{'fraction_non_alphanumeric': 0.03238242097147263, 'fraction_numerical': 0.016962220508866616, 'mean_word_length': 5.588832487309645, 'pattern_counts': {'":': 0, '<': 1, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Evidence of calpain and PKC cosignaling in diabetic endothelial dysfunction

Vascular complications are a well‐known cause of morbidity and mortality in diabetes. Endothelial dysfunction is thought to be a primary event in vascular inflammation. Both protein kinase C (PKC) and, more recently, calpain have been implicated in this process. Calpains are a family of calcium‐dependent cysteine proteases that are involved in many cellular processes including the activation of PKC. We hypothesized that calpain and PKC cosignal in the endothelial dysfunction of hyperglycemia. Studies were performed in streptozotocin‐induced diabetic rats before and after calpain inhibition. Biochemical analysis of mesenteric tissue extracts demonstrated a 1.5‐fold increase in calpain activity and a 1.3‐fold increase in PKC activity in diabetic rats. Intravital microscopy of mesenteric post‐capillary venules demonstrated a calpain‐dependent increase in leukocyte adhesion in diabetic rats (adherent leukocytes/100 μm vessel length were 2.8±0.5, 6.9±0.4; and 3.5±1.2 in control rats, diabetic rats and diabetic rats treated with the calpain inhibitor ZLLal, respectively; p<0.05). Taken together, these data indicate a novel relationship between calpain and PKC in the endothelial dysfunction of hyperglycemia.