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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 || testosterone related research references || melanin related research references

Mol Cell Biol. 2003 Aug;23(15):5245-55.
The actin-binding domain of Slac2-a/melanophilin is required for melanosome distribution in melanocytes.

Kuroda TS, Ariga H, Fukuda M.

Fukuda Initiative Research Unit, RIKEN (The Institute of Physical and Chemical Research), 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.

Melanosomes containing melanin pigments are transported from the cell body of melanocytes to the tips of their dendrites by a combination of microtubule- and actin-dependent machinery. Three proteins, Rab27A, myosin Va, and Slac2-a/melanophilin (a linker protein between Rab27A and myosin Va), are known to be essential for proper actin-based melanosome transport in melanocytes. Although Slac2-a directly interacts with Rab27A and myosin Va via its N-terminal region (amino acids 1 to 146) and the middle region (amino acids 241 to 405), respectively, the functional importance of the putative actin-binding domain of the Slac2-a C terminus (amino acids 401 to 590) in melanosome transport has never been elucidated. In this study we showed that formation of a tripartite protein complex between Rab27A, Slac2-a, and myosin Va alone is insufficient for peripheral distribution of melanosomes in melanocytes and that the C-terminal actin-binding domain of Slac2-a is also required for proper melanosome transport. When a Slac2-a deletion mutant (DeltaABD) or point mutant (KA) that lacks actin-binding ability was expressed in melanocytes, the Slac2-a mutants induced melanosome accumulation in the perinuclear region, possibly by a dominant negative effect, the same as the Rab27A-binding-defective mutant of Slac2-a or the myosin Va-binding-defective mutant. Our findings indicate that Slac2-a organizes actin-based melanosome transport in cooperation with Rab27A, myosin Va, and actin.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12861011&dopt=Abstract

Endocrinology. 2003 Aug;144(8):3514-23.
Melanin-concentrating hormone receptor 1 activates extracellular signal-regulated kinase and synergizes with G(s)-coupled pathways.

Pissios P, Trombly DJ, Tzameli I, Maratos-Flier E.

Section on Obesity, Research Division, Joslin Diabetes Center, Beth Israel-Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts 02215, USA.

Melanin-concentrating hormone (MCH) is a hypothalamic neuropeptide that plays a key role in energy homeostasis. Like many neuropeptides, it signals through two G protein-coupled receptors. MCH receptor 1 (MCHR1) is the sole receptor expressed in rodents and couples to G(i) and G(q) proteins. Little is known about the intracellular pathways engaged by MCH and its receptor. Using HEK293 cells stably expressing MCHR1, we demonstrate that MCH, acting through MCHR1, antagonizes the action of forskolin, an adenylate cyclase activator that increases intracellular levels of cAMP. MCH also inhibits cAMP induction by the G(s)-coupled beta-adrenergic receptor. Activation of either the G(i)- or G(s)-dependent pathway typically results in ERK phosphorylation in HEK293 cells. In contrast to opposing actions on cAMP synthesis, simultaneous MCH and forskolin treatment results in synergistic activation of ERK. This synergy proceeds through pertussis toxin-independent pathways and requires several enzymatic activities such as protein kinase A, protein kinase C, phospholipase C, and Src kinase. Finally, we provide evidence that such positive interactions are not limited to cell lines but can also be observed in the brain.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12865333&dopt=Abstract

Lasers Surg Med. 2003;33(1):16-24.
Thermal response of human skin epidermis to 595-nm laser irradiation at high incident dosages and long pulse durations in conjunction with cryogen spray cooling: an ex-vivo study.

Dai T, Pikkula BM, Tunnell JW, Chang DW, Anvari B.

Department of Bioengineering, Rice University, Houston, Texas 77251, USA.

BACKGROUND AND OBJECTIVES: Improved laser treatment of cutaneous hypervascular lesions is expected by utilizing higher incident dosages, longer pulse durations and longer wavelengths than those currently used in clinical settings. However, simply increasing the incident dosage will also increase the risk of nonspecific thermal injury to the epidermis due to light absorption by melanin. In this study, we investigated the thermal response of human skin epidermis to 595-nm wavelength laser irradiation at high incident dosages (up to 20 J/cm(2)) and long pulse durations (up to 40 milliseconds) in conjunction with cryogen spray cooling (CSC) using ex-vivo human skin samples. STUDY DESIGN/MATERIALS AND METHODS: The Candela V-beam trade mark laser (595-nm wavelength) was used in the experiments. Ex-vivo human skin samples (Fitzpatrick types I-VI) were irradiated at the incident dosages D(0) = 4, 6, 10, 15, and 20 J/cm(2), laser pulse durations tau(laser) = 1.5, 10, and 40 milliseconds, without and with CSC (refrigerant-134A, spurt duration tau(CSC) = 100 milliseconds). Thermal injury to the epidermis was evaluated by histological observations. RESULTS: Under the same incident dosage, longer pulse durations led to reduced thermal injury to the epidermis. Without CSC, no demonstrable thermal injury to the epidermis was observed in skin types I-II irradiated at the incident dosage as high as 15 J/cm(2), and in skin types III-IV at 10 J/cm(2). When CSC was applied, no evidence of thermal injury to the epidermis was present in skin types I-II even when irradiated at the maximum available incident dosage of the laser system (20 J/cm(2)). In skin types III-IV, no demonstrable thermal injury to the epidermis was observed when using incident dosage as high as 15 J/cm(2) in conjunction with CSC. In skin type VI, thermal injury to the epidermis could not be avoided even at the setting D(0) = 4 J/cm(2), tau(laser) = 40 milliseconds in conjunction with CSC. CONCLUSIONS: For a given incident dosage, longer pulse durations help reduce thermal injury to the epidermis. When a 100-millisecond cryogen spurt is applied, thermal injury to the epidermis can be prevented in ex-vivo skin types I-IV when irradiated at higher incident dosages (15-20 J/cm(2)) than those currently used in clinical settings. Further studies on optimizing the CSC parameters in conjunction with the laser irradiation parameters are needed to protect skin types V-VI from thermal injury to the epidermis. 2003 Wiley-Liss, Inc.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12866117&dopt=Abstract [PubMed - in process]

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