosphorylated peptides, is described. Peptides containing phosphoserine or phosphothreonine were prepared by use of these building blocks in the Boc mode of liquid-phase peptide synthesis. Sites phosphorylated by cdc2 kinase were easily identified using these chemically synthesized phosphopeptides.

Amino Acid Sequence↗

PubMed1990

Phosphate-dependent monoclonal antibodies to neurofilaments and Alzheimer neurofibrillary tangles recognize a synthetic phosphopeptide.

Five phosphate-dependent monoclonal antibodies to the neurofilament heavy polypeptide bound strongly to a phosphorylated synthetic peptide, which contains a single Lys-Ser-Pro sequence that occurs in human neurofilaments. Three of the antibodies label Alzheimer's disease neurofibrillary tangles and two do not, suggesting that in tangles an epitope similar to the peptide is available to some but not all of the antibodies. In addition, some antibodies were found to be more affected than others by enzymatic dephosphorylation of the antigen, but because all the antibodies bound the same synthetic phosphopeptide they do not bind to mutually exclusive phosphorylation sites. Instead the more phosphate-dependent antibodies might bind the phosphate group more directly, as suggested by their inhibition by inorganic phosphate and free phosphoserine.

Alzheimer Disease↗

PubMed1967

The regional distribution of the nerve-stimulating phosphopeptide (nerveside, substance B) in the central nervous system.

1. The nerve-stimulating phosphopeptide, nerveside, is present mainly in the cerebrum and brain stem, while the cerebellum contains only a trace amount of it.2. Nerveside is uniformly distributed over all parts of the cerebral cortex.3. The cerebral cortex contains the greatest concentration of nerveside. If the nerveside activity of 1 g cerebral cortex is expressed as 100 then the relative activities of the other parts of the C.N.S. are hippocampus 41, caudate nucleus 21, diencephalon (without hypothalamus) 24, midbrain 19, pons 7, medulla 12 and cerebellum 6.4. The nerveside activity of the hypothalamus is the same as that of the cerebral cortex.5. The pattern of distribution of nerveside in the C.N.S. suggests that it may be part of a corticipetal or corticifugal system.

Animals↗

PubMed1978

RNA tumor virus phosphoproteins: primary structural analysis and identification of phosphopeptides.

Two-dimensional tryptic peptide mapping was used to compare the peptide sequences of the phosphoprotein (pp12) of cloned ecotropic and amphotropic wild mouse leukemia viruses, strains 1504 and 292. The maps of two ecotropic isolates were very similar to one another, as were the maps of two amphotropic isolates. There was also extensive similarity between the maps of this protein from ecotropic and amphotropic viruses, although characteristic peptide differences were readily recognized. These differences were consistent with the general type specificity of oncovirus phosphoproteins. The pp12 of the field isoalte of 292 virus contained five phosphopeptides, and the non-phosphorylated and variously phosphorylated species of this pp12 showed identical peptide maps, indicating differential phosphorylation of a single polypeptide.

Base Sequence↗

PubMed1997

Remineralization of enamel subsurface lesions by casein phosphopeptide-stabilized calcium phosphate solutions.

