Design of a bactericidal hydrogel scaffold containing genipin crosslinked HF-18 peptide

Wound healing is a process getting affected by internal and external factors and might be interrupted by infections. To overcome infections during wound healing, novel antibacterial agents such as antimicrobial peptides have gained popularity because of the rising antibiotic resistance. Therefore, in this study, a three-dimensional polymeric scaffold was designed for the controlled release of HF-18 peptide, with the contribution of hyaluronic acid, chondroitin sulfate, and chitosan polymers with the crosslinker genipin. The obtained scaffold structure (OPT) was found to have interconnected pores, was pH-responsive and swelled more in acidic conditions (5446.5% at pH: 5.0). It was observed that HF-18-loaded OPT (P-OPT) was able to release HF-18 peptide both in acidic and neutral conditions in a controlled release manner. This study also demonstrated that both OPT and P-OPT were biocompatible and promoted L929 cell attachment and migration. Antimicrobial activity assessments demonstrated that P-OPT was effectively bactericidal on Staphylococcus aureus and methicillin-resistant S. aureus. Moreover, OPT produced a synergistic effect on the antimicrobial activity of HF-18 peptide, as P-OPT showed activity below the reported MIC value. As a result, OPT is considered a promising scaffold as a carrier for HF-18 for wound healing.     

Convergent evolution of cysteine residues in sperm protamines of one genus of marsupials, the Planigales

A characteristic feature of the sperm P1 protamines of eutherian mammals is the constant presence of six to nine cysteine residues per molecule. During spermiogenesis these residues become oxidized to form a three-dimensional network of disulfide bridges between, and within, protamine molecules in the sperm chromatin. This covalent cross linking strongly stabilizes eutherian sperm nuclei. In contrast, protamines sequenced from teleost fish, birds, monotremes, and marsupials all lack cysteine residues and their sperm nuclei, without the stabilizing cross links, are easily decondensed in vitro. We have now found that one genus of tiny, shrewlike dasyurid marsupials, the Planigales, possess P1 protamines containing five to six cysteine residues. These residues appear to have evolved since the divergence of Planigales from other members of the family Dasyuridae, such as the marsupial mouse, Sminthopsis crassicaudata. We believe this constitutes a case of convergent evolution in a subfamily of dasyurid marsupials toward the cysteine-rich eutherian form of sperm protamine P1.      

Pseudoephedrine is without ergogenic effects during prolonged exercise

Gillies, Hunter, Wayne E. Derman, Timothy D. Noakes, Peter Smith, Alicia Evans, and Gary Gabriels.Pseudoephedrine is without ergogenic effects during prolongedexercise. J. Appl. Physiol. 81(6): 2611-2617, 1996.This study was designed to measure whether a single dose of 120 mg pseudoephedrine ingested 120 min before exercise influencesperformance during 1 h of high-intensity exercise. The effects ofexercise on urinary excretion of the drug were also studied. Tenhealthy male cyclists were tested on two occasions, separated by atleast 7 days, by using a randomly assigned, double-blind,placebo-controlled, crossover design. Exercise performance was testedduring a 40-km trial on a laboratory cycle ergometer, and skeletalmuscle function was measured during isometric contractions. On a thirdoccasion, subjects ingested 120 mg pseudoephedrine but did not exercise[control (C)]. Pseudoephedrine did not influence eithertime trial performance [drug (D) vs. placebo: 58.1 ± 1.4 (SE) vs. 58.7 ± 1.5 min] or isometric muscle function. Urinary pseudoephedrine concentrations were significantly increased 1 h after exercise (D vs. C: 114.3 ± 27.2 vs. 35.4 ± 13.1 µg/ml; P < 0.05). Peak plasma pseudoephedrineconcentrations (P < 0.05) but not time taken to reach peakplasma concentrations or the area under the plasma pseudoephedrineconcentration vs. time curve was significantly increased in the totalgroup with exercise (D vs. C). In three subjects, plasmapseudoephedrine concentrations were not influenced by exercise. Onlythese subjects showed increased urinary pseudoephedrine excretionduring exercise. We conclude that a single therapeutic dose ofpseudoephedrine did not have a measurable ergogenic effect duringhigh-intensity exercise of 1-h duration, but plasma drug concentrationsand urinary excretion were altered by exercise. These findings havepractical relevance to doping control regulations in internationalsporting competitions.

