Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Wool”

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 307 records · Page 17Linked to original sources
PubMed1989

The amino acid sequence of component 7c, a type II intermediate-filament protein from wool.

Component 7c is one of the four homologous type II intermediate-filament proteins that, by association with the complementary type I proteins, form the microfibrils or intermediate filaments in wool. Component 7c was isolated as the S-carboxymethyl derivative from Merino wool and its amino acid sequence was determined by manual and automatic sequencing of peptides produced by chemical and enzymic cleavage reactions. It is an N-terminally blocked molecule of 491 residues and Mr (not including the blocking group) of 55,600; the nature of the blocking group has not been determined. The predicted secondary structure shows that component 7c conforms to the now accepted pattern for intermediate-filament proteins in having a central rod-like region of approximately 310 residues of coiled-coil alpha-helix flanked by non-helical N-and C-terminal regions. The central region is divided by three non-coiled-coil linking segments into four helical segments 1A, 1B, 2A and 2B. The N-and C-terminal non-helical segments are 109 and 71 residues respectively and are rich in cysteine. Details of procedures use in determining the sequence of component 7c have been deposited as a Supplementary Publication SUP 50152 (65 pages) at the British Library Document Supply Centre, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1989) 257,5. The information comprises: (1) details of chemical and enzymic methods used for cleavage of component 7c, peptides CN1, CN2 and CN3, and various other peptides, (2) details of the procedures used for the fractionation and purification of peptides from (1), including Figures showing the elution profiles from the chromatographic steps used, (3) details of methods used to determine the C-terminal sequence of peptide CN3, and (4) detailed evidence to justify a number of corrections to the previously published sequence.

Amino Acid Sequence↗
PubMed1978

Effects of abomasal supplements of methionine on the wool follicles and skin of wheat-fed sheep.

In wheat-fed sheep, supplemented abomasally with 1.5-6.0 g methionine per day, poor formation and improper keratinization of the wool fibres were evident 4 days after the start of the methionine supplementation. This led to kinking of the fibres. Subsequently severe distortion of the fibres, accompanied by gross thickening of the outer root sheaths, occurred in the distal (upper) halves of most follicles. Within this thickened region partial degradation of the distorted fibres occurred before emergence from the skin surface, causing a marked reduction in the tensile strength of the wool. It is postulated that kinking of the fibres stimulated the accumulation of outer root sheath cells, which led to hyperactivity of the process that normally degrades the inner root sheath, so that the poorly keratinized fibres were also partly degraded. Thickening of the epidermis and cellular infiltration of the upper dermis sometimes occurred during the infusions of methionine, whereas there were negligible effects on the sebaceous and sweat glands. Disappearance of the excess accumulation of outer root sheath cells after cessation of the methionine supplementation occurred gradually following improvement in keratinization and elimination of kinking of the fibres.

Abomasum↗
PubMed1978

An electron microscope study of fibril: matrix arrangements in high- and low-crimp wool fibres.

The crimped structure of wool fibres is generally associated with a bilateral arrangement of ortho- and paracortical cells. The most obvious difference between these cell types is in the arrangement and relative proportions of microfibril and matrix proteins that constitute the fibre cortex. In the low-crimp fibres examined there is a poorer expression of bilateral cortical asymmetry compared with the high-crimp wools together with a higher proportion of intermediate-staining mesocortical cells. These mesocortical cells exhibit much more regular arrays of microfibrils than paracortical cells. It is suggested that the packing arrangement of microfibrils in all three cell types is basically hexagonal and the variation observed in mature cells is a function of the fibril:matrix ratio.

Animals↗
PubMed1978

Dexamethasone concentrations in ovine plasma during its intravenous infusion, its relation to the production of some endogenous hormones, and some of the effects on wool growth.

Plasma concentrations of dexamethasone have been measured in sheep during an 8-day infusion of dexamethasone-21 phosphate. The dexamethasone concentration profiles generally revealed a reproducible pattern with three phases--a peak during the first 48 h infusion which was followed by falling concentrations during the next 5 days, and a small increase in dexamethasone concentration during the final 24 h infusion was not uncommon. The pattern of dexamethasone concentrations was retained when dosage was arranged in such a way as to infuse increasing quantities of hormonal analogue as infusion progressed. Aspects of the metabolism of the analogue are discussed. Endogenous thyroxine and cortisol were significantly depressed during infusion. In these experiments wool was completely shed in three out of four animals dosed at a rate of 8.5 mg dexamethasone/kg0.75. The recovery of wool growth to its pretreatment values occurred by about one month after infusion. The consumption of food and body weight increases were satisfactory during the post-infusion period.

