Anemia of chronic disease is normocytic and normochromic. One of the mechanisms is misbalance of iron metabolism. Hepcidin, a kind of protein secreted by liver is considered to be the hormone regulating iron metabolism. It binds to ferroportin and induces the latter one's internalization. Thus, iron transportation from iron storage cells to serum is reduced. Cytokines are elevated in chronic disease. They stimulate hepcidin expression in liver through JAK2/STAT3 pathway. As a result, iron absorption and reabsorption is blocked, which leads to the misbalance of iron metabolism in anemia of chronic disease. In this article, the hepcidin and its relation to iron metabolism and anemia in chronic disease are reviewed.
Anemia ; metabolism ; Antimicrobial Cationic Peptides ; metabolism ; Chronic Disease ; Hepcidins ; Humans ; Iron ; metabolism

OBJECTIVE: To evaluate the application of heparin-binding protein (HBP) in diagnosis of sepsis in adult patients. METHODS: An extensive search for the Chinese and English literatures from the PubMed, Embase, the Cochrane Library, Wanfang data, CNKI and VIP up to July 2019 was performed. The articles regarding HBP for the diagnosing of sepsis in adult patients were enrolled. Two researchers independently extracted related literature. The quality of the studies was assessed using the Quality Assessment of Diagnostic Accuracy Studies (QUADAS-2) tool. Meta-Disc 1.4 and STATA 12.0 were used for Meta-analysis. The pooled sensitivity, specificity, positive likelihood ratio (PLR), negative likelihood ratio (NLR), and diagnostic odds ratio (DOR) were calculated. Summary receiver operating characteristic (SROC) curves and area under the curve (AUC) were used to evaluate the diagnostic performance of HBP for sepsis. Deek funnel plot was used to detect publication bias. RESULTS: A total of 10 studies with 1 884 patients were included in this Meta-analysis. The quality of the literature was relatively moderate. HBP in plasma were detected by enzyme linked immunosorbent assay (ELISA) in all studies. The studies showed substantial heterogeneity, and random effect model was used for Meta-analysis. The pooled sensitivity, specificity, PLR, NLR, and DOR were 0.80 [95% confidence interval (95%CI) was 0.77-0.83], 0.80 (95%CI was 0.78-0.82), 3.96 (95%CI was 2.45-6.41), 0.28 (95%CI was 0.20-0.39) and 14.63 (95%CI was 6.83-31.30) respectively. The pooled AUC was 0.86 and the Cochran-Q was 0.79. To explore the potential sources of heterogeneity, subgroup analyses were performed based on the severity of the disease, diagnostic criteria and region. However, the results indicated that no methodological covariates affected the diagnostic accuracy of HBP, indicating that there was still unexplained heterogeneity. In addition, the sensitivity analysis by removing individual studies were performed. No outlier study was identified and the results were relatively stable and reliable. Deek funnel plot showed little publication bias. CONCLUSIONS There is preferable value of HBP for diagnosis of sepsis in adult patients. However, it needs to be further confirmed by large multicenter studies.
Adult ; Antimicrobial Cationic Peptides/metabolism* ; Blood Proteins/metabolism* ; Humans ; Sensitivity and Specificity ; Sepsis/metabolism*

Hepcidin can regulate cell irons' efflux transport. The expression of hepcidin can be influenced by the body signals (such as serum ferritin and erythropoietin levels) as well as inflammation, hypoxia and other disease states. These stimulus activate the signaling pathway of BMP-the SMAD, the JAK-STAT and HIF1 through the liver parenchymal cell surface type I transmembrane glycoprotein of HFE, transferrin receptor 1, 2, hepcidin regulatory proteins, thereby changing the hepcidin gene transcription, regulating the expression levels of hepcidin. However, the molecular mechanism that regulate hepcidin expression is unclear. From the signal factors that affect hepcidin expression and signaling pathways involved in its expression, the latest research progress on regulatory mechanism of hepcidin are summarized.
Animals ; Antimicrobial Cationic Peptides ; metabolism ; Hepcidins ; Humans ; Membrane Proteins ; metabolism ; Signal Transduction

Antimicrobial Cