Fibroblasts play a stimulatory role in keratinocyte proliferation but an inhibitory role in melanocyte growth and pigmentation in a skin equivalent system from skin type 4 D Lee, 1, 2 J Lee, 1 E Lee, 1 K Cho3 and J Yang1, 2 1 Department of Dermatology, Sungkyunkwan University School of Medicine Samsung Medical Center, Seoul, South Korea, 2 Samsung Biomedical Research Institute, Seoul, South Korea and 3 Dermatology, Seoul National University College of Medicine, Seoul, South Korea There have been conflicting results regarding the influence of fibroblasts on melanocytes. In this study we investigated the effects of fibroblasts on the number of melanocytes and melanin pigemntation in a skin equivalent model derived from skin type 4. In addition, the effect of fibroblasts on the proliferation of melanocytes in monolayer culture was evaluated using the MTT assay. The skin color in the skin equivalent with fibroblasts SEF ; was much lighter macroscopically than in the skin equivalent without fibroblast SENF ; . Histologically, both the SEF and the SENF produced a multilayered epidermis with a compact horny layer. Less melanin, however, was found in the SEF than in the SENF. Immunohistochemical staining with a melanocyte-specific antibody MEL-5 ; revealed that the number of melanocytes in the SEF was much smaller than in the SENF. However, in the SEF, the number of Ki-67-positive keratinocytes was increased compared to the number in the SENF. In the monolayer culture, absorbance in the MTT assay by melanocytes with fibroblast conditioned medium was significantly increased compared with that of melanocytes in control culture, suggesting that some types of fibroblast-derived factors may have positive effects on the growth of melanocytes in monolayer systems. Our results show that in a skin equivalent, fibroblasts stimulate proliferation of keratinocytes while reducing the number of melanocytes and suppressing melanin pigmentation, and that in monolayer culture, fibroblasts at least do not suppress melanocyte growth directly.
Maria C Freire is President and Chief Executive Officer of the Global Alliance for TB Drug Development TB Alliance and Chair of the Working Group on New TB Drugs ; . From 1995 to 2001, she directed the Office of Technology Transfer at the United States National Institutes of Health NIH ; . Prior to joining the NIH, Dr Freire established and headed the Office of Technology Development at the University of Maryland at Baltimore and the University of Maryland, Baltimore County. An internationally recognized expert in technology commercialization, Dr Freire was appointed in February 2004 as a Commissioner of the World Health Organization's newly formed Commission on Intellectual Property Rights, Innovation and Public Health CIPIH ; . She has written and spoken extensively about science in the public interest and how society's most advanced technologies can be leveraged for global health priorities, for example, coumadin patient education.
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With an undetermined risk B1 and B2 ; , potentially harmful drugs B3, C, D, and X ; and drugs that were not included in the classification. For the 35 drug groups that were most widely used by non-pregnant women, the proportion of prescriptions for safe, undetermined, potentially harmful and unclassified drugs was determined both for non-pregnant women.
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Subjects. The Statement of Principle of Pharmaceutical Research in Paediatric Subjects was adopted by BPS at its Barcelona meeting and is currently under review by the FIP Public Policy Committee. The other two Statements of Principle are under review of the BPS members. BIO-International 1999 Under the leadership of Dr K. Midha and the conference co-chairs Dr L. Z. Benet, Dr H. Blume, Dr A. C. Moffat, Dr Y Sugiyama and Dr R. Williams, BIO International 1999 was held from 29 September to 1 October 1999 in London, UK. It was attended by more than 170 participants. Millennial World Congress 2000 Under the leadership of Dr L. Benet, Chairman of BPS, meetings of the Millennial World Congress Organising Committee were organised in New York and New Orleans to make the major event for pharmaceutical sciences in 2000 in San Francisco happen. The deadline for abstract submission was 1 December 1999 and about 800 research abstracts together with about 200 abstracts of the symposia speakers were received. Major sponsorship from USA and Japan was received as well!