Animals↗
PubMed1981

Structural studies on the microfibrillar proteins of wool: characterization of the alpha-helix-rich particle produced by chymotryptic digestion.

The alpha-helix-rich particle produced by chymotryptic digestion of the reduced and alkylated microfibrillar proteins of wool was characterized by physicochemical methods. The preparations were homogeneous with respect to size and the particle molecular weight was found to be 50 200 +/- 2 000. Hydrodynamic methods indicated a length of about 20 nm for the particle. The properties of the particle, derived from two methods of isolation of the microfibrillar proteins, were identical and were also independent of the type of wool used. From a consideration of the molecular weight in denaturing solvents and from cross-linking experiments with dimethyl suberimidate a four-chain structure, consisting of a pair of double-stranded alpha-helices, is proposed for the particle.

Animals↗
PubMed1985

Characterization of melanocytes in wool-bearing skin of Merino sheep.

The distribution and character of melanocytes in the wool-bearing skin of Merino sheep of known genotypes were examined by light and electron microscopy. In black Merino sheep (ww, homozygous recessive), melanocytes were localized within three regions of the skin: epidermal-dermal border, outer root sheath and follicle bulb. Melanocytes within these regions were found to be actively producing melanin, had numerous dendritic extensions and were able to transfer melanin to adjacent keratinocytes. In a black Merino sheep whose fibres were white due to an experimentally induced copper deficiency the melanocytes were amelanotic. In contrast, for both WW (homozygous dominant) and Ww (heterozygous) white Merino sheep melanocytes were observed only at the epidermal-dermal border of the epidermis. The melanocytes appeared also to differ in character containing less melanin, appearing less dendritic in shape and having a reduced ability to transfer melanin to adjacent keratinocytes. The gene for white fleece (W), therefore, appears able to regulate pigmentation in Merino sheep, at least in part, by controlling the location and activity of melanocytes within the wool-bearing skin.

Animals↗
PubMed1998

The effects of fibroblast growth factors 1 and 2 on fibre growth of wool follicles in culture.

The effects of fibroblast growth factor-1 (FGF-1) and FGF-2 on fibre growth and follicle function were examined using a previously described procedure to culture wool follicles. Because the FGFs bind to glycosaminoglycan components of the extra-cellular matrix, we also investigated interactions between FGF-1 and FGF-2 with heparin on wool fibre growth. Individual follicles were microdissected from Merino sheepskin and transferred to culture. Follicles increased in length for 6 days, and in all groups, no significant differences in follicle length were observed. Increase in follicle length was associated with fibre growth, follicles maintained normal anagen morphology and incorporated [3H]thymidine into the bulb and outer root sheath cells. Follicles in all treatments continued to produce fibre keratins, as detected by immunohistochemistry. However, the patterns of fibre and cytoskeletal proteins incorporating [35S]methionine in control and treated follicles were significantly different. We found a considerable decrease in the intermediate filament keratins or low sulphur proteins in follicles cultured in the presence of FGF-1 and FGF-2 compared to controls. The majority of proteins detected in these samples were acidic high sulphur proteins. These studies provide evidence for a specific role for the fibroblast growth factors in the regulation of fibre differentiation.

Animals↗
PubMed1987

Apoptosis in wool follicles during mouse epidermal growth factor (mEGF)-induced catagen regression.

Depilatory infusions of mouse epidermal growth factor (mEGF) induced regressive involution (catagen) in the wool follicles of Merino sheep. The follicles were examined by transmission electron microscopy prior to infusion and at intervals during catagen regression in order to determine the mechanism(s) involved in follicle involution. Cell deletion by apoptosis occurred in all cell types in the proximal region of catagen follicles between 12 h and 6 days after the beginning of infusion. Apoptosis also occurred in the basal layer of involuting sebaceous glands at 2 and 3 days, following earlier mEGF-induced proliferation. This process involved nuclear chromatin condensation and margination in single, scattered cells which subsequently fragmented and were ultimately phagocytosed and degraded by adjacent unaffected cells. It was concluded that during mEGF-induced catagen, wool follicle involution was accomplished largely through cell death and deletion by apoptosis.

Animals↗
PubMed1992

Localization of epidermal growth factor immunoreactivity in sheep skin during wool follicle development.

