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Metabolism, Diabetes, and Cancer · Journal article
Kinases and Phosphatases · September 10, 2026
Raises a question worth testing. It does not answer one.
This is a mechanistic review article examining how dysregulation of protein kinase C (PKC) may contribute to insulin resistance and metabolic syndrome through serine/threonine phosphorylation of insulin signaling proteins. The source presents established biochemical concepts and theoretical pathways but does not report primary experimental or clinical evidence, and thus frames questions for investigation rather than providing answers.
Journal article.
PKC dysregulation is associated with development of metabolic syndrome, a cluster including insulin resistance, lipid dysregulation, chronic inflammation, hypertension, and obesity. Serine/threonine phosphorylation of insulin receptor and downstream substrates is associated with decreased insulin signaling and insulin resistance. PKC dysregulation can impair insulin-facilitated glucose uptake and storage and disrupt lipid storage mechanisms, exacerbating insulin resistance.
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The source did not state who this applies to in practice.
A mechanistic review examining PKC's role in insulin resistance and metabolic syndrome that raises questions about signaling pathways rather than reporting primary experimental evidence or clinical outcomes.
Graded across the dimensions that decide whether you should act, each from what the source actually supports. There is no single score, and where a dimension was not assessed it says so.
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One mechanism contributing to insulin resistance is the serine/threonine phosphorylation of critical proteins involved in insulin signaling, particularly the insulin receptor, its downstream substrates, and the activation of protein tyrosine phosphatases. These modifications are associated with decreased insulin signaling, leading to insulin resistance. Protein kinase C (PKC), a family of serine/threonine kinases activated by lipids and/or Ca2+, is essential for regulating metabolism and maintaining cellular homeostasis. These kinases regulate glucose uptake and lipid storage, thereby influencing energy balance through tissue-specific mechanisms. However, dysregulation of PKC activity is closely associated with the development of metabolic syndrome (MetS), a cluster of interconnected physiological and biochemical alterations, including insulin resistance, lipid dysregulation, chronic inflammation, hypertension, and obesity, all of which increase the risk of cardiovascular disease (CVD) and type 2 diabetes (T2D). Notably, alterations in PKC signaling can impair insulin’s ability to facilitate glucose uptake and storage and disrupt lipid storage mechanisms, thereby exacerbating insulin resistance. These dysfunctions significantly contribute to the pathophysiology of MetS. This review aims to examine PKC activation under normal physiological conditions, with particular emphasis on its role in insulin signaling, and to explore how PKC dysregulation participates in the pathophysiology of insulin resistance and MetS.
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