References: Hair growth and hair loss
J Anim Sci. 1998 Feb;76(2):513-21.
Essential and nonessential amino acid composition of pigs from birth to 145 kilograms of body weight, and comparison to other studies.
Mahan DC, Shields RG Jr.
Animal Sciences Department, The Ohio State University, and The Ohio Agricultural Research and Development Center, Columbus 43210-1095, USA.
The amino acid composition of the body components (carcass, hair, whole blood, and a composite of the other body tissues) were determined from a total of 81 crossbred pigs at 10 weight intervals from birth to 145 kg body weight. Body component amino acid compositions (g/100 g protein) were multiplied by their respective protein contents, resulting in calculated whole-body amino acid compositions. From 8.5 to 145 kg body weight, the amino acid compositions were similar within each body component but differed between body components. There was a higher concentration of carcass lysine, arginine, and histidine (P < .01) in the carcass, and isoleucine (P < .12), threonine (P < .15), and methionine (P < .08) tended to be higher than in the composite of the other body tissue. Whole blood was, however, higher in leucine, valine, and lysine, and hair was higher in cystine than the carcass. The relative concentration of lysine in the whole body increased to about 37 kg body weight and reached a plateau, whereas the other essential amino acids increased to 8.5 kg and then reached a plateau. Tryptophan, however, decreased from birth to 8.5 kg and then remained at a similar concentration to 145 kg body weight. Whole-body amino acid composition of pigs in our study was generally similar to that noted in other scientific reports, but there was a wide variation in amino acid values between studies.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=9498360&dopt=Abstract
J Burn Care Rehabil. 1998 Jan-Feb;19(1 Pt 1):10-7.
Cutaneous nerve distribution in adult rat hairy skin after thermal injury--an immunohistochemical study.
Ward RS, Tuckett RP, English KB, Johansson O.
Division of Physical Therapy, University of Utah School of Medicine, Salt Lake City, USA.
Regrowth of cutaneous nerves after thermal injury was examined in rat hairy skin with use of protein gene product 9.5, which has been shown to label nerves in skin preparations. Tissue biopsies were obtained from injured and control skin at postburn days 1, 7, 14, 28, and 120, fixed in 4% paraformaldehyde, cryoprotected, sectioned, and immunostained with rhodamine conjugated goat anti-rabbit immunoglobulin G. Immunoreactivity for protein gene product 9.5 was intense and illustrated the process of nerve regrowth in rat skin after thermal injury. No nerve growth was detectable in 1- and 7-day preparations. Variable regeneration was noted in 14-day preparations. The 28- and 120-day groups produced nerve counts that were similar to control sections. Results suggest that rat hairy skin has a capacity for nerve regrowth after thermal injury. Nerves were noted to regenerate from beneath the scar. Burn wounds in rats demonstrated vigorous cutaneous nerve regeneration.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=9502018&dopt=Abstract
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Pelage growth cycles are regulated by circulating prolactin in many mammals, but the intercellular mediators of this signaling are unknown. Binding sites for insulin-like growth factors (IGFs) were examined in sheep skin to show changes in distribution and abundance of IGF receptors associated with a prolactin stimulus and the subsequent hair follicle growth cycle. Follicle cycles were induced in New Zealand Wiltshire ewes by a surge in plasma prolactin following a 4-month period of prolactin suppression with bromocriptine. Eight treated and three control sheep were slaughtered at intervals over 43 days during the follicle growth cycle. At 12-20 days after the elevation of prolactin, wool follicles passed through brief catagen and telogen phases, followed by a return to anagen. IGF binding sites were localized in skin sections by incubation with 125I-IGF-I or 125I-IGF-II. Displacement with competitive binding inhibitors (unlabeled IGF-I, IGF-II, des(1-3)IGF-I, des(1-6)IGF-II, or insulin) and affinity cross-linking showed that these binding sites were predominantly IGF type 1 and type 2 (mannose-6-phosphate) receptors. The radioligands bound especially to follicle germinal cells and prekeratinocytes. Increases in specific binding of both radioligands were observed after the rise in prolactin, but prior to anatomical changes in follicles associated with cessation of growth. For IGF-I, highest binding density was observed during catagen in the germinal matrix and dermal papilla cells. For IGF-II, peak density occurred during late anagen/early catagen in the germinal matrix and during telogen in the dermal papilla. These cycle associated changes in receptor availability suggest that IGF receptors are involved in control of the wool growth.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=9505430&dopt=Abstract
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