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Interferon research abs 1 || Hemoglobin research abs || Stem cell research abs || Nucleic acid research abs || Herpes research abs || Bronchitis research abs || Schizophrenia research abs || Tuberculosis research abs || Pneumonia research abs || Constipation research abs || Laxative research abs || hair research abs || hair related research references

J Biomech. 2001 Mar;34(3):319-25.
The failure behavior of the anchorage of hairs during slow extraction.

Roersma ME, Douven LF, Lefki K, Oomens CW.

Eindhoven University of Technology, Faculty of Mechanical Engineering, Section Materials Technology, P.O. box 513, 5600 MB Eindhoven, Netherlands. michiel.roersmhilips.com

Treatment of excessive hair growth is an important issue in both dermatological and cosmetic practice. In contrast to treatments with medication, most physical methods are treatments that focus on the hair follicle. To obtain insight in the failure behavior of the anchorage of hairs, hairs were extracted (in vitro) from pig skin at a speed of 0.1mm/s, one at a time. The pulling force and tweezers displacement were recorded. The extracted hairs were classified with respect to the phase in the growing cycle: anagen (growing phase), telogen (resting phase) or other (catagen phase or unable to determine). The anagen hairs showed a different relation between the tweezers displacement and the pulling force than the telogen hairs. Moreover, the maximum force that could be applied before a hair was extracted proved to be lower for anagen hairs than for telogen hairs (0.36N, 1.8N, respectively). The extracted hair length, defined as the part of the hair that had been embedded in the skin which was extracted, was higher for anagen hairs than for telogen hairs (4.8mm, 3.0mm, respectively). Removing proximal skin tissue and the embedded parts of the anagen hair (root) resulted in a change of the extraction curves. The results indicate that two phenomena play a role in the anchorage of anagen hairs. We have proposed a model for the extraction of an anagen hair that has been based on these results: first the interface between hair and skin that is located around the inner root sheath (IRS) starts to fail, followed by failing of the hair itself in the region where the hair keratinizes.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11182122&dopt=Abstract

Peptides. 2002 Oct;23(10):1759-63.
In vitro release of digestive enzymes by FMRF amide related neuropeptides and analogues in the lepidopteran insect Opisina arenosella (Walk.).

Harshini S, Nachman RJ, Sreekumar S.

Department of Zoology, University College, Trivandrum 695 034, Kerala, India.

The insect neuropeptides FMRF amide, leucomyosupressin (LMS) and neuropeptide analogues leucosulfakinins (FLSK and LSK II Ser (SO(3)H)), perisulfakinin (PSK), proleucosulfakinin (PLSK), 14A[phi1]WP-I, 542phi1, and 378A[5b]WP-I were assayed for their effects on the release of amylase and protease from the midgut tissue of larvae of Opisina arenosella. In the bioassay, empty midgut tubes ligated at both ends using hair were incubated with insect saline containing neuropeptides/analogues in a bioassay apparatus at 37 degrees C for 30 min. After incubation the contents of the midgut preparations were analyzed for amylase and protease activity. In control experiments, the midgut preparations were incubated in insect saline without neuropeptides. The results of the study reveal that for stimulating amylase release from midgut tissue, the peptides require an FXRF amide (X may be methionine or leucine) sequence at the C-terminal. The presence of HMRF amide at C-terminal of peptides may inhibit the release of amylase. Meanwhile, peptides with both FMRF and HMRF amide sequence at the C-terminal are found to be effective in stimulating protease release. The tetrapeptide segment at the C-terminal probably represent the active core of the neuropeptide.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12383863&dopt=Abstract

Gene. 2000 Oct 3;256(1-2):19-27.
Kdap, a novel gene associated with the stratification of the epithelium.

Oomizu S, Sahuc F, Asahina K, Inamatsu M, Matsuzaki T, Sasaki M, Obara M, Yoshizato K.

Tissue Regeneration Project, Hiroshima Prefecture Joint-Research Project for Regional Intensive, Japan Science and Technology Corporation, Institute of Industrial Science and Technology, 3-10-32, Kagamiyama, Higashihiroshima, Japan.

The skin develops and differentiates during embryogenesis, which is concertedly regulated by a variety of genes. The present study isolated from the rat embryonic skin a novel differentiation-associated gene named Kdap (keratinocyte differentiation-associated protein) by suppression subtractive hybridization between the skin of 14day postcoitus (dpc) embryo (the prehair-germ stage) and that of 17dpc embryo (the hair-germ stage). Its mRNA contained four spliced forms in these tissues. The gene encoded a protein of total 98 amino acids with a calculated molecular mass of 11kDa and an isoelectric point of 6.1 as an unspliced form. The two splicing zones were well conserved among rat, mouse, and human. This protein had a high hydrophobic N-terminal region, a possible signal sequence, and contained two putative N-myristoylation sites and two casein kinase II phosphorylation sites. In situ hybridization experiments detected Kdap transcripts exclusively in the suprabasal cell layers of the embryonic epidermis. Intense expression was also seen in suprabasal cells in regions of infundibulum of the hair follicle. These results indicated that Kdap provides a new insight into the mechanism of differentiation and the maintenance of stratified epithelia.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11054531&dopt=Abstract

Semin Cell Dev Biol. 1997 Jun;8(3):265-275.
Developmental changes in the physiology of hair cells.

Eatock RA, Rusch A.

Department of Otolaryngology, Baylor College of Medicine, Houston, TX, 77030, USA

Mature hair cells express complements of ion channels which vary with hair cell type. Immature hair cells in the inner ears of neonatal mice and pre-hatch chicks share mechanosensitive and certain voltage-gated conductances: delayed rectifier and inwardly rectifying potassium conductances, voltage-gated calcium and sodium conductances. Over the course of several days the immature cells acquire other conductances that confer upon them the distinctive voltage-dependent properties of mature hair cells. In the mouse utricle, postnatal acquisition of additional delayed and inward rectifiers transforms the neonatal hair cells into two classes with the electrophysiological profiles of mature type I and type hair II cells. Electromotility, a highly differentiated, voltage-dependent property of mature outer hair cells from the mammalian cochlea, is also acquired after mechanosensitivity.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10024489&dopt=Abstract [PubMed - as supplied by publisher]

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