Casein phosphopeptides (CPP) stabilize amorphous calcium phosphate (ACP), localize ACP in dental plaque, and are anticariogenic in animal and in situ human caries model. In this vitro study, CPP-stabilized calcium phosphate solutions were shown to remineralize subsurface lesions in human third-molar enamel. Solutions were used to examine the effect of CPP-calcium phosphate concentration on remineralization. Other solutions were used to examine the effect of increasing pH, which decreased the concentrations of free calcium and phosphate ions and increased the level of CPP-bound ACP. Although most of the remineralizing solutions were supersaturated with respect to the amorphous and crystalline calcium phosphate phases, the solutions were stabilized by the CPP such that spontaneous precipitation of calcium phosphate did not occur. After a ten-day remineralization period, enamel lesions were sectioned, subjected to microradiography, and the mineral content determined by microdensitometry. All solutions deposited mineral into the bodies of the lesions, with the 1.0% CPP-calcium phosphate (pH 7.0) solution replacing 63.9 +/- 20.1% of mineral lost at an averaged rate of 3.9 +/- 0.8 x 10(-8) mol hydroxyapatite/m2/s. The remineralizing capacity was greater for the solutions with the higher levels of CPP-stabilized free calcium and phosphate ions. Remineralization was not significantly correlated with either the CPP-bound ACP of the degrees of saturation for hydroxyapatite, octacalcium phosphate, or ACP. However, remineralization was significantly correlated with the degree of saturation for dicalcium phosphate dihydrate (CaHPO4.2H2O), but his was attributed to the significant correlation of remineralization with the activity gradients from the solution into the lesion of some calcium phosphate ions and ion pairs, in particular the neutral ion pair CaHPO4(0). The CPP, by stabilizing calcium phosphate in solution, maintain high-concentration gradients of calcium and phosphate ions and ion pairs into the subsurface lesion and thus effect high rates of enamel remineralization.

Calcium↗

PubMed1996

The effect of casein phosphopeptides on zinc and calcium absorption from high phytate infant diets assessed in rat pups and Caco-2 cells.

Milk and other foods of animal origin have been shown to improve zinc absorption from phytate-rich diets. The ability of milk proteins and casein phosphopeptides (CPP), the latter formed during digestion of casein, to overcome the inhibitory effect of phytate on zinc and calcium absorption was investigated. Suckling rat pups were given aqueous phytate-containing solutions, oat diet, or soy formula alone or with milk proteins or CPP added. Diets labeled extrinsically with 65Zn and 47Ca were given by gastric intubation. Absorption was determined from measurement of radioisotope activity in intestine, organs, and carcass. Addition of CPP improved zinc and calcium absorption from aqueous phytate-containing solutions and from oat diet. The effect of CPP on calcium absorption from soy formula was less pronounced. The influence of CPP on zinc absorption from aqueous phytate-containing solutions was also examined using a human colon carcinoma-derived cell line, Caco-2. Binding + uptake of 65Zn was determined after incubation with these solutions. Phytate reduced zinc binding + uptake to 79% of the control value. Addition of 14 mumol of CPP/L increased zinc binding + uptake to 94%, whereas 36 and 72 mumol of CPP/L depressed zinc binding + uptake (75 and 39%). In conclusion, CPP improved zinc and calcium bioavailability from high phytate meals in the rat pup model. In the Caco-2 cell system, addition of 14 mumol of CPP/L showed a positive effect on zinc binding + uptake from phytate-containing solutions, whereas higher levels of CPP inhibited zinc binding + uptake.

Animals↗

PubMed1995

Preparation of casein phosphopeptides from casein micelles by ultrafiltration.

Casein phosphopeptides (CPPs), which inhibit the precipitation of calcium phosphate in the intestines, were prepared as CPP-calcium phosphate complexes from casein micelles by the ultrafiltration method. The prepared CPPs hardly contained any other peptides, so there was no need to treat with active carbon to remove the bitter peptides. The sum of alpha s1-CN-5P(f59-79) and beta-CN-4P(f1-25) comprised 60% of the CPP composition by an analysis of the elution pattern from a Q-Sepharose FF column. The content of alpha s1-CN-5P(f59-79), which has high retention ability for calcium phosphate, was the highest in the CPPs.

Animals↗

PubMed1998

Casein phosphopeptides from casein micelles by successive digestion with pepsin and trypsin.

When milk is ingested, casein micelles will be successively digested by pepsin in the stomach and trypsin in the intestine. Therefore, we digested casein micelles successively with pepsin at pH 4.0 and trypsin at pH 7.0, and recovered casein phosphopeptides (CPP) as CPP-calcium phosphate (CP) complexes. The CPP-CP complexes contained 248 mg of calcium/g peptides and 175 mg of inorganic phosphorus/g peptides, which were higher than those of CPP-CP complexes driven from acid-precipitated casein and casein micelles by tryptic digestion only. It contained more alpha S1-CN-5P(f59-79) than the other CPP preparations did.

