Expression of Myosin Light Chain Kinase in Kidney of Streptozotocin-Induced Diabetic Rats

Zhu, Huaqing; Zhang, Xiaolin; Zuo, Li; Zhou, Qing; Gui, Shuyu; Wei, Wei; Wang, Yuan

doi:10.3390/i7110510

Cited by 2 publications

(1 citation statement)

References 29 publications

(28 reference statements)

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“…This indicates that some factors in the macroalbuminuric sera activate NM-IIA and may thereby enhance GSV docking and fusion and glucose uptake into podocytes. Further support for a role for NM-IIA and associated kinases in DN is provided in a study showing that the expression of myosin light chain kinase increases in the kidneys in streptozotocin-induced diabetes [41]. In addition, polymorphisms in MYH9 , which encodes NMHC-IIA, are associated with DN in European Americans [42].…”

Section: Discussionmentioning

confidence: 99%

Septin 7 reduces nonmuscle myosin IIA activity in the SNAP23 complex and hinders GLUT4 storage vesicle docking and fusion

Wasik

Dumont

Tienari

et al. 2017

Experimental Cell Research

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Glomerular epithelial cells, podocytes, are insulin responsive and can develop insulin resistance. Here, we demonstrate that the small GTPase septin 7 forms a complex with nonmuscle myosin heavy chain IIA (NMHC-IIA; encoded by MYH9), a component of the nonmuscle myosin IIA (NM-IIA) hexameric complex. We observed that knockdown of NMHC-IIA decreases insulin-stimulated glucose uptake into podocytes. Both septin 7 and NM-IIA associate with SNAP23, a SNARE protein involved in GLUT4 storage vesicle (GSV) docking and fusion with the plasma membrane. We observed that insulin decreases the level of septin 7 and increases the activity of NM-IIA in the SNAP23 complex, as visualized by increased phosphorylation of myosin regulatory light chain. Also knockdown of septin 7 increases the activity of NM-IIA in the complex. The activity of NM-IIA is increased in diabetic rat glomeruli and cultured human podocytes exposed to macroalbuminuric sera from patients with type 1 diabetes. Collectively, the data suggest that the activity of NM-IIA in the SNAP23 complex plays a key role in insulin-stimulated glucose uptake into podocytes. Furthermore, we observed that septin 7 reduces the activity of NM-IIA in the SNAP23 complex and thereby hinders GSV docking and fusion with the plasma membrane.

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Section: Discussionmentioning

confidence: 99%