scholarly journals Rhesus Monkey (Macaca mulatta) Mucosal Antimicrobial Peptides Are Close Homologues of Human Molecules

2001 ◽  
Vol 8 (2) ◽  
pp. 370-375 ◽  
Author(s):  
Robert Bals ◽  
Christiane Lang ◽  
Daniel J. Weiner ◽  
Claus Vogelmeier ◽  
Ulrich Welsch ◽  
...  
Keyword(s):  
Rhesus Monkey ◽  
Antimicrobial Peptides ◽  
Polyclonal Antibodies ◽  
Amino Acid Sequences ◽  
Model Organisms ◽  
Immune Functions ◽  
Mucosal Surfaces ◽  
High Degree ◽  
Identification And Characterization

ABSTRACT One component of host defense at mucosal surfaces appears to be epithelium-derived antimicrobial peptides. Molecules of the defensin and cathelicidin families have been studied in several species, including human and mouse. We describe in this report the identification and characterization of rhesus monkey homologues of human mucosal antimicrobial peptides. Using reverse transcriptase PCR methodology, we cloned the cDNAs of rhesus monkey β-defensin 1 and 2 (rhBD-1 and rhBD-2) and rhesus monkey LL-37/CAP-18 (rhLL-37/rhCAP-18). The predicted amino acid sequences showed a high degree of homology to the human molecules. The expression of the monkey antimicrobial peptides was analyzed using immunohistochemistry with three polyclonal antibodies to the human molecules. As in humans, rhesus monkey antimicrobial peptides are expressed in epithelia of various organs. The present study demonstrates that β-defensins and cathelicidins of rhesus monkeys are close homologues to the human molecules and indicate that nonhuman primates represent valid model organisms to study innate immune functions.

Characterization of a cDNA for Rhesus Monkey Protein C Inhibitor – Evidence for N-Terminal Involvement in Heparin Stimulation

1995 ◽  
Vol 74 (04) ◽  
pp. 1079-1087 ◽  
Author(s):  
Klaus-P Radtke ◽  
José A Fernández ◽  
Bruno O Villoutreix ◽  
Judith S Greengard ◽  
John H Griffin
Keyword(s):  
Rhesus Monkey ◽  
Protein C ◽  
Activated Protein C ◽  
Pcr Amplification ◽  
Amino Acid Sequences ◽  
Heparin Binding ◽  
Reactive Center ◽  
Protein C Inhibitor ◽  
Polymerase Chain

SummarycDNAs for protein C inhibitor (PCI) were cloned from human and rhesus monkey 1 liver RNAs by reverse transcription and polymerase chain reaction (PCR) amplification. Sequencing showed that rhesus monkey and human PCI cDNAs were 93% identical. Predicted amino acid sequences differed at 26 of 387 residues. Pour of these differences (T352M, N359S, R362K, L3631) were in the reactive center loop that is important for inhibitory specificity, and two were in the N-terminal helix (M8T, E13K) that is implicated in glycosaminoglycan binding. PCI in human or rhesus monkey plasma showed comparable inhibitory activity towards human activated protein C in the presence of 10 U/ml heparin. However, maximal acceleration of the inhibition of activated protein C required 5-fold lower heparin concentration for rhesus monkey than for human plasma, consistent with the interpretation that the additional positive charge (E13K) in a putative-heparin binding region increased the affinity for heparin.

scholarly journals Plasmid-mediated trimethoprim-resistance in Staphylococcus aureus. Characterization of the first gram-positive plasmid dihydrofolate reductase (type S1)

1987 ◽  
Vol 243 (1) ◽  
pp. 309-312 ◽  
Author(s):  
H K Young ◽  
R A Skurray ◽  
S G B Amyes
Keyword(s):  
Staphylococcus Aureus ◽  
Dihydrofolate Reductase ◽  
Specific Activity ◽  
Gram Positive ◽  
Heat Stable ◽  
Dihydrofolate Reductases ◽  
High Degree ◽  
Moderately Resistant ◽  
Identification And Characterization

