The role of neutrophil-gelatinase-associated lipocalin in early diagnosis of contrast nephropathy.

Neutrophil-gelatinase-associated lipocalin (NGAL) is a biomarker of acute kidney injury. The aim of this study was to define a cut-off for NGAL in the early diagnosis of contrast-induced nephropathy (CIN) in patients with normal kidney function. We enrolled 121 patients with normal serum creatinine who underwent coronary angiography. NGAL was measured in urine before the procedure and 12 and 24 h afterward. CIN was defined as a 0.3 mg/dl increase in serum creatinine within 48 h after the procedure. Seven of 121 patients had CIN (5.8%). The NGAL levels in the 12- and 24-h urine samples of these patients were 30 (5-45) and 20 (15-40) ng/ml, respectively, whereas those in patients without CIN were 15 (5-45) and 15 (10-51) ng/ml, respectively (P = 0.8). In patients with CIN, the sensitivity and specificity of NGAL with a cut-off of 22.5 ng/ml were 71.4% and 57.9% in 12-h urine samples, with the negative predictive values (NPV) and positive predictive values (PPV) of 97.1% and 9.4%, respectively. In conclusion, we suggest that urine NGAL with cut-off point of 22.5 ng/ml has acceptable sensitivity and specificity for early diagnosis of CIN in patients with normal serum creatinine, but regarding NPV and PPV the best performance of this value is to rule out the CIN in patients at risk who received contrast media.

Quality and Quantity of Health Evaluation and the Follow-up of Iranian Living Donors.

BACKGROUND: Shortage of donors is the main obstacle in organ transplantation. In renal transplantation living donation is the key solution for removing this barrier. The Iranian model of kidney transplantation has been faced with many challenges, but there are limited reports about the depth of evaluation and outcome of donors. This study was conducted to assess the quality and quantity of donors' health evaluation before donation and their follow-up afterward. METHODS: With assistance of the Iranian Kidney Foundation, we accessed the contact information of living donors through the years 2001-2012. We tried to contact donors who have donated at least 2 years before the survey. We interviewed these donors according to a questionnaire that was approved by the ethics committee of the research deputy of Tehran University of Medical Sciences. The collected data were analyzed using the SPSS software version 20. RESULTS: The contact data of 388 donors were available but we were able to contact only 60 donors. We found that 40% of donors had been informed about the risks and benefits of donation. Also, 11% of donors had not had a full physical examination and in 5% even blood pressure was not measured before donation by the transplantation team. The donors reported that 34% of them had not been educated on how they should follow up their health status and 50% of the donors did not have any follow-up after donation. CONCLUSION: In the Iranian model of transplantation the donors are the neglected victims of renal transplantation and this model should be revised immediately, concerning both the medical and ethical issues.

The secreted Dictyostelium protein CfaD is a chalone.

Dictyostelium discoideum cells secrete CfaD, a protein that is similar to cathepsin proteases. Cells that lack cfaD proliferate faster and reach a higher stationary-phase density than wild-type cells, whereas cells that overexpress CfaD proliferate slowly and reach the stationary phase when at a low density. On a per-nucleus basis, CfaD affects proliferation but not growth. The drawback of not having CfaD is a reduced spore viability. Recombinant CfaD has no detectable protease activity but, when added to cells, inhibits the proliferation of wild-type and cfaD(-) cells. The secreted protein AprA also inhibits proliferation. AprA is necessary for the effect of CfaD on proliferation. Molecular-sieve chromatography indicates that in conditioned growth medium, the 60 kDa CfaD is part of a approximately 150 kDa complex, and both chromatography and pull-down assays suggest that CfaD interacts with AprA. These results suggest that two interacting proteins may function together as a chalone signal in a negative feedback loop that slows Dictyostelium cell proliferation.