PubMed · 10873421
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A Saxon. 2000. Good "negative results".. https://doi.org/10.1006/clim.2000.4885
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OBJECTIVE: To investigate whether detectable C-peptide levels in type 1 diabetes is associated with a lower risk of diabetic ketoacidosis (DKA). RESEARCH DESIGN AND METHODS: We analyzed the Diabetes Control and Complications Trial publicly available data repository for the association between detectable stimulated C-peptide (>0.2 nmol/mL, measured annually) and DKA incidence over an average 6.5-year follow-up. We used crude and adjusted Andersen-Gill models for recurrent DKA events with time-dependent covariates. RESULTS: Of the 1,441 participants (53% male, median age 27 years), 129 (9%) experienced 180 DKA events. Of these events, 179 (99.44%) occurred after C-peptide was ≤0.2 nmol/L in the prior year and only 1 event occurred with C-peptide >0.2 nmol/L. C-peptide >0.2 nmol/L was associated with a DKA hazard ratio of 0.07 (95% CI 0.01-0.48; P = 0.007), consistent across adjusted models. CONCLUSIONS: Endogenous insulin production was significantly associated with lower DKA risk, suggesting that treatments preserving insulin production could decrease long-term DKA risk.
OBJECTIVES: The catabolic state is a major contributor to morbidity and mortality of critical illness and may be related to endocrine changes. We studied whether protein and lipid turnover correlate with insulin and growth and thyroid hormone plasma levels in critically ill infants. DESIGN: Prospective clinical study. SETTING: Pediatric intensive care unit. PATIENTS: Twelve critically ill children and ten age-matched controls. MEASUREMENTS: We measured lipolysis and protein turnover by infusing albumin-bound uniformly 13C palmitic acid and 2H3-leucine for 3 hrs and 2H5-glycerol for 5 hrs to critically ill infants. Simultaneously, we measured serum growth hormones, insulin, C-peptide, thyroid-stimulating hormone, T4, T3, albumin, retinol binding protein (RBP), and prealbumin. Hormone and serum protein levels were also measured in six children when recovered from critical illness. Ten healthy age-matched children served as controls for hormone serum levels comparison. RESULTS: Palmitic acid and glycerol turnover were 5.6 +/- 2.2 micromol/kg/min and 12.2 +/- 7.3 micromol/kg/min, respectively, whereas alpha-ketoisocaproic turnover was 4.9 +/- 2.8 micromol/kg/min. Alpha-ketoisocaproic turnover positively correlated (R = 0.7, p = .03) with duration of pediatric intensive care unit admission and with prealbumin and RBP serum levels (R = 0.9, p = .001). Insulin-like growth factor binding protein (IGFBP)-2 was significantly higher and IGFBP-3 was significantly lower in critically ill children (p = .03 and p = .04 vs. recovery phase, respectively). No other hormonal differences were found. Serum albumin was significantly lower in sick children. We found a significant correlation between prealbumin and RBP and IGFBP-3 (R = 0.6, p = 0.03 and R = 0.6, p = .04, respectively). Alpha-ketoisocaproic turnover positively correlated with IGFBP-1 (R = 0.79, p = .01) and did not correlate with insulin-like growth factor I (R = -0.5, p = .15 [not significant]) No other correlations were found. Lipid turnover measurements did not correlate with any endogenous hormone levels or with duration of critical illness. CONCLUSION: Protein turnover but not lipolysis correlated with a persisting critically ill condition, serum prealbumin, RBP, and plasma IGFBP-1.
Proinsulin C-peptide exerts physiological effects on kidney and nerve function, but the mechanisms involved remain incompletely understood. Using fluorescence correlation spectroscopy, we have studied binding of rhodamine-labelled human C-peptide to intact human skin fibroblasts and to detergent-solubilised extracts of fibroblasts, K-562, and IEC-6 cells. Specificity was shown by displacement of rhodamine-labelled human C-peptide with unlabelled human C-peptide. C-peptide was found to bind to the cell membranes of intact fibroblasts with an association constant of 3 x 10(9) M(-1), giving full saturation at about 0.9 nM, close to the physiological C-peptide plasma concentration. Treatment of all investigated cells with the zwitter-ionic detergent Chaps was found to release macromolecules that bind specifically to C-peptide. The binding in Chaps extracts of fibroblasts was sensitive to time but remained reproducible for up to 2 h at room temperature. Lysophosphatidylcholine, Triton X-100, beta-octylglucopyranoside, SDS, or cholate gave extracts with only low or nonspecific binding. It is concluded that C-peptide binding components can be solubilised from cells, and that Chaps appears to be a suitable detergent.