The trimethoprim-resistance gene located on plasmid pSK1, originally identified in a multi-resistant Staphylococcus aureus from Australia, encodes the production of a dihydrofolate reductase (type S1), which confers a high degree of resistance to its host and is quite unlike any plasmid-encoded dihydrofolate reductase hitherto described. It has a low Mr (19,700) and has a higher specific activity than the constitutive Gram-negative plasmid dihydrofolate reductases. The type S1 enzyme is heat-stable and has a relatively low affinity for the substrate, dihydrofolate (Km 10.8 microM). It is moderately resistant to trimethoprim, and is competitively inhibited by this drug with an inhibitor-binding constant of 11.6 microM. This is the first identification and characterization of a plasmid-encoded trimethoprim-resistant dihydrofolate reductase derived from a Gram-positive species.

Identification and characterization of antimicrobial peptides from the skin of the endangered frog Odorrana ishikawae

Peptides ◽  
2011 ◽  
Vol 32 (4) ◽  
pp. 670-676 ◽  
Author(s):  
Eiko Iwakoshi-Ukena ◽  
Kazuyoshi Ukena ◽  
Aiko Okimoto ◽  
Miyuki Soga ◽  
Genya Okada ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Identification And Characterization

scholarly journals Identification and Characterization of a Novel Tobamovirus from Tropical Soda Apple in Florida

Plant Disease ◽  
2007 ◽  
Vol 91 (3) ◽  
pp. 287-293 ◽  
Author(s):  
Scott Adkins ◽  
Ivanka Kamenova ◽  
Erin N. Rosskopf ◽  
Dennis J. Lewandowski
Keyword(s):  
Seed Transmission ◽  
Amino Acid Sequences ◽  
Vegetable Crops ◽  
Foliar Symptoms ◽  
Tropical Soda Apple ◽  
Initial Survey ◽  
Noxious Weed ◽  
Solanum Viarum ◽  
Identification And Characterization

Foliar symptoms suggestive of virus infection were recently observed on the noxious weed tropical soda apple (Solanum viarum) in Florida. An agent was mechanically transmitted to Nicotiana benthamiana, and virions were isolated from systemically infected leaves. Rod-shaped particles ~300 nm in length were observed in the partially purified preparations by electron microscopy. The host range determined by mechanical inoculation with purified virions included all tested plants in the Solanaceae (16 species including the important vegetable crops, pepper and tomato) and Chenopodiaceae (2 species) but excluded all tested plants in the Ama-ranthaceae, Apocynaceae, Brassicaceae, Caryophyllaceae, Cucurbitaceae, Fabaceae, Lamiaceae, Malvaceae, and Tropaeolaceae, including several common virus indicator hosts. Comparisons of the coat and movement protein nucleotide and deduced amino acid sequences of this putative tobamovirus with recognized members of this genus, indicate that it is a novel tobamovirus that shares the highest level of sequence identity with Pepper mild mottle virus followed by other members of the Solanaceae-infecting subgroup of tobamoviruses. The virus, for which the name Tropical soda apple mosaic virus (TSAMV) is proposed, was found to be widespread in tropical soda apple in peninsular Florida during an initial survey. TSAMV contamination of seed from infected tropical soda apple plants was found, suggesting that seed transmission may be important for TSAMV dissemination and epidemiology.

Immunological characterization of neutral cholesteryl ester hydrolase from rat liver cytosol

1992 ◽  
Vol 70 (9) ◽  
pp. 800-803 ◽  
Author(s):  
Shobha Ghosh ◽  
W. McLean Grogan
Keyword(s):  
Cholesteryl Ester ◽  
Rat Liver ◽  
Polyclonal Antibodies ◽  
Cross Reactivity ◽  
Cholesteryl Ester Hydrolase ◽  
Ester Hydrolase ◽  
Immunological Comparison ◽  
High Degree ◽  
Rat Liver Cytosol

