ABSTRACT
Purpose: To evaluate the prognostic potential of systemic inflammatory index in the course of retinopathy of prematurity (ROP). Methods: This is a retrospective case-control study. 303 infants with a gestational age of ≤35 weeks were screened with and without ROP at birth and 1 month after the birth of complete blood counts (CBC) were included in this study. Serum neutrophil-to-lymphocyte ratio (NLR), lymphocyte-to-monocyte ratio (LMR), platelet-to-lymphocyte (PLR), and systemic immune-inflammation index (SII) was calculated at birth and one month after. LMR was calculated by dividing the absolute lymphocyte count by the absolute monocyte count. NLR and PLR were determined by dividing the absolute neutrophil count or the absolute platelet count by the absolute lymphocyte count, respectively. The SII was calculated by the formula = neutrophilxplatelet/lymphocyte. All statistical analyses were performed using SPSS 22 (SPSS for Windows, version 22.0; SPSS, Inc. Chicago, IL, USA). Results: A total of 303 infants were included 145 with ROP and 158 without ROP. The NLR, LMR, PLR and SII values were 0.56 ± 1.17/0.51 ± 1.04 (P = 0.997), 13.7 ± 18/9.49 ± 13.1 (P = 0.014), 31.69 ± 68/24.1 ± 37.7 (P = 0.268), 131.42 ± 326/124.66 ± 267 (P = 0.935) in with ROP and without ROP infant at birth respectively. The NLR, LMR, PLR, and SII values were 0.68 ± 1.27/0.34 ± 0.99 (P = 0.001), 2.58 ± 6.01/2.46 ± 14.5 (P = 0.706), 47.5 ± 78.33/33.55 ± 42.4 (P = 0.035), and 253 ± 681/114 ± 345 (P = 0.001), respectively in with ROP and without ROP infant at 1 month after birth. Conclusion: The NLR, PLR, and SII seem an independent predictor of the development of ROP.
Subject(s)
Retinopathy of Prematurity , Blood Cell Count , Case-Control Studies , Humans , Infant , Infant, Newborn , Inflammation , Prognosis , Retinopathy of Prematurity/diagnosis , Retrospective StudiesABSTRACT
The ethyl acetate extract of the Bangladeshi mango mistletoe (Loranthus globosus) bark was found to be most effective against both Gram (+) and Gram (-) bacteria and it also showed good cytotoxicity with a LC50 10.83 microg/ml.
Subject(s)
Anti-Bacterial Agents/pharmacology , Loranthaceae , Phytotherapy , Plant Extracts/pharmacology , Animals , Anti-Bacterial Agents/administration & dosage , Anti-Bacterial Agents/therapeutic use , Artemia/drug effects , Bangladesh , Gram-Negative Bacteria/drug effects , Gram-Positive Bacteria/drug effects , Humans , Medicine, Traditional , Microbial Sensitivity Tests , Plant Bark , Plant Extracts/administration & dosage , Plant Extracts/therapeutic useABSTRACT
(+)-Catechin, 3,4-dimethoxycinnamyl alcohol and 3,4,5-trimethoxycinnamyl alcohol were isolated from the barks of Loranthus globosus. All compounds showed significant antimicrobial and cytotoxic activities.
Subject(s)
Anti-Infective Agents/pharmacology , Antifungal Agents/pharmacology , Gram-Negative Bacteria/drug effects , Gram-Positive Bacteria/drug effects , Loranthaceae , Phytotherapy , Plant Extracts/pharmacology , Animals , Anti-Bacterial Agents , Anti-Infective Agents/administration & dosage , Anti-Infective Agents/therapeutic use , Antifungal Agents/administration & dosage , Antifungal Agents/therapeutic use , Artemia/drug effects , Aspergillus flavus/drug effects , Humans , Lethal Dose 50 , Microbial Sensitivity Tests , Plant Bark , Plant Extracts/administration & dosage , Plant Extracts/therapeutic use , Rhizopus/drug effectsABSTRACT
The formation of beta A4 amyloid in the brains of individuals with Alzheimer's disease requires the proteolytic cleavage of amyloid precursor protein. Several lines of evidence suggest that cathepsin D, the major lysosomal/endosomal aspartic protease, may be involved in this process. In this work, we used a sensitive in vitro method of detection to investigate the role of cathepsin D in the proteolytic processing of a 100-amino acid C-terminal fragment (C100) inclusive of beta A4 and cytoplasmic domain of APP. Digestion of C100 with cathepsin D resulted in cleavage at the amyloidogenic gamma-cleavage sites. This occurred preferentially at Thr43-Val44 and at Ala42-Thr43, generating full length beta A4 43 and beta A4 42 amyloid peptides, respectively. Cathepsin D was also found to cleave the substrate at the following nonamyloidogenic sites; Leu34-Met35, Thr48-Leu49 and Leu49-Val50. A high concentration of cathepsin D resulted in cleavage also occurring at Phe19-Phe20, Phe20-Ala21 and Phe93-Phe94 of the C100, suggesting that these sites are somewhat less sensitive to the action of cathepsin D. Digestion of C100 using different solublizing agents indicated that the cleavage of C100 by cathepsin D is greatly influenced by the structural integrity of the substrate. However, our results suggest that cathepsin D could generate the pathogenic beta A4 amyloid peptides from its precursor in vitro, which may indicate a role in the amyloidogenesis of Alzheimer's disease.
