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Unfolded protein response modulates Tyrosinase levels and melanin production during melanogenesis.

J Dermatol Sci

January 2025

Department of Biochemistry, Institute of Biomedical & Health Sciences, Hiroshima University, Hiroshima, Japan; Department of Frontier Science and Interdisciplinary Research, Faculty of Medicine, Kanazawa University, Ishikawa, Japan. Electronic address:

Background: Melanocytes protect the body from ultraviolet radiation by synthesizing melanin. Tyrosinase, a key enzyme in melanin production, accumulates in the endoplasmic reticulum (ER) during melanin synthesis, potentially causing ER stress. However, regulating ER function for melanin synthesis has been less studied than controlling Tyrosinase activity.

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The scientific discipline of endocrinology has been invaluable to our understanding of the estrous cycle. In the second half of the twentieth century the development of immunoassay technologies provided a rapid and sensitive method to quantify circulating concentrations of reproductive hormones and relate them to stage of the estrous cycle and physiological status of the animal. Ovarian ultrasonography provided the ability to track the growth and regression of ovarian structures within the same animal across the estrous cycle in real time and, in combination with hormonal profiling, accurately identify mechanisms regulating the estrous cycle and early pregnancy.

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Type II restriction-modification (R-M) systems play a pivotal role in bacterial defense against invading DNA, influencing the spread of pathogenic traits. These systems often involve coordinated expression of a regulatory protein (C) with restriction (R) enzymes, employing complex feedback loops for regulation. Recent studies highlight the crucial balance between R and M enzymes in controlling horizontal gene transfer (HGT).

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Aims: Sarcoendoplasmic reticulum Ca-ATPase 2 (SERCA2), encoded by ATP2A2, is a key protein involved in intracellular Ca homeostasis. The SERCA2a isoform is predominantly expressed in cardiomyocytes and type I myofibres. Variants in this gene are related to Darier disease, an autosomal dominant dermatologic disorder, but have never been linked to myopathy.

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Small Molecular Oligopeptides Adorned with Tryptophan Residues as Potent Antitumor Agents: Design, Synthesis, Bioactivity Assay, Computational Prediction, and Experimental Validation.

J Chem Inf Model

January 2025

Key Laboratory for Photonic and Electronic Bandgap Materials, Ministry of Education, College of Chemistry and Chemical Engineering, Harbin Normal University, Harbin 150025, China.

Tryptophan participates in important life activities and is involved in various metabolic processes. The indole and aromatic binuclear ring structure in tryptophan can engage in diverse interactions, including π-π, π-alkyl, hydrogen bonding, cation-π, and CH-π interactions with other side chains and protein targets. These interactions offer extensive opportunities for drug development.

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