Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “PROLINE”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,279 records · Page 71Linked to original sources
PubMed1997

Effects of dipeptides containing the amino acid, proline on the chemotaxis of Tetrahymena pyriformis. Evolutionary conclusions on the formation of hormone receptors and hormones.

Our investigations demonstrate that proline-containing dipeptides can provoke a chemosensory response from the unicellular Tetrahymena pyriformis. The chemotactic effects of the dipeptides have a close relationship with the side chain and the lipophilicity of the amino-terminal amino acid. Comparison of 'mirror' variants of proline-containing dipeptides points to the fact that dipeptides with small side chain and non-polar character amino acids (Gly-Pro, Ala-Pro) are preferred on the amino-terminal end. In the case of amino acids with very variable side chains, small (Pro-Gly) and the large side chain and non-polar character amino acids (Pro-Leu, Pro-Phe) on the carboxyl-terminal end can induce significant chemotactic responses. With valine on any terminus the proline-containing dipeptide induced a weak repellent effect.

Animals↗
PubMed1998

Interactions of proline, serine, and leucine with isolated spinach thylakoids: solute loading during freezing is not related to membrane fluidity.

We have investigated the physical mechanisms through which amino acids influence freeze-thaw damage to isolated spinach (Spinacia oleracea L.) thylakoid membranes. The cryoprotective amino acid proline reduced osmotic membrane rupture during thawing by reducing solute loading of thylakoids during freezing for 1 h to -5 degreesC. Evidence for binding of proline to the thylakoid surface was obtained by determining the partitioning of the hydrophobicity-sensitive dye merocyanine 540 between the bulk solution and the membranes in the presence of different concentrations of proline. This binding led to a decrease in lipid fluidity at the membrane surface, as measured with fluorescence depolarization spectroscopy using the probe trimethylammonium-diphenylhexatriene (TMA-DPH). The hydrophobic core of the membranes, as probed with 1,6-diphenyl-1,3,5,-hexatriene, was not influenced. Surprisingly, cryotoxic concentrations of both serine and leucine resulted in the same amount of reduction of thylakoid lipid fluidity, without reducing solute loading during freezing. In the case of these cryotoxic amino acids, unknown additional interactions with the membranes must result in membrane destabilization during a freeze-thaw cycle.

Leucine↗
PubMed2001

Molecular cloning, physical mapping, and expression analysis of a novel gene, BCL2L12, encoding a proline-rich protein with a highly conserved BH2 domain of the Bcl-2 family.

Members of the Bcl-2 family of apoptosis-regulating proteins contain at least one of the four evolutionarily conserved domains, termed BH1, BH2, BH3, or BH4. Here, we report the identification, cloning, physical mapping, and expression pattern of BCL2L12, a novel gene that encodes a BCL2-like proline-rich protein. Proline-rich sites have been shown to interact with Src homology region 3 (SH3) domains of several tyrosine kinases, mediating their oncogenic potential. This new gene maps to chromosome 19q13.3 and is located between the IRF3 and the PRMT1/HRMT1L2 genes, close to the RRAS gene. BCL2L12 is composed of seven coding exons and six intervening introns, spanning a genomic area of 8.8 kb. All of the exon-intron splice sites conform to the consensus sequence for eukaryotic splice sites. The BCL2L12 protein is composed of 334 amino acids, with a calculated molecular mass of 36.8 kDa and an isoelectric point of 9.45. The BCL2L12 protein contains one BH2 homology domain, one proline-rich region similar to the TC21 protein and, five consensus PXXP tetrapeptide sequences. BCL2L12 is expressed mainly in breast, thymus, prostate, fetal liver, colon, placenta, pancreas, small intestine, spinal cord, kidney, and bone marrow and to a lesser extent in many other tissues. We also identified one splice variant of BCL2L12 that is primarily expressed in skeletal muscle.

