Chemerin acts as both a chemotactic agent and an adipokine that undergoes proteolytic cleavage, converting inactive precursors into their active forms before being subsequently inactivated. Elevated chemerin levels are linked to obesity and type 2 diabetes mellitus (T2D). This study aimed to elucidate the effects of T2D and obesity on chemerin levels by comparing plasma samples from individuals with a normal weight and T2D (BMI < 25; NWD group = 22) with those from individuals who are overweight or obese and have T2D (BMI ≥ 25; OWD group = 39).
View Article and Find Full Text PDFChemerin is a chemokine/adipokine, regulating inflammation, adipogenesis and energy metabolism whose activity depends on successive proteolytic cleavages at its C-terminus. Chemerin levels and processing are correlated with insulin resistance. We hypothesized that chemerin processing would be higher in individuals with type 2 diabetes (T2D) and in those who are insulin resistant (IR).
View Article and Find Full Text PDFOsteopontin (OPN) is a matricellular protein containing binding sites for a variety of ligands including an RGD sequence for binding to αβ integrins. OPN is a conserved substrate for thrombin, the effector protease of the coagulation cascade. Thrombin cleaves OPN at a single site revealing new functionalities such as a previously cryptic αβ and αβ integrin-binding site.
View Article and Find Full Text PDFBackground: Procarboxypeptidase B2 (proCPB2 or TAFI) is a zymogen that after activation cleaves C-terminal basic residues from peptides or proteins with many identified targets. A splice variant of CPB2 has been found in the brain lacking essential residues for its carboxypeptidase function. The aim was to determine CPB2 expression in the brain and effects of CPB2 deficiency ( ) on behavior.
View Article and Find Full Text PDFOsteopontin (OPN) is a multi-functional protein that is involved in various cellular processes such as cell adhesion, migration, and signaling. There is a single conserved thrombin cleavage site in OPN that, when cleaved, yields two fragments with different properties from full-length OPN. In cancer, OPN has tumor-promoting activity and plays a role in tumor growth and metastasis.
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