Calcium Phosphates↗

PubMed2004

Stimulatory effects of casein phosphopeptide (CPP-III) on mRNA expression of cytokines in Caco-2 cells.

The effect of CPP-III, a commercially available casein phosphopeptide, on the mRNA expression of cytokines in Caco-2 cells was investigated. CPP-III enhanced the mRNAs of interleukin (IL)-6 and tumor necrosis factor-alpha while IL-1beta was not affected. The mRNA expression of IL-6 was stronger in the presence of both CPP-III and bacterial components such as peptidoglycan from Lactobacillus acidophilus and lipopolysaccharide from Salmonella typhimurium. These results suggest that CPP-III influences the expression of cytokines in intestinal epithelial cells.

Caco-2 Cells↗

PubMed2004

The relationship between the pY+3 amino acid in the phosphopeptide ligands and the specificity for various SH2 domains.

After consideration of the tertiary structure of the pY+3 binding pocket in SH2 domains, isoleucine of Ac-pYEEIE was replaced with various unnatural aliphatic amino acids and the binding affinities for Lck, Src, and Fyn SH2 domains were measured. We determined the characteristics of the amino acid at the pY+3 position in the phosphopeptide ligands for the specificity for the SH2 domains.

Amino Acids↗

PubMed1986

Casein phosphopeptide (CPP) enhances calcium absorption from the ligated segment of rat small intestine.

A casein phosphopeptide (CPP) was prepared from beta-casein of cow's milk and the effect of this peptide on the absorption of calcium from a ligated segment of rat small intestine was investigated. CPP injected into a ligated loop of rat small intestine enhanced absorption of calcium from the loop and augmented the deposition of calcium in the femur. Furthermore, CPP inhibited the precipitation of calcium phosphate in vitro, suggesting that this peptide enhances calcium absorption from the small intestinal lumen by increasing the concentration of soluble calcium. This new evidence confirms our previous hypothesis that CPP is an important factor in raising the availability of calcium in milk.

Animals↗

PubMed1994

The influences of casein phosphopeptides on metabolism of ectopic bone induced by decalcified bone matrix implantation in rats.

The effect of casein phosphopeptides (CPP) on bone metabolism was studied in the ectopic bone induced by the implantation of decalcified bone matrix in rats. Forty-two Wistar male rats of 7 weeks old were fed low calcium diets (0.39% of calcium) with or without supplying 0.50% of CPP, or a control diet (0.91% of calcium) without CPP supplementation. After a 1-week preliminary period, each rat was subcutaneously implanted with 30 mg of demineralized bone matrix powder. Fourteen and 21 days after the implantation, the implants were harvested from 7 rats of each group. Calcium content in the graft was not significantly different among all groups on day 14. Subsequently, the content of calcium rapidly increased in the grafts irrespective of diets given. However, the graft of the CPP- group contained less calcium than the other groups and the calcium content was more in the control rats compared to the CPP+ animals on day 21. Alkaline phosphatase activity (an index of bone and cartilage calcification) was lower in the control group than in the CPP+ group on day 14. The enzyme activity subsequently decreased in the control group but the activity was not changed in the other groups. As a result, the activity of alkaline phosphatase was lower in the control animals than in the other rats on day 21. Tartrate-resistant cap phosphatase activity (an index of bone resorption) was higher in the CPP--group compared to the control on day 14. On day 21, the activity was higher in the CPP--group compared to the others.(ABSTRACT TRUNCATED AT 250 WORDS)

Alkaline Phosphatase↗

PubMed1998

Preparation and characterization of micellar calcium phosphate-casein phosphopeptide complex.