Amino Acid Sequence↗
PubMed1993

Kinetic models for unfolding and refolding of ribonuclease T1 with substitution of cis-proline 39 by alanine.

The replacement of cis proline 39 of ribonuclease T1 by an alanine residue leads to a decrease in stability by about 20 kJ/mol and to major changes in the folding kinetics that are not easily explained by the proline model for protein folding. In particular, a novel very slow reaction is observed in the refolding of the Pro39Ala variant. Here the unfolding and refolding kinetics of this protein are further investigated. We show that the very slow reaction is not a prolyl isomerization. It is not created by a slow isomerization of the unfolded protein, nor is it catalyzed by prolyl isomerase, and all molecules have to undergo this reaction during refolding. Most of the unfolded Pro39Ala molecules contain an incorrect trans isomer at the remaining cis Pro55. They use a sequential pathway for refolding, in which trans to cis isomerization at Pro55 precedes the very slow reaction. The refolding of the minor fraction of unfolded Pro39Ala molecules with a correct cis isomer at proline 55 is a single first-order reaction that is limited in rate by the very slow step. The folding mechanism of wild-type ribonuclease T1 cannot be used to explain these results and independent mechanisms are proposed to model the unfolding and refolding of the Pro39Ala variant. The molecular interpretation of the changes in the folding mechanism is tied to the question, as to whether the cis character of the peptide bond at position 38-39 is maintained after the substitution of Pro39 by alanine. A possible explanation could be that the novel very slow folding reaction involves the trans to cis isomerization of the Tyr38-Ala39 bond. Such a reaction is probably slow, since the activation energy is high and since tight coupling with the formation of structure is required to stabilize the cis form of a non-prolyl peptide bond. Alternatively, the strong decrease in folding rate could be correlated with the general destabilization of ribonuclease T1 by the Pro39Ala mutation.

Alanine↗
PubMed1994

Sequence analysis identifies the proline dehydrogenase and delta 1-pyrroline-5-carboxylate dehydrogenase domains of the multifunctional Escherichia coli PutA protein.

The PutA protein of Escherichia coli has two enzymatic activities: proline dehydrogenase (PDH) and delta 1-pyrroline-5-carboxylate dehydrogenase (P5CDH). It associates with the cytoplasmic membrane as PDH and P5CDH and with put control region DNA as put repressor. Reduction of the PutA flavin by proline, a PutA conformational change and association of PutA with membranes are coincident. The nucleotide base sequence of E. coli putA was determined, that of S. typhimurium putA was updated and the deduced PutA protein sequences were surveyed for catalytic domains and ligand binding sites. The two sequences were very similar (80.5% and 95% on the nucleic acid and protein levels, respectively). Residues 650 through 1130 of PutA were very similar to the sequences of P5C dehydrogenases and aldehyde dehydrogenases from both prokaryotes and eukaryotes. Glutamate 883 and cysteine 917 of PutA were conserved with the corresponding residues in P5C dehydrogenases and with those proposed to be active site residues in the aldehyde dehydrogenases. Those relationships suggest that gamma-glutamic semialdehyde, believed to equilibrate spontaneously with P5C, is the substrate for P5C dehydrogenases. Residues 340 through 590 of PutA were similar in sequence to proline dehydrogenases from Saccharomyces cerevisiae and Drosophila melanogaster. Limited similarities were also found between residues 315 through 357 of PutA and a consensus sequence near a putative active site and FAD-binding region shared by succinate dehydrogenase sequences from several organisms. Since residues 228 through 358 of PutA were similar in sequence to several serine-pyruvate aminotransferases, PutA is proposed to catalyze the hydrolysis of P5C (a Schiff's base intermediate) to gamma-glutamic semialdehyde. A carboxyl-terminal sequence that resembles a leucine zipper motif may be involved in association of PutA with put control region DNA.

1-Pyrroline-5-Carboxylate Dehydrogenase↗
PubMed1995

A proline-rich chitinase from Beta vulgaris.