     

Nucleotide sequences of liver, lachrymal, and submaxillary gland mouse major urinary protein mRNAs: mosaic structure and construction of panels of gene-specific synthetic oligonucleotide probes.

The mouse major urinary proteins (MUPs) are encoded by a gene family of about 35 to 40 members. MUPs are synthesized in at least six secretory tissues under a variety of developmental and endocrine controls, but the identities of the individual genes expressed in each tissue have not previously been established. In this article, we present the nucleotide sequences of five MUP mRNAs which we designate MUP I through V. MUPs I, II, and III are the most abundant MUP mRNA species in the liver, and MUPs IV and V are the most abundant MUP mRNA species in the lachrymal gland and the submaxillary gland, respectively. The sequence data show that each of the five mRNAs is encoded by a distinct member of the gene family. The structures of the MUP mRNA consist of interspersed segments of variable and conserved sequences. On the basis of the sequences of the variable segments, gene-specific panels of synthetic oligonucleotide probes were prepared. The gene-specific panels were used to identify cloned genes and, as described in the accompanying paper (K. Shahan, M. Denaro, M. Gilmartin, Y. Shi, and E. Derman, Mol. Cell. Biol. 7:1947-1954, 1987), to characterize the expression of MUP genes I through V.     

MINERAL DISTRIBUTION IN RELATION TO FRUIT DEVELOPMENT AND MONOCARPIC SENESCENCE IN ANOKA SOYBEANS

The changes in distribution of several important mineral nutrients (N, K, Ca, Mg, Mn, and Fe) were studied in relation to monocarpic senescence (measured as leaf yellowing) and fruit development in hydroponically-grown (and to a lesser extent field-grown) Anoka soybeans with particular emphasis on the leaves and seeds. Only N shows a clear redistribution from the leaves to the seeds as the seeds grow, and this transfer starts before visible leaf yellowing. K, Ca, Mn and Fe do not seem to redistribute, but Mg may undergo limited redistribution. Depodding prevents the drop in the amounts of minerals in attached leaves by blocking leaf shedding and/or redistribution and also creates some quantitative changes in mineral distribution. On a g fresh weight basis, only the N content of leaf blades decreases during yellowing; the K, Mg, Ca, Mn and Fe contents do not decrease. Therefore, depletion of the latter minerals from the leaves cannot be responsible for their yellowing. Although N deficiency alone could cause foliar chlorosis, the monocarpic yellowing pattern is distinctly different from that induced by N deprivation.     

Escherichia coli alkaline phosphatase localized to the cytoplasm slowly acquires enzymatic activity in cells whose growth has been suspended: a caution for gene fusion studies.

Alkaline phosphatase is normally localized to the periplasm of Escherichia coli and is unable to fold into its native conformation if retained in the cytoplasm of growing cells. The alkaline phosphatase activity of E. coli expressing a version of the protein without a signal sequence was nonetheless found to increase gradually when the growth of cells was suspended. At least 30% of the protein was activated over the course of several hours when freshly grown exponential-phase cells were held on ice. Similar behavior was observed with cells expressing certain other mutant versions of alkaline phosphatase that are retained in the cytoplasm. The activation resulted not from the passage of the alkaline phosphatase into the periplasm but from the slow folding of alkaline phosphatase into its native conformation in the cytoplasm. These findings indicate that the mechanism by which proteins are normally kept reduced in the cytoplasm fails to function if cells are not growing. It was found that the addition of the sulfhydryl-alkylating agent iodoacetamide to cells after growth blocks this activation completely. This treatment can therefore diminish the likelihood of spurious enzyme activity measurements in studies that make use of alkaline phosphatase fusion proteins.