Micellar calcium phosphate (MCP) in bovine milk was separated as the complex with casein phosphopeptide (CPP) by the following procedures. Rennet curd obtained from skim milk was suspended in water, the pH was adjusted to 4.6, and the suspension was centrifuged at 1,000 x g. CPP was separated from the precipitated casein by tryptic hydrolysis and ethanol precipitation. The supernatant, which contained calcium and inorganic phosphate liberated from casein micelles by acidification, and CPP were mixed; the pH was adjusted to 6.7; and then the solution was lyophilized. From 1 L of skim milk, 3.16 g of the MCP-CPP complex was obtained. The dried MCP-CPP complex was easily dissolved in water and contained 12.7% calcium, 0.3% magnesium, 3.4% inorganic phosphorous, and 2.2% organic phosphorous. No crystal structure of hydroxyapatite was shown in the MCP-CPP complex by the X-ray diffraction analysis, although the pattern of NaCl crystal was observed. The X-ray diffraction pattern of commercial whey mineral, which was prepared by precipitation at alkaline pH from rennet whey, was similar to that of hydroxyapatite. It was confirmed by high-performance gel chromatographic analysis that the form of calcium phosphate in the MCP-CPP complex was similar to that of casein micelles. The MCP-CPP complex was also separated from commercial rennet casein. The method for the separation of MCP-CPP complex described above can be applied to the large-scale preparation.

Animals↗

PubMed1999

Bioavailability of milk micellar calcium phosphate-phosphopeptide complex in rats.

We evaluated the bioavailability of two types of calcium from milk in two experiments. One was a micellar calcium phosphate-phosphopeptide (MCP-PP) complex in which the chemical form was similar to the original form of milk, and the other was a commercial whey calcium in which the chemical form was different from that of milk. In experiment 1, the calcium absorption, bone mineral density, and bone strength were examined when growing female rats were fed either MCP-PP complex or whey calcium as the sole source of calcium for 46 d. In experiment 2, the calcium solubility in the small intestine was measured when female rats were meal-fed either MCP-PP complex or whey calcium. The apparent calcium absorption rate in both groups decreased time-dependently during the experimental period, but the time-dependent change in the apparent calcium absorption rate was statistically different. It decreased more slowly in rats fed the MCP-PP diet than in rats fed the whey calcium diet. The bone mineral density of the femur in rats fed the MCP-PP diet was significantly higher than that of the rats fed the whey calcium diet. The bone strength (breaking force and energy) of the femur in rats fed the MCP-PP diet was higher than in the rats fed the whey calcium diet. The amount of soluble calcium in the small intestinal contents in rats at 2.5 h after ingestion of the MCP-PP diet was approximately three times higher than that found in rats fed the whey calcium diet. These results indicate that the calcium bioavailability of MCP-PP complex is higher than that of whey calcium, and this difference is due in part to the solubility in the intestine.

Absorption↗

PubMed2002

Absorption of zinc from dietary casein phosphopeptide complex with zinc in rats given a soybean protein-based diet.

The absorption of zinc (Zn) in the form of casein phosphopeptide (CPP) complex was compared with that of its chloride form in rats given a soybean protein-based diet. We prepared 67Zn complex with CPP (67Zn-CPP). Male rats were given a diet containing ZnCl2 in the preliminary period. After overnight food deprivation, they were fed a test meal labeled 67Zn-CPP or 67ZnCl2 (4 g Zn-free diet + 0.12 mg 67Zn) with 0.5 mg Dysprosium (Dy) as a fecal marker. Feces were collected for 5 d and analyzed for 67Zn isotopic enrichment and Dy concentration with an inductively coupled plasma mass spectrometer. Fecal Dy excretion closely paralleled that of 67Zn, and more than 89% of the administered Dy was recovered in the feces collected for 5 d. Moreover, the Zn source did not affect the excretion pattern of 67Zn. Since Dy and 67Zn were almost excreted within 3 d after the administration, the apparent absorption of 67Zn was calculated from the pooled data for 3 d. The source of Zn did not affect the apparent absorption of 67Zn. These results suggested that dietary Zn in the form of CPP complex did not show higher absorbability in rats.

