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Chromium has been known to be a micronutrient for mammals for four decades, but progress in elucidating the role of chromium has proceeded slowly. However, recent studies have shed light on a potential role of chromium in maintaining proper carbohydrate and lipid metabolism at a molecular level. The oligopeptide chromodulin binds chromic ions in response to an insulin-mediated chromic ion flux, and the metal-saturated oligopeptide can bind to an insulin-stimulated insulin receptor, activating the receptor's tyrosine kinase activity. Thus, chromodulin appears to play a role in an autoamplification mechanism in insulin signaling. The molecular agent responsible for transporting chromium from mobile pools to insulin-sensitive cells is probably the metal transport protein transferrin. Chromium from the popular dietary supplement chromium picolinate enters cells via a different mechanism. Release of chromium from chromium picolinate for use in cells requires reduction of the chromic center, a process that can lead potentially to the production of harmful hydroxyl radicals.

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Chromium is an essential trace element for mammals and is required for maintenance of proper carbohydrate and lipid metabolism. However, elucidating its function at a molecular level has proved to be problematic. Recent research has revealed that the chromium-binding oligopeptide chromodulin may play a unique role in the autoamplification of insulin signaling. Attempts to develop chromium-containing nutritional supplements and therapeutics are described.

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A possible new mechanism for the amplification of insulin receptor tyrosine kinase activity in response to insulin has been identified. The chromium-containing oligopeptide low molecular weight chromium-binding substance (LMWCr) does not effect the tyrosine protein kinase activity of rat adipocytic membrane fragments in the absence of insulin; however, insulin-stimulated kinase activity in the membrane fragments is increased up to 8-fold by the oligopeptide. Using isolated rat insulin receptor, LMWCr has been shown to bind to insulin-activated insulin receptor with a dissociation constant of circa 250 pM, resulting in the increase of its tyrosine protein kinase activity. The ability of LMWCr to stimulate insulin receptor tyrosine kinase activity is dependent on its chromium content. The results appear to explain the previously poorly understood relationship between chromium and adult-onset diabetes and cardiovascular disease.

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