Interactions among the cells and matrices of the epidermis and mesenchyme of skin are essential for hair follicle initiation and development. The identification of receptors for epidermal growth factor (EGF) on epithelial components of the follicle during growth has suggested that the ligand participates in some of these events. We have used affinity-purified antibodies together with an alkaline phosphatase detection procedure to investigate the distribution of EGF in the skin of the sheep during wool follicle formation. Immunoreactivity was restricted to the periderm and intermediate layers of fetal epidermis at 55 d of gestation, when the first wave of wool follicles are initiated. This particular distribution persisted during subsequent development but never became associated with the basal cells of the epidermis. The activity was lost around 118 d, coinciding with sloughing of the periderm. No immunoreactivity was found in the plugs or the dermal condensations of the developing follicles. At approximately 105 d of gestation, however, reactions were detected in the outer root sheath as the follicles matured and in the differentiating cells of the sebaceous glands. A similar distribution pattern was also noted at 140 d, just prior to birth, and in adult animals, indicating that EGF was sequestered and perhaps synthesized within the follicle. The presence of immunoreactive material was also associated with the pilary canals and the skin surface, suggesting that this may have had its origin in the sebaceous glands. We examined this using a radioreceptor assay for EGF. Material washed from the skin surface and sebaceous gland extracts were found to displace 125I-EGF from rat liver membranes, in parallel with mouse EGF.

Animals↗
PubMed1996

Note: microbial resistance of wool fabric treated with bis-Quats compounds.

In this paper, the antibacterial activity against Bacillus pumilus, Staphylococcus aureus, Escherichia coli and Pseudomonas aeruginosa of the wool fabrics treated with new antimicrobial bis-quaternary surfactants, DABK and DABB, is studied. The activity was established on the basis of the agar diffusion and protective antibacterial test results and on the basis of scanning electron microscopy (SEM) observation. The results were compared with the HTAB, a monoquaternary surfactant of conventional use. The results from the agar diffusion and protective antibacterial tests do not enable us to confirm whether these compounds are potentially useful antimicrobial agents for the protection of textiles. However, SEM observations show clearly the efficacy of these compounds to protect the wool fabrics against the micro-organisms. SEM has been a useful technique for the assessment of antibacterial activity in textiles.

Animals↗
PubMed1985

Sheep keratins: characterization of cDNA clones for the glycine + tyrosine-rich wool proteins using a synthetic probe.

cDNA clones coding for the high-glycine + tyrosine (HGT) proteins of sheep wool keratin have been isolated and sequenced. Clones were identified using a 25-base synthetic oligonucleotide probe, deduced from the amino acid sequence of a HGT protein present at about 0.4% in the wool fibre. Southern and Northern blot analysis suggest that the gene is present as a single copy in the genome and is transcribed as an mRNA species, 600 bases in size.

Animals↗
PubMed1987

Sheep wool (glycine + tyrosine)-rich keratin genes. A family of low sequence homology.

We report the isolation and complete nucleotide sequence of genes encoding the two major high-(glycine + tyrosine) (HGT) keratins of sheep wool in separate genomic clones. The genes have negligible sequence homology except for an 18-bp conserved element immediately preceding the initiation codon. The same element has been found in the corresponding position of a number of co-expressed high-sulphur (HS) keratin genes and may therefore represent a common element between these wool intermediate-filament-associated proteins. As seen for the HS keratin genes, the HGT keratin genes also lack introns. Southern blot data show that both HGT genes are unique in the sheep genome, indicating that the observed heterogeneity of the HGT protein class may not be as complex as previously suggested.

Animals↗
PubMedDate not supplied

Biodegradation of wool by Trichophyton simii and Aspergillus niger.

The amount of protein released into liquid culture medium and weight loss were taken as measures of wool degradation by Trichophyton simii and Aspergillus niger. Protein released into the culture medium was observed to be greater after T. simii treatment than after A. niger treatment. Sulphitolysis was shown by T. simii, whereas it was absent in the case of A. niger, pH was found to be alkaline with an increase in soluble protein in the culture medium in the case of both uniculture and dual culture. However, both the weight loss of wool and the amount of protein released were significantly reduced when both fungi were allowed to attack the substrate. The behaviour of these fungi in dual culture reflects their antagonistic activities.

Animals↗
PubMed1987

Itching from wool fibres in atopic dermatitis.

In 24 girls with atopic dermatitis and a history of irritation to wool, more intense itching was provoked on normal skin on the abdomen by a material with coarse wool fibres (36 microns) than with thinner fibres (20 microns). The probability of the materials causing itching could be predicted by the girls by handling the materials.

