DreamPharm Products:
Lutein-20||Herbs for headache, fever, and migraine ||
Milk thistle||Saw palmetto||
Triple B Super Vision||Garlic, Ginger, and Grapeseed Extract||
Ginseng and Ginkgo||Hair Million||
DHEA||Coenzyme Q10||
Sleep Aid herbal formula - natural sleep aid||Herbal Breath - herbs for bad breath problems.||
Weight loss herbal formula for menopause and pms||Ginkgo biloba||
Colon cleansing, Laxative||ViaVita, Lecithin for healthy liver
Fatty acids resources:
Pathogen research abs 1 || Pathogen research abs 2 || Pathogen research abs 3 || Pathogen research abs 4 || Pathogen research abs 5 ||
Hormone and endocrine research abs 1 || Hormone and endocrine research abs 2 || Hormone and endocrine research abs 3 || Hormone and endocrine research abs 4 || Hormone and endocrine research abs 5
J Histochem Cytochem. 1979 Apr;27(4):867-72.
Immunocytochemistry with osmium-fixed tissue. I. Light microscopic localization of growth hormone and prolactin with the unlabeled antibody-enzyme method.
Baskin DG, Erlandsen SL, Parsons JA.
Growth hormone and prolactin were localized on thin plastic sections of rat anterior pituitary gland and mammosomatotropic tumor MtTW15 that were fixed with osmium tetroxide (alone,mixed with aldehydes, or after aldehydes). Intense immunocytochemical staining for both antigens was obtained after plastic was removed from sections with an alcoholic solution of sodium hydroxide. The results indicated that antigenic determinants of rat prolactin and growth hormone were not completely destroyed or inactivated by fixation with osmium and embedment in epoxy resin, and that removal of the polymerized epoxy resin was necessary to obtain light microscopic postembedding immunocytochemical staining of these antigens. The results also demonstrated that tissues which have been conventionally processed for morphological evaluation by electron microscopy may be suitable for postembedding immunocytochemical staining of some antigens for light microscopy.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=109497&dopt=Abstract
J Nutr. 1979 Jul;109(7):1321-32.
Characteristics of thyroid function in experimental protein malnutrition.
Tulp OL, Krupp PP, Danforth E Jr, Horton ES.
Two experiments were conducted to study the effects of protein malnutrition on thyroid function. Resting oxygen consumption and serum concentrations of triiodothyronine (T3), thyroxine (T4) and thyroid stimulating hormone (TSH) were measured and correlated with thyroid histology, gain in weight, feed efficiency and carcass energy content in male rats fed isoenergetic diets ad libitum containing 22% (control) or 8% (protein malnourished, PM) casein for 28 or 32 days postweaning. A third group was pair-fed to the PM rats with the control diet. In experiment 2 additional groups were pair-fed to the PM rats with 8% casein diets in which the casein was substituted with different mixtures of carbohydrate and fat. Resting oxygen consumption/body weight (0.75) decreased as body weights increased in all groups, but was consistently greatest in PM rats. In PM rats, plasma T3 was 130% of controls after 11 days of the dietary regimen and averaged 215% of controls from days 18 through 32. In experiment 2 both T3 and T4 concentrations were approximately twice controls in all PM groups. TSH concentrations were within the normal range in all groups throughout. Feed efficiency averaged 36 to 40% of controls and mean weight gain was 30 g after 28 days in the PM groups, compared to 114 and 91 g, respectively, in the pair-fed control rats. Carcass energy content of PM rats after 28 days was significantly lower than in control or pair-fed control rats. Thyroid morphology was compatible with increased secretory activity in all the protein-malnourished groups, compared with normal activity in the control and pair-fed control groups. Thermogenesis, as measured by oxygen consumption, was markedly increased in the PM rats compared to controls. These observations are consistent with a diet-induced thermogenesis in the protein-malnourished rats. In contrast to simple under-nutrition where energy expenditure may be conserved by decreases in thyroid function and thermogenesis, increases in thyroid function and thermogenesis in protein malnutrition could provide an energy balancing mechanism whereby unneeded non-protein energy in the diet could be dissipated as heat, and survival enhanced.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=109585&dopt=Abstract
J Pediatr. 1979 Aug;95(2):210-3.
Impaired parathyroid response to induced hypocalcemia in thalassemia major.
Gertner JM, Broadus AE, Anast CS, Grey M, Pearson H, Genel M.