Animals↗

PubMed2005

Characterization of casein phosphopeptides from fermented milk products.

This study dealt with the potential of fermented milk products as a source of functional casein phosphopeptides (CPPs) using plain yogurts and Camembert cheeses. The CPPs were prepared by tryptic digestion from four commercially available plain yogurts (P1-P4), five Camembert cheeses (C1-C5), and raw milk. From portions with a 1-g protein content of the plain yogurts, the Camembert cheeses, and the raw milk, 171 mg, 139 mg, and 146 mg of CPPs were obtained, respectively. The Camembert cheeses retained high amounts of organic phosphorus (32 microg) per 1 mg CPPs compared to the raw milk (15 microg) and plain yogurts (16 microg). Reverse-phase high-performance liquid chromatographic analysis showed that the elution patterns and retention times of the three major peaks of CPPs from P1 and C1 were similar to those from raw milk. Moreover, CPPs from P1 and C1 showed a mitogenic effect, while CPPs from C1 showed an IgA-enhancing effect in mouse spleen cell cultures. These results suggest that fermented milk products such as plain yogurts and Camembert cheeses generate functional CPPs in the body and exert beneficial effects on the immune system.

Animals↗

PubMedDate not supplied

[Comparative study of phosphopeptides in various animal tissues].

We determined the phosphopeptide (PP) level in several tissues and compared the values to the phosphoprotein and phosphatide level. We studied whole organs and subcellular fractions isolated from these organs. The results showed that the PP were preferentially localised in membranes. Among all the organs analyzed, the electrical organ of "Torpedo marmorata" had the highest PP level. The phosphoprotein distribution was different from the PP one; the highest level of phosphorproteins was found in nuclei. There was also an increase in phosphoprotein level comparing whole tissues and membranes isolated from the same tissue. The preferential localisation of PP in membranes is also suggested by the parallelism between PP and phosphatide level, which is also higher in membranes than in whole organs. The peculiar polyanionic structure, as well as the active metabolism and the membranous localisation of PP support the hypothesis that these compounds might be good intermediates in active transport mechanisms.

Anguilla↗

PubMed1992

Efficient solid phase synthesis of mixed Thr(P)-, Ser(P)- and Tyr(P)-containing phosphopeptides by "global" "phosphite-triester" phosphorylation.

The synthesis of the mixed Thr(P)/Tyr(P)-containing peptide, Ala-Thr(P)-Tyr(P)-Ser-Ala, was accomplished by "phosphite-triester" phosphorylation of the resin-bound Thr/Tyr-containing peptide using di-t-butyl N,N-diethylphosphoramidite as the phosphitylation reagent. The pentapeptide-resin was assembled by Fmoc/solid-phase peptide synthesis with the use of PyBOP as coupling reagent and the hydroxy-amino acids incorporated as side-chain free Fmoc-Tyr-OH and Fmoc-Thr-OH. "Global" bis-phosphorylation of the peptide-resin was accomplished by treatment with di-t-butyl N,N-diethylphosphoramidite/1H-tetrazole followed by m-chloroperoxybenzoic acid oxidation of the intermediate di-t-butylphosphite triester. Simultaneous peptide-resin cleavage and peptide deprotection was effected by treatment of the peptide-resin with 5% anisole/TFA and gave the Thr(P)/Tyr(P)-containing phosphopeptide in high yield and purity. In addition, the tyrosyl residue was found to be phosphitylated in preference to the threonyl residue since the phosphitylation of the pentapeptide-resin using only 1.1 equiv. of di-t-butyl N,N-diethylphosphoramidite gave Ala-Thr-Tyr(P)-Ser-Ala as the major product and both Ala-Thr(P)-Tyr(P)-Ser-Ala and Ala-Thr-Tyr-Ser-Ala as minor products.

Amino Acid Sequence↗