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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
Endocrinology. 1999 Mar;140(3):1219-27.
Growth hormone and dexamethasone stimulate lipolysis and activate adenylyl cyclase in rat adipocytes by selectively shifting Gi alpha2 to lower density membrane fractions.
Yip RG, Goodman HM.
Department of Physiology, University of Massachusetts Medical School, Worcester 01655, USA.
GH, in the presence of glucocorticoid, produces a delayed increase in lipolysis in rat adipose tissue, but the biochemical mechanisms that account for this action have not been established. Other lipolytic agents rapidly activate adenylyl cyclase (AC) and the resulting production of cAMP initiates a chain of reactions that culminates in the activation of hormone-sensitive lipase. We compared responses of segments of rat epididymal fat or isolated adipocytes to 30 ng/ml GH and 0.1 microg/ml dexamethasone (Dex) with 0.1 ng/ml isoproterenol (ISO), which evoked a similar increase in lipolysis. All measurements were made during the fourth hour after the addition of GH+Dex or immediately after the addition of ISO to cells or tissues that had been preincubated for 3 h without hormone. Although no significant increases in cAMP were discernible in homogenates of GH+Dex-treated tissues, Rp-cAMPS (Rp-adenosine 3'5'-phosphothioate), a competitive inhibitor of cAMP, was equally effective in decreasing lipolysis induced by GH+Dex or ISO. The proportion of PKA that was present in the active form was determined by measuring the incorporation of 32P from [gamma-32P]ATP into kemptide in the absence and presence of saturating amounts of cAMP. GH+Dex and ISO produced similar increases in protein kinase A activity in tissue extracts. Treatment with GH+Dex did not change the total forskolin-stimulated AC present in either a crude membrane pellet sedimented at 16K x g or a less dense membrane pellet sedimented at 100K x g, but doubled the AC activity in the 16K pellet when assayed in the absence of forskolin. To evaluate possible effects on G proteins, pellets obtained from centrifugation of adipocyte homogenates at 16K x g and 100K x g were solubilized and subjected to PAGE and Western analysis. GH+Dex decreased Gi alpha2 by 44% (P < 0.02) in the 16K pellets and increased it by 52% (P < 0.01) in the 100K pellets. Gs alpha in the 16K pellet was unaffected by GH+Dex and was decreased (P < 0.05) in the 100K pellet. Sucrose density fractionation of the 16K pellets revealed a similar GH+Dex-dependent shift of Gi alpha2 to less dense fractions as determined by both Western analysis and [32P]NAD ribosylation catalyzed by pertussis toxin. No such changes were seen in the distribution of Gs alpha or 5'-nucleotidase. Colchicine (100 microM) blocked the GH+Dex-dependent shift of Gi alpha2 from the 16K to the 100K pellet and blocked the lipolytic effects of GH+Dex, but not those of ISO. We conclude that by modifying the relationship between AC and Gi alpha2, GH+Dex relieves some inhibition of cAMP production and consequently increases lipolysis.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10067847&dopt=Abstract
Gen Comp Endocrinol. 1999 Mar;113(3):360-8.
Cloning, in vitro expression, and novel phylogenetic classification of a channel catfish estrogen receptor.
Xia Z, Patino R, Gale WL, Maule AG, Densmore LD.
Department of Biological Sciences, Texas Tech University, Lubbock, Texas, 79409, USA.
We obtained two channel catfish estrogen receptor (ccER) cDNA from liver of female fish using RT-PCR. The two fragments were identical in sequence except that the smaller one had an out-of-frame deletion in the E domain, suggesting the existence of ccER splice variants. The larger fragment was used to screen a cDNA library from liver of a prepubescent female. A cDNA was obtained that encoded a 581-amino-acid ER with a deduced molecular weight of 63.8 kDa. Extracts of COS-7 cells transfected with ccER cDNA bound estrogen with high affinity (Kd = 4.7 nM) and specificity. Maximum parsimony and Neighbor Joining analyses were used to generate a phylogenetic classification of ccER on the basis of 18 full-length ER sequences. The tree suggested the existence of two major ER branches. One branch contained two clearly divergent clades which included all piscine ER (except Japanese eel ER) and all tetrapod ERalpha, respectively. The second major branch contained the eel ER and the mammalian ERbeta. The high degree of divergence between the eel ER and mammalian ERbeta suggested that they also represent distinct piscine and tetrapod ER. These data suggest that ERalpha and ERbeta are present throughout vertebrates and that these two major ER types evolved by duplication of an ancestral ER gene. Sequence alignments with other members of the nuclear hormone receptor superfamily indicated the presence of 8 amino acids in the E domain that align exclusively among ER. Four of these amino acids have not received prior research attention and their function is unknown. The novel finding of putative ER splice variants in a nonmammalian vertebrate and the novel phylogenetic classification of ER offer new perspectives in understanding the diversification and function of ER. 1999 Academic Press.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10068497&dopt=Abstract
Gen Comp Endocrinol. 1999 Mar;113(3):369-73.