A gene (Ch1) encoding a novel type of chitinase was isolated from Beta vulgaris. The Ch1 protein consists of an N-terminal hydrophobic prepeptide of 25 amino acids followed by a hevein-like domain of 22 amino acid residues, an unusually long proline-rich domain of 131 amino acid residues with 90 prolines, and finally a catalytic domain of 261 amino acid residues. Proteins with similar proline-rich domains are present in some other plants. The Ch1 gene shows a transient expression in response to fungal infection.

Amino Acid Sequence↗
PubMed1990

Non-existence of a tight association between a 444leucine to proline mutation and phenotypes of Gaucher disease: high frequency of a NciI polymorphism in the non-neuronopathic form.

A 444leucine to proline mutation detected by a NciI polymorphism in the human glucocerebrosidase gene was studied to investigate the correlation of the three clinical phenotypes of Gaucher disease with this mutation in 11 Japanese patients with Gaucher disease (type I, 8 patients; type II, 1 patient; type III, 2 patients) and to determine the feasibility of the use of genomic probe DNA for carrier detection and prenatal diagnosis in 8 Japanese families with Gaucher disease and agreeable to family study (type I, 6 families; type III, 2 families). The homoallelic 444leucine to proline mutation was found only in patients with type I disease. Of the 8 type I patients, 5 had the homoallelic mutation and 2 had one mutant allele. One patient with type II disease did not have this mutant allele. Of the 2 type III patients, one had a single mutant allele whereas the other exhibited no mutation of this kind. These results suggest that the 444leucine to proline mutation is very common in the type I (non-neuronopathic form) disease and is not tightly associated only with neuronopathic types of Gaucher disease in Japanese patients. These findings seem to conflict with others showing that this mutation is partially responsible for the occurrence of neuronopathic Gaucher disease. Thus, the NciI polymorphism will not be useful for the diagnosis of subtypes of Gaucher disease. Carrier detection was feasible in three families with type I disease of the 8 families analyzed by the NciI polymorphism.

Deoxyribonucleases, Type II Site-Specific↗
PubMed1975

A study of 14C-proline and 14C-hydroxyproline incorporation in different homogenate fractions of the hepatopancreas of the snail, Helix pomatia L.

The fate of 14C in snails given 14C-proline and 14C-hydroxyproline has been examined by radiometric analyses of hepatopancreas homogenates. Free 14C-proline and 14C-hydroxyproline in the structural protein of three different hepatopancreas homogenate fractions: (a) granules, (b) small calcium spherites, and (c) large calcium sperites. The presence of hydroxyproline in granules and calcium spherites gives reason to believe that a fibrillar protein related to the collagen-type might occur within these structures. The 14C-proline and 14C-hydroxyproline incorporation test measured total radioactivity of each homogenate fraction, expressed as net counts per minute (cpm) per mg of dry weight of each fraction. The radioactivity of the granule and small calcium spherite fractions was about 6-8 times greater than that of the large calcium spherite fraction.

Animals↗
PubMed1989

Identification of proline-specific carboxypeptidase localized to brush border membrane of rat small intestine and its possible role in protein digestion.

A proline-specific carboxypeptidase (carboxypeptidase P, EC 3.4.12.-) was identified and partially characterized in the brush border membrane fraction of rat intestinal enterocytes and shown to be distinct from pancreatic proteases. The carboxypeptidase activity of isolated brush border membranes, with Z-Gly-Pro-Leu as substrate, was 43 nmol/min/mg protein representing a 16-fold purification when compared with mucosal cell homogenates. Activity was maximal in the middle region of the small intestine, and villus cells had twice the activity of crypt cells. Carboxypeptidase activity was maximal at pH 7.0, was stimulated by divalent cations, and was inhibited by metal chelating agents, suggesting that it is a metalloenzyme. The enzyme had the highest activity with synthetic peptides containing proline penultimate to the carboxy terminus. In vivo patterns of hydrolysis and absorption of amino acids from Z-Pro-Trp were examined using an intestinal perfusion technique. These studies indicate that brush border membrane carboxypeptidase may play an important role in the digestion of proline-containing peptides and proteins.