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10. Kwong K, Lee LY. Prostaglandin E2 sensitizes cultures pulmonary vagal chemosensitive neuron to chemical and electrical stimuli. J Appl Physiol 2002; 93: 1419-1428. Missale C, Nash SR, Robinson SW, Jaber M, Caron MG. Dopamine receptors: from structure to function. Physiol Rev 1998; 78: 189-225. Momiyama T, Todo N, Sasa M. A mechanism underlying dopamine D1 and D2 receptor-mediated inhibition of dopaminergic neurones in the ventral tegmental area in vitro. Br J Pharmacol 1993; 109: 933-940. Bisgard GE, Mitchell RA, Herbert DA. Effects of dopamine, norepinephrine and 5hydroxytryptamine on the carotid body of the dog. Respir Physiol 1979; 37: 61-80. Jackson DM, Simpson WT. The effect of dopamine on the rapidly adapting receptors in the dog lung. Pulm Pharmacol Ther 2000; 13: 39-42. Lawrence AJ, Krstew E, Jarrott B. Functional dopamine D2 receptors on rat vagal afferent neurones. Br J Pharmacol 1995; 114: 1329-1134. Peiser C, Fischer A. Expression of dopamine receptors in sensory neurones of the rat. J Respir Crit Care Med 2001; 163: A905. 17. Lin YS, Gu Q, Lee LY. Activation of dopamine D2 receptor attenuates hyperresponsiveness of pulmonary C fibers induced by prostaglandin E2 in rats. FASEB J 2001; 15: A797. 18. Lin YS, Lee LY. Stimulation of pulmonary vagal C-fibres by anandamide in anaesthetized rats: role of vanilloid type 1 receptors. J Physiol 2002; 539: 947-955 and diovan.
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Androgen-free AR. Thus, androgen binding either reduces phosphatase targeting to AR or induces an AR conformation that protects Ser81 and Ser308 from dephosphorylation. Phosphorylation of Ser256 is strongly dependent on the LBD for reasons related either to phospho-site conformation or kinase targeting to AR or simply because Ser256 in LBD AR is dephosphorylated more efficiently than it is phosphorylated. DISCUSSION Androgen binding regulates multiple aspects of AR function, including subcellular localization, interactions with transcriptional regulators, and protein degradation 10, 28, 36, ; . Ligand binding regulates these activities by altering AR conformation, chaperone composition, and protein interactions 20 ; . In the current study we have analyzed several aspects of AR structure and activity that are linked to androgen-dependent conformational changes. The entree for these studies was our recent finding that the phosphatase PP2A recognizes the agonist conformation of AR 48 ; , interaction that we have characterized in the present study. Mechanism of PP2A binding to AR. The PP2A core enzyme is a heterodimer that contains a catalytic C subunit and a structural A subunit. In previous work we showed that the A subunit of PP2A contacts AR, and we presented data suggesting that ST-induced conformational changes in the A subunit are critical for PP2A A C heterodimer to bind the androgenbound form of AR 48 ; binds directly to the A subunit 34 ; , and we found that ST binding to the A subunit in vitro alters the protease sensitivity of sites both within and outside of the ST interaction site 48 ; . Work from other laboratories had mapped the ST binding site to HEAT repeats 3 to 6 the N-terminal region of the A subunit 34 ; . We found that deletion of HEAT repeats 3 to 5 abrogated ST-induced PP2A binding to AR Fig. 1 ; , suggesting that HEAT repeats 3 to 5 the interface between HEAT repeats 3 and 5 ; are critical elements of the ST binding site Fig. 10A ; . Our deletion analysis also revealed that removal of HEAT repeats 13 to 15 the C-terminal region of the A subunit eliminates PP2A binding to AR. Moreover, we determined that deletion of HEAT repeat 13 is sufficient to disrupt PP2A A-subunit binding to AR. Together, these results indicate that ST binding to N-terminal HEAT repeats elicits a conformational change in the C-terminal HEAT repeats that creates binding site for AR. The PP2A C subunit also binds to C-terminal HEAT repeats in the A subunit; its binding site overlaps, but is nonidentical to, the binding site for AR. This conclusion is based on two observations. First, we can isolate an AR complex that contains both the A subunit and the C subunit of PP2A, and the levels of the three polypeptides are approximately stoichiometric 48 ; . Second, deletion of HEAT repeats 14 to 15 from the A subunit causes the loss of C-subunit binding without affecting AR binding. Removing HEAT repeat 13 from the A subunit, however, resulted in loss of both AR and C-subunit binding. Recent crystal structures of PP2A show that several residues within HEAT repeat 13 of the A subunit are important for the interface with the C subunit 5, 46 ; . The PP2A A subunit binds stably to a site that includes the LBD of AR, thereby functioning as a targeting subunit for the PP2A C subunit. The ability of the PP2A C subunit to dephosphorylate five phospho-sites.
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