Adolescent↗
PubMed2006

Annual pattern of plasma melatonin and progesterone concentrations in hair and wool ewe lambs kept under natural photoperiod at lower latitudes in the southern hemisphere.

To study the annual pattern of plasma melatonin and progesterone concentrations in hair [Santa Inês (SI)] and wool [Romney Marsh (RM) and Suffolk (SU)] ewe lambs kept under natural photoperiods at 21 degrees 59'S, 12 ewe lambs (four/breed) were used. For melatonin, blood samples were collected monthly throughout the year at the onset (17:00, 19:00 and 21:00 hr) and end (04:00, 06:00 and 08:00 hr) of the night, and for progesterone the samples were collected in the morning, two to three times a week throughout the year. Plasma melatonin concentrations at different times of the day changed according to the season. In diurnal periods (17:00 and 8:00 hr) no seasonal differences were observed but they became evident in the nocturnal intervals (21:00 and 4:00 hr) and transitional night-day (6:00 hr) times. The patterns of melatonin secretion were higher in winter and autumn than in spring and summer. The patterns of plasma progesterone secretion were affected by interaction between breed and season. There was no seasonal variation in plasma progesterone concentrations for SI females. The progesterone pattern for RM and SU females varied with season. The plasma levels were higher in autumn and winter than in spring and summer. At 21 degrees 59'S hair and wool ewe lambs showed the same annual pattern of plasma melatonin concentration while the annual progesterone profiles were quite different. For SI females this pattern was constant along all seasons and for RM and SU females this pattern was higher during autumn and winter than spring and summer.

Animals↗
PubMed1966

Quantitative studies on fabrics as disseminators of viruses. I. Persistence of vaccinia virus on cotton and wool fabrics.

The persistence of vaccinia virus on wool (blanket and gabardine) and cotton (sheeting, terry cloth, and knit jersey) fabrics was studied. The fabrics were exposed to the virus by three methods: direct contact, aerosol, and virus-containing dust having a high content of textile fibers. Fabrics exposed to virus by each method were held in 35 and 78% relative humidities at 25 C. Virus was recovered for up to 14 weeks from wool fabrics exposed to virus and held in the low humidity. In contrast, virus persisted for shorter periods of time on the cotton fabrics. No virus was detected on terry cloth as early as 3 days after exposure to virus. The virus appeared to be less stable in the high humidity, and the method of exposure of the fabrics to virus apparently had an effect upon the persistence of the agent. On all fabrics, viral persistence was of sufficient duration to be of epidemiological significance.

Animals↗
PubMed1999

Isolation and partial characterisation of extracellular keratinase from a wool degrading thermophilic actinomycete strain Thermoactinomyces candidus.

The keratinase production by the thermophilic actinomycete strain Thermoactinomyces candidus was induced by sheep wool as the sole source of carbon and nitrogen in the cultivation medium. For complete digestion of wool by the above strain, both keratinolytic serine proteinase and cellular reduction of disulfide bonds were involved. Evidence was presented that substrate induction was a major regulatory mechanism and the keratinase biosynthesis was not completely repressed by addition of other carbon (glucose) and nitrogen (NH4C1) sources. The enzyme was purified 62-fold by diethylaminoethyl-anion exchange and Sephadex G-75 gel permeation chromatographies. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that the purified keratinase is a monomeric enzyme with a molecular mass of 30 kDa. The pH and temperature optima were determined to be 8.6 and 70 degrees C, respectively. The purified thermophilic keratinase catalyses the hydrolysis of a broad range of substrates and displays higher proteolytic activity against native keratins than other proteinases. Ca2+ was found to have a stabilizing effect on the enzyme activity at elevated temperatures.

Ammonium Chloride↗
PubMedDate not supplied

Effect of internal wool lipid liposomes on skin repair.

Intercellular lipids of the stratum corneum (SC) play a crucial role in keeping an optimal skin barrier function and in regulating the water-holding capacity. Recently, the internal lipids have been extracted from wool fibre. This lipid extract has a composition similar to that of the SC lipids. Two parameters were used to test the effect of topically applied internal wool lipids (IWL), structured as liposomes, on the water barrier functions of disturbed and intact skin: transepidermal water loss and skin capacitance. Liposomes made up of lipids that simulate the composition of the SC were also applied for comparison. The single application of the IWL liposomes on disturbed skin resulted in an accelerated recovery of water barrier functions. Daily application of these liposomes on intact skin for 5 days reinforced the skin barrier and increased the water-holding capacity. The repairing effect of the IWL enhances their suitability in the treatment, prevention and care of skin.

Adult↗