Animals↗
PubMed1977

Alternative pathways for proline synthesis in mammalian cells.

Proline is synthesized in animal cells by way of two alternative pathways. Both of these pathways are functional in many cell lines. The relative contribution of a pathway to total proline synthesis may be altered by a mutational event. Differences in the developmental origin of a cell line are retained as differences in the pathways of proline synthesis.

Cell Line↗
PubMed1976

Proline endopeptidase and exopeptidase activity in polymorphonuclear granulocytes.

Peptidases capable of releasing proline residues from polypeptides are present in the cytoplasmic fraction of rabbit polymorphonuclear granulocytes. This was shown with peptide substrates where proline is present either at the carboxy-terminal or within the polypeptide chain. Lysosomal and plasma membrane enzymes were inactive towards such polypeptides. The proline residue was hydrolyzed at either its amino end or its carboxy end. It is noteworthy that a Pro:Pro bond was cleaved both in the pentapeptide Thr-Lys-Pro-Arg and the dipeptide Pro:Pro.

Animals↗
PubMed1992

The presence of free D-serine, D-alanine and D-proline in human plasma.

Twelve neutral free amino acids, i.e. serine, threonine, glutamine, asparagine, alanine, proline, methionine, tyrosine, valine, leucine, isoleucine and phenylalanine, were surveyed for the presence of D-enantiomers in plasma samples from patients with renal diseases and from normal subjects. D-serine, D-alanine and D-proline were found in the patient's plasma. The highest concentrations (D/L ratio) of D-serine, D-alanine and D-proline were 0.2362, 0.2087 and 0.0986, respectively. The sum of the contents of the three D-amino acid was shown to be present in the plasma proteins.

Adult↗
PubMed1994

Role of proline in the imprinting developed by dipeptides--in Tetrahymena. Possible role in hormone evolution.

The effects of proline and serine dipeptides containing phenylalanine, alanine and leucine on the behaviour of receptors of Tetrahymena were investigated. Only proline-containing dipeptides were able to develop positive imprinting, and the activity depended on which other amino acid was present in the dipeptide. In contrast to the positive imprinting effect of the dipeptides Pro-Phe and Pro-Ala, the dipeptide Pro-Pro and Pro-Leu caused negative imprinting. Serine dipeptides produced negative imprinting in all cases. The possible importance of proline in the evolution of hormone specificity is discussed.

Animals↗
PubMed2005

Proline-based modulation of 2,4-diacetylphloroglucinol and viable cell yields in cultures of Pseudomonas fluorescens wild-type and over-producing strains.

The antifungal compound 2,4-diacetylphloroglucinol (DAPG) is produced in the rhizosphere of wheat by pseudomonad populations responsible for the natural biological control phenomenon known as "take-all decline." Studies were conducted to elucidate the impact of DAPG and its co-product 2,4,6-trihydroxyacetophenone (THA) on the production of Pseudomonas fluorescens for biological control. Increasing DAPG from 0.1 g/l to 0.5 g/l and THA from 0.05 g/l to 0.5 g/l significantly inhibited the growth and lowered the yield of viable bacteria in liquid cultures. On further examination of these metabolites applied in seed coatings, levels of DAPG and THA exceeding 0.05 mg/g seed significantly reduced wheat germination percentages. The three-way interaction of DAPG, THA, and culture medium ingredients was significant, and greatest seed germination loss (40-50%) was observed when 0.5 mg DAPG and 0.25 mg THA were combined in a coating of 0.5 ml culture medium per gram of seed. Based on the results of Biolog GN microplate, flask, and fermentor screens of C sources, proline was found to optimize the viable cell yields of the P. fluorescens strains tested. The combination of proline with glucose and urea as C and N sources in growth media could be optimized to minimize DAPG production and maximize the vitality of P. fluorescens Q8R1-96 and Q69c-80:miniTn5:phl20 (DAPG over-producer). In production cultures, the proline supply rate offers a potentially useful means to optimize the biological control agent yield and quality.