Rabbit polyclonal antibodies were raised against rat liver bile salt-independent neutral cholesteryl ester hydrolase (CEH) and used for subcellular localization and immunological comparison with isoforms from other tissues. Antibodies exhibited a high degree of specificity for the liver CEH through all stages of purification and neutralized 70–80% of the activity of liver cytosolic CEH. They exhibited various levels of cross-reactivity with cytosolic proteins from other tissues, but reacted weakly with pancreatic and intestinal proteins and did not inhibit pancreatic CEH. Cytosol contained 78% of total cellular CEH activity and 75% of CEH immunoreactive protein. Washed microsomes contained 3% of CEH activity and 5% of CEH protein.Key words: cholesteryl esterase, polyclonal antibodies, rat liver, subcellular distribution.

scholarly journals Identification and Characterization of a Mucosal Antimicrobial Peptide Expressed by the Chinchilla (Chinchilla lanigera) Airway

2004 ◽  
Vol 279 (19) ◽  
pp. 20250-20256 ◽  
Author(s):  
Randall H. Harris ◽  
Dennis Wilk ◽  
Charles L. Bevins ◽  
Robert S. Munson ◽  
Lauren O. Bakaletz
Keyword(s):  
Bacterial Colonization ◽  
Upper Airway ◽  
Northern Analysis ◽  
Opportunistic Pathogens ◽  
Rodent Host ◽  
Recombinant Peptide ◽  
Reverse Transcription Pcr ◽  
Mucosal Surfaces ◽  
Identification And Characterization

Cationic antimicrobial peptides (APs) are produced at mucosal surfaces and play a key role as a first line of defense against infection. To understand how APs might impact disease progression in otitis media (OM), our goal was to identify and characterize APs expressed by the epithelium lining the uppermost airway of the chinchilla, the established rodent host for the study of the bacterial-viral pathogenesis in OM. Using a molecular approach, we cloned a cDNA encoding a homolog of human β-defensin 3, designated chinchilla β-defensin-1 (cBD-1), and found by Northern analysis expression of the corresponding mRNA in nasopharyngeal and tongue mucosae as well as skin. By reverse transcription-PCR, cBD-1 mRNA was also detected in RNA isolated from trachea, lung, and Eustachian tube tissues. The predicted mature form of cBD-1, expressed as a recombinant peptide inEscherichia coli, demonstrated bactericidal activity against the three primary opportunistic pathogens of OM as well asCandida albicans. Continued study of this and other APs will allow us to determine their role in bacterial colonization of the upper airway as well as how viruses might contribute to the pathogenesis of OM by modulating AP expression.

Identification and characterization of antimicrobial peptides from skin of Amolops ricketti (Anura: Ranidae)

Peptides ◽  
2012 ◽  
Vol 33 (1) ◽  
pp. 27-34 ◽  
Author(s):  
Hui Wang ◽  
Ran Ran ◽  
Haining Yu ◽  
Zhijun Yu ◽  
Yuhong Hu ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Identification And Characterization

scholarly journals Purification and characterization of an acetone-inducible cytochrome P-450 from hamster liver microsomes

1992 ◽  
Vol 287 (3) ◽  
pp. 863-870 ◽  
Author(s):  
P Puccini ◽  
S Menicagli ◽  
V Longo ◽  
A Santucci ◽  
P G Gervasi
Keyword(s):  
Polyclonal Antibodies ◽  
Cytochrome B5 ◽  
Liver Microsomes ◽  
Amino Acid Sequences ◽  
High Rate ◽  
Hepatic Microsomes ◽  
Syrian Golden Hamsters ◽  
Km Value ◽  
High Degree ◽  
Cytochrome P 450