Fish calcitonin genes: primitive bony fish genes have been conserved in some lower vertebrates.
Suzuki N, Ueda K, Sakamoto H, Sasayama Y.
Noto Marine Laboratory, Faculty of Science, Kanazawa University, Ishikawa, 927-0553, USA.
Using the polymerase chain reaction method, we amplified calcitonin genes from the cDNA of the ultimobranchial glands or from the genomic DNA of the blood cells and liver of various fishes. The fishes examined were primitive bony fishes (lungfish, polypterus, sturgeon, and gar), 16 species of teleosts, and cartilaginous fishes (stingray). Sequenced calcitonin genes were compared among fishes and with those of reptiles and chickens. The similarity of the calcitonin genes was the highest between the reptile and chicken groups and the primitive bony fishes (sequence similarity of the nucleotides 81-90%). The values between teleosts and the primitive bony fishes were 70-81%, with the exception of eels. Eel calcitonin genes were very similar to those of primitive bony fishes (83-88%). Stingray calcitonin genes were relatively more similar to those of the primitive bony fishes (74-78%) than to teleosts (63-73%). In goldfish and sardine, two types of calcitonin genes were found. We concluded that the genes of primitive bony fish are placed at a fundamental position in this hormone, at least among these vertebrates. 1999 Academic Press.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10068498&dopt=Abstract
Anim Genet. 1999 Feb;30(1):60-2.
Mapping four genes from human chromosome 4 to porcine chromosome 8 further develops the comparative map for an economically important chromosome of the swine genome.
Rohrer GA.
US Department of Agriculture, US Meat Animal Research Center, Clay Center, NE 68933-0166, USA.
Because porcine chromosome (SSC) 8 has become the focal point of many efforts aimed at identifying quantitative trait loci affecting ovulation rate, genes distributed across human chromosome (HSA) 4 were physically mapped in the pig. A more refined comparative map of this region for these two species was produced. In this study, four genes were selected based on their location in the human genome, the availability of nucleotide sequence and their genomic organization. The genes selected were fibroblast growth factor basic (FGF2; HSA 4q25-27), gonadotropin releasing hormone receptor (GNRHR; HSA 4q13), phosphodiesterase 6 B (PDE6B; HSA 4p16.3) and aminopeptidase S (PEPS; HSA 4p11-q12). Genomic libraries were screened via PCR and clones were physically assigned using fluorescence in situ hybridization (FISH). These four genes from HSA 4 were physically mapped to SSC 8p2.3 (PDE6B), 8p1.1 (PEPS), 8q1.1-1.2 (GNRHR) and 8q2.2-2.4 (FGF2). These assignments provide additional benchmarks for the comparative map and help define the level of gene order conserved between HSA 4 and SSC 8.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10050287&dopt=Abstract
Brain Res. 1999 Mar 13;821(2):309-21.
Sex differentiation of growth hormone-releasing hormone and somatostatin neurons in the mouse hypothalamus: an immunohistochemical and morphological study.
Nurhidayat, Tsukamoto Y, Sigit K, Sasaki F.
Department of Veterinary Anatomy, Osaka Prefecture University, Gakuen-cho 1-1, Sakai, Osaka 599-8531, Japan.
We examine sexual dimorphism in growth hormone-releasing hormone (GHRH) in the arcuate nucleus (ARC), and somatostatin (SS) in the periventricular nucleus (PeN) of the hypothalamus, and investigate when it becomes evident. Using immunohistochemical staining and morphometry, we observed ARC GHRH-immunoreactive (ir) neurons, ARC SS-ir neurons and PeN SS-ir neurons in male and female mice at 5, 20, 30, 40 and 60 days old. The number of ARC GHRH-ir neurons was significantly higher in males than females, after 20 days old. ARC SS-ir neurons showed no significant differences between sexes. On the other hand, PeN SS-ir neurons were significantly more numerous in males at 30, 40 and 60 days than in females. During postnatal development, these GHRH- and SS-ir neurons changed in different patterns from ages 20 to 60 days. The number of ARC GHRH-ir neurons in both sexes decreased from 5 to 20 days, increased until day 40, and then decreased at day 60, while ARC SS-ir neurons in both sexes increased from day 5 to day 60. PeN SS-ir neurons in both sexes increased from days 5 to 20 to 116% in males and 189% in females. Furthermore, in male mice, the increase continued until 40 days of age, while in females, there was no significant difference from days 20 to 60. There were no apoptotic cells; a few proliferating cell nuclear antigen (PCNA) stained cells were found in the ARC and PeN. Our results suggest that the sex difference of ARC GHRH neurons and PeN SS neurons appears by stimulation with testosterone during the development life. The developmental fluctuation in the number of ARC GHRH-ir neurons may not be modulated by testosterone, but by ARC SS neurons. 1999 Elsevier Science B.V.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10064817&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.
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Constipation relief, laxative, colon cleansing ||
Lutein ||
Progesterone Cream ||
Natural herbal formula for hair loss problems ||