Antifungal Agents↗
PubMed1992

Rapid robust separation of hydroxyproline and proline.

The presence of hydroxyproline, and the determination of the ratio of the secondary amino acids proline to hydroxyproline, in amino acid hydrolysates specifically identifies collagen and collagen peptides. o-Phthalaldehyde, and then 9-fluorenylmethyl chloroformate, were used to carry out sequential prederivatization of amino acid hydrolysates in an in-line high-performance liquid chromatography sample loop. After derivatization, reversed-phase high-performance liquid chromatography with a C-18 ODS Hypersil cartridge column was used to resolve the hydroxyproline and proline from all primary amino acids, with resolution and detection of hydroxyproline and proline within 2.0 and 2.8 min, respectively, at concentrations in the range of picomoles per microliter of derivatized amino acid. The assay has a turnaround time of 10.75 min.

Chromatography, High Pressure Liquid↗
PubMed1992

High sugar content of extracts interferes with colorimetric determination of amino acids and free proline.

Sugars were found to interfere with the determinations of alpha-amino nitrogen and free proline with ninhydrin. Suitable modifications are proposed for the quantitative analysis of these compounds in the presence of large amounts of carbohydrates. In this new method of proline assay, the improvement consists of using a citrate buffer adjusted to pH 4.6. Free proline is assayed by ninhydrin reagent prepared without phosphoric acid. This latter procedure uses less ninhydrin and appears to be simplified in comparison with the commonly used method. Both procedures permit a simple, sensitive, and specific determination of nitrogenous compounds in crude extracts. Elimination of carbohydrate interference makes our procedure applicable to crude extracts from various food products such as fruits and plants that accumulate soluble carbohydrates.

Amino Acids↗
PubMed1983

Transport of glycine, serine, and proline into spinach leaf mitochondria.

The transport of radioactive glycine, serine, and proline into the matrix of spinach leaf mitochondria was studied using the silicone oil centrifugation technique. The uptake of all three amino acids showed a biphasic characteristic. At concentrations higher than 0.5 mM, an apparent diffusion process dominated. The uptake was not saturable at increasing amino acid concentrations, and there was no accumulation of amino acid in the matrix (i.e., concentration was similar to that in the medium). At concentrations lower than 0.5 mM, in addition to the diffusion process, an active uptake system that accumulated amino acid in the matrix became apparent. This system was partially inhibited by rotenone, antimycin A, and carbonylcyanide-m-chlorophenyl hydrazone. Also, uptake of glycine and serine was mutually inhibitory. These two amino acids exhibited comparatively less inhibitory effect on proline uptake, and proline also did not inhibit glycine or serine uptake. The results suggest that the active uptake system consists of at least two components with different degrees of amino acid specificity. The diffusion process dominates at amino acid concentrations of 0.5 mM or higher, whereas the active uptake system becomes more prominent as the amino acid concentration decreases.

Biological Transport, Active↗
PubMed1979

Sodium gradient dependence of proline and glycine uptake in rat renal brush-border membrane vesicles.

The sodium-dependent entry of proline and glycine into rat renal brush-border membrane vesicles was examined. The high Km system for proline shows no sodium dependence. The low Km system for glycine entry is strictly dependent on a Na+ gradient but shows no evidence of the carrier system having any affinity for Na+. The low Km system for proline and high Km system for glycine transport appear to be shared. Both systems are stimulated by a Na+ gradient and appear to have an affinity for the Na+. The effect of decreasing the Na+ concentration in the ionic gradient is to alter the Km for amino acid entry and, at low Na+ concentrations, to inhibit the V for glycine entry.

Animals↗