A form of cytochrome P-450 has been purified to electrophoretic homogeneity from the hepatic microsomes of Syrian golden hamsters treated with acetone. This P-450 form, designated ha P-450j, had an M(r) of approximately 55,000, bound dimethyl sulphoxide and exhibited a CO-reduced absorbance maximum at 451 nm. The absolute spectra of its oxidized form indicated that ha P-450j was predominantly in the low-spin state. In a reconstituted system, ha P-450j showed relatively low catalytic activities towards 7-ethoxycoumarin, 7-ethoxyresorufin, aminopyrine, ethylmorphine and benzphetamine, whereas it catalysed the oxidation of aniline, acetone and thiobenzamide with a high catalytic-centre activity. In addition, ha P-450j catalysed at a high rate the high-affinity component of dimethylnitrosamine N-demethylase; in contrast, only the low-affinity component of diethylnitrosamine N-de-ethylase was efficiently catalysed. The addition of cytochrome b5 to the reconstitution system decreased the Km value for dimethylnitrosamine N-demethylase by a factor of 5 and increased the Vmax. value, and slightly enhanced the other activities. Thiobenzamide and diethyldithiocarbamate were found to be the most effective inhibitors of the ha-P-450j-dependent aniline hydroxylation. Polyclonal antibodies against rat P-450j recognized ha P-450j in immunoblots of control and treated hamster liver microsomes. Treatment of hamsters with acetone increased the apparent abundance of ha P-450j in microsomes, whereas phenobarbital and beta-naphthoflavone did not induce it. Analysis of N-terminal amino acid sequences demonstrated that ha P-450j has a high degree of sequence identity with rat P-450j. All the evidence presented in this study indicates that ha P-450j could represent the hamster orthologue of the previously described CYP2E1(s) of other species.

scholarly journals Conserved and Divergent Mechanisms That Control TORC1 in Yeasts and Mammals

Genes ◽  
2021 ◽  
Vol 12 (1) ◽  
pp. 88
Author(s):  
Yuichi Morozumi ◽  
Kazuhiro Shiozaki
Keyword(s):  
Current Knowledge ◽  
Small Gtpases ◽  
Cellular Growth ◽  
Model Organisms ◽  
Environmental Cues ◽  
Active Research ◽  
Mtorc1 Activation ◽  
Molecular Bases ◽  
Identification And Characterization

Target of rapamycin complex 1 (TORC1), a serine/threonine-protein kinase complex highly conserved among eukaryotes, coordinates cellular growth and metabolism with environmental cues, including nutrients and growth factors. Aberrant TORC1 signaling is associated with cancers and various human diseases, and TORC1 also plays a key role in ageing and lifespan, urging current active research on the mechanisms of TORC1 regulation in a variety of model organisms. Identification and characterization of the RAG small GTPases as well as their regulators, many of which are highly conserved from yeast to humans, led to a series of breakthroughs in understanding the molecular bases of TORC1 regulation. Recruitment of mammalian TORC1 (mTORC1) by RAGs to lysosomal membranes is a key step for mTORC1 activation. Interestingly, the RAG GTPases in fission yeast are primarily responsible for attenuation of TORC1 activity on vacuoles, the yeast equivalent of lysosomes. In this review, we summarize our current knowledge about the functions of TORC1 regulators on yeast vacuoles, and illustrate the conserved and divergent mechanisms of TORC1 regulation between yeasts and mammals.

scholarly journals Identification and characterization of Saccharomyces cerevisiae yapsin 3, a new member of the yapsin family of aspartic proteases encoded by the YPS3 gene

1999 ◽  
Vol 339 (2) ◽  
pp. 407-411 ◽  
Author(s):  
Vicki OLSEN ◽  
Niamh X. CAWLEY ◽  
Jakob BRANDT ◽  
Michi EGEL-MITANI ◽  
Y. Peng LOH
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Cleavage Sites ◽  
Basic Residue ◽  
Aspartic Proteases ◽  
N Terminus ◽  
High Degree ◽  
Identification And Characterization ◽  
Degree Of Similarity

A new aspartic protease from Saccharomyces cerevisiae, with a high degree of similarity with yapsin 1 and yapsin 2 and a specificity for basic residue cleavage sites of prohormones, has been cloned. This enzyme was named yapsin 3. Expression of a C-terminally truncated non-membrane anchored yapsin 3 in yeast yielded a heterogeneous protein between 135–200 kDa which, upon treatment with endoglycosidase H, migrated as a 60 kDa form. Amino-acid analysis of the N-terminus of expressed yapsin 3 revealed two different N-terminal residues, serine-48 and phenylalanine-54, which followed a dibasic and a monobasic residue respectively. Cleavage of several prohormones by non-anchored yapsin 3 revealed a specificity distinct from that of yapsin 1.

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