Ethylene diamine tetra-acetic acid-induced hypocalcemia was used as provocative test of parathyroid reserve in eight normocalcemic patients with thalassemia major (age 8 to 26 years) and five young adult control subjects (age 22 to 35). In response to an intravenous infusion of disodium EDTA (50 mg/kg), serum immunoreactive parathyroid hormone rose by 1.97 +/- 1.93 (SD) microliterEq/ml in the patients, controls showing a rise of 10.6 +/- 3.6 microliterEq/ml (t = 5.46, P less than 0.001). There was no relationship between parathyroid response and total iron burden as measured by serum ferritin- or desferrioxamine-induced urinary iron excretion. Impairment of parathyroid reserve is common in transfused patients with thalassemia major and may serve as a marker of significant iron overload.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=109597&dopt=Abstract
Mol Cell Endocrinol. 2003 Mar 28;201(1-2):123-31.
Point mutations in follitropin receptor result in ER retention.
Nechamen CA, Dias JA.
Wadsworth Center, David Axelrod Institute for Public Health, New York State Department of Health, 120 New Scotland Avenue, 12208, Albany, NY, USA
Accumulating evidence suggests that the human follitropin receptor is unusually sensitive to mutation. Previous results (Mol. Cell. Endo. 166 (2000) 101) determined that scanning mutations in a.a. 12-14 and 22-30 neither bound follitropin nor were present on the cell surface, suggesting that these regions are involved in either hormone binding or trafficking. To distinguish between these hypotheses, single alanine substitutions in a.a. 12-14 and 22-30 were generated, all of which appeared to bind 125I-follitropin with an affinity constant similar to wild type (wt) follitropin receptor. However, the level of receptor on the cell surface varied widely, in some cases 100-fold lower than wt. Expression on the cell surface corresponded to expression of the mature 80 kD follitropin receptor. An accumulation of the ER-resident 62 kD band of follitropin receptor was observed in mutants that had low surface expression of receptor, suggesting that misfolded protein was trapped in the ER by a quality control mechanism.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12706300&dopt=Abstract [PubMed - in process]
Am J Cardiol. 1979 Jul;44(1):9-12.
Occult thyrotoxicosis: a correctable cause of "idiopathic" atrial fibrillation.
Forfar JC, Miller HC, Toft AD.
Serum total thyroxine, triiodothyronine and thyrotropin response to thyrotropin-releasing hormone were measured in 75 consecutive patients presenting to a cardiology clinic with atrial fibrillation with no obvious cardiovascular cause. A lack of response of serum thyrotropin to thyrotropin-releasing hormone, indicative of thyrotoxicosis, was found in 10 patients (13 percent), not all whom had raised serum thyroid hormone levels. These 10 patients were predominantly male, had no clinical signs of thyrotoxicosis and a relative excess of nonpalpable autonomous thyroid nodules demonstrated with scintigraphy. Eight of the 10 patients had reversion to stable sinus rhythm after treatment with iodine-131 or carbimazole, either spontaneously or after direct current cardioversion. It would appear that clinically occult thyrotoxicosis can be identified consistently only with the thyrotropin-releasing hormone test and is the cause of "idiopathic" atrial fibrillation in a significant proportion of patients.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=110126&dopt=Abstract
Like developmental biology of any part of our body, hair growth is a complicated process. Hence the homework for
modern science to yet unravel the process and mechanism to a completion. There exist a number of traditional and alternative therapeutic methods that include drugs, surgery, suppelements, and even snake oils that have been developed and used for those who lose hair.
No understanding, and there is no solution. Of course, none of these approaches are perfect for all hair loss problems, especially due to the heterogeneity of the causes underlying hair losses. Most of chemical drugs and hair transplantation surgeries are accompanied by undesirable side effects.
DHEA is a natural hormone, and it is produced in our body by the adrenal glands.
DHEA has been suggested to provide numerous potential benefits. DHEA (or dehydroepiandrosterone) is converted into androgens (male hormones)
or estrogens (female hormones) in the cells.
Our bodies produce decreasing amount of DHEA as we get older.
various health benefits: To deter aging,
improve sexual function/erectile dysfunction, treat cognitive decline, enhance athletic performance,
facilitate weight loss, improve strength, prevent osteoporosis, enhance immunomodulation for rheumatic conditions,
and treat depression.
DreamPharm Online Healthy Supplements ||
Constipation relief, laxative, colon cleansing ||
Lutein ||
Progesterone Cream ||
Natural herbal formula for hair loss problems ||