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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

Colloids Surf B Biointerfaces. 2001 Apr;20(4):315-319.
Oxygen adsorption and photoreduction on fractal melanin particles.

Crippa PR.

INFM and Department of Environmental Sciences, University of Parma, Parco Area delle Scienze 7/A, 43100, Parma, Italy

The main putative functions of melanins in living cells, that is photoprotection and dark or light-dependent oxido-reductive activity, still requires an interpretation which takes into account the micro-mesoscopic structure of native melanin particles. It is indeed well established that a different chemical composition of melanins, even if derived from different biosynthetic pathways, has only a little influence on the biological and physical properties of the solid aggregates, the common form in which the pigment is found [P.R. Crippa et al., Chemistry of melanins, in: A. Brossi (Ed.) The Alkaloids, vol. 36, Academic Press, New York, 1989, pp. 253-323]. In the present work a model for interfacial electron transfer is proposed describing the process of light induced superoxide formation through a monoelectronic reduction of dioxygen adsorbed on melanin solid surface. This process is presumed to be dependent on the surface fractal characteristics, and its kinetics must be interpreted as a heterogeneous interfacial reaction involving light produced carriers and the adsorbed acceptor, like in colloidal inorganic semiconductors such as TiO(2).

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11166541&dopt=Abstract [PubMed - as supplied by publisher]

Brain Res. 2001 Jan 19;889(1-2):1-22.
The posterior hypothalamic area: chemoarchitecture and afferent connections.

Abrahamson EE, Moore RY.

Department of Neuroscience, University of Pittsburgh, W1656 Biomedical Science Tower, Pittsburgh, PA 15261, USA. eeasmap.pitt.edu

This study provides an analysis of the chemoarchitecture of the posterior hypothalamic area (PHA) and a retrograde transport analysis of inputs to the PHA in the rat. The chemoarchitectural analysis reveals that the majority of PHA neurons contain glutamate. Hypocretin, melanin concentrating hormone, tyrosine hydroxylase, neuropeptide Y and gamma-aminobutyric acid are also found in subsets of PHA neurons, and fibers immunoreactive for these substances as well as for serotonin, dopamine-beta-hydroxylase and met-enkephalin are observed in the area and aid in the delineation of its borders. The retrograde tracing study demonstrates that the PHA receives input from multiple, diverse neuron populations. Descending projections to the PHA arise from the limbic forebrain (cingulate cortex and lateral septum) and both the medial and lateral hypothalamus. Subcortical visual nuclei, including the ventral lateral geniculate nucleus and intergeniculate leaflet, pretectal area, and superior colliculus, and the subthalamus (zona incerta, fields of Forel) also project to the PHA. Ascending projections to the PHA arise from brainstem cholinergic nuclei, the reticular formation, midbrain raphe nuclei, periaqueductal gray and parabrachial nucleus. Retrograde transport studies using the psuedorabies virus (PRV) demonstrate that the PHA receives input indirectly from the hippocampus, amygdala and suprachiasmatic nucleus through circuits including nuclei in the limbic forebrain and hypothalamus. These data suggest that the PHA is important in the neural control of behavioral state, modulating aspects of hippocampal, autonomic and cortical function as they relate to the elaboration of adaptive behavior.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11166682&dopt=Abstract

Br J Dermatol. 2001 Jan;144(1):55-65.
Increased sensitivity of melanocytes to oxidative stress and abnormal expression of tyrosinase-related protein in vitiligo.

Jimbow K, Chen H, Park JS, Thomas PD.

Department of Dermatology, Sapporo Medical University School of Medicine, S-1, W-16, Chuo-ku, Sapporo 060-8543, Japan. jimboapmed.ac.jp

BACKGROUND: Vitiligo is a depigmenting disease of the skin, which may derive from programmed melanocyte death or destruction due to inherent sensitivity to oxidative stress arising from either toxic intermediates of melanin, a melanocyte-specific protein, or other sources. Tyrosinase-related protein (TRP) -1 has been shown to be involved not only in melanin biosynthesis but also in the prevention of premature melanocyte death in animals. OBJECTIVES: To clarify the biological role of human TRP-1 in melanocyte survival. METHODS: Cultured melanocyte strains from an active advancing border of vitiligo were established and studied. RESULTS: The established 'vitiligo melanocytes' showed large perikaryon and stubby dendrites. They showed early cell death when exposed to oxidative stress (ultraviolet B) and increased and abnormal immunostaining and immunoprecipitation by antibodies against human and mouse TRP-1, indicating an altered synthesis and processing of TRP-1. In pulse-chase and sequential immunoprecipitation experiments, vitiligo melanocytes revealed abnormal protein-protein interaction with calnexin, a melanogenesis-associated chaperone, suggesting altered folding and maturation of nascent TRP-1 polypeptides. Northern blot analysis indicated a decreased expression of TRP-1 mRNA, but heteroduplex analysis and verification of the mutation at the carboxy terminus of TRP-1 by restriction enzyme analysis did not show any abnormality. CONCLUSIONS: Our study suggests that the early cell death of vitiligo melanocytes is related to their increased sensitivity to oxidative stress, which may arise from complex processes of abnormal synthesis and processing of TRP-1 and its interaction with calnexin.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11167683&dopt=Abstract

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