Scalp Condition Impacts Hair Growth and Retention via Oxidative Stress.

Conventionally, the medical focus has been either on hair loss or the condition of the scalp in terms of specific dermatological diseases. Indeed, the proximate structural arrangement of the scalp and hair leads to an interdependent relationship between the two. While protective benefits of the hair to the scalp are obvious, the role of the scalp as an incubatory environment for the preemergent hair fiber has largely been ignored. In fact, there is a wealth of observational data on specific dermatological conditions of the scalp providing evidence for the role of the scalp condition in supporting the production of healthy hair. Oxidative stress, the inability of the body to sufficiently counteract the sources of oxidation, is prevalent in many skin conditions, including normal skin aging. On the scalp, the hair appears to be impacted prior to emergence, and oxidative stress appears to play a role in premature hair loss. The scalp commensal organism, Malassezia, has been recognized to be a source of oxidative damage. Therefore, hair care products, specifically shampoos, with active Malassezia inhibitory agents, such as zinc pyrithione, tend to reduce premature hair loss, besides the known benefits in treating specific dermatologic scalp pathologies, and therefore should represent an integral part of every treatment regimen for hair loss, even in individuals not showing symptoms of scalp pathologies.

Mechanism of insulin sensitization by BMOV (bis maltolato oxo vanadium); unliganded vanadium (VO4) as the active component.

Organovanadium compounds have been shown to be insulin sensitizers in vitro and in vivo. One potential biochemical mechanism for insulin sensitization by these compounds is that they inhibit protein tyrosine phosphatases (PTPs) that negatively regulate insulin receptor activation and signaling. In this study, bismaltolato oxovanadium (BMOV), a potent insulin sensitizer, was shown to be a reversible, competitive phosphatase inhibitor that inhibited phosphatase activity in cultured cells and enhanced insulin receptor activation in vivo. NMR and X-ray crystallographic studies of the interaction of BMOV with two different phosphatases, HCPTPA (human low molecular weight cytoplasmic protein tyrosine phosphatase) and PTP1B (protein tyrosine phosphatase 1B), demonstrated uncomplexed vanadium (VO(4)) in the active site. Taken together, these findings support phosphatase inhibition as a mechanism for insulin sensitization by BMOV and other organovanadium compounds and strongly suggest that uncomplexed vanadium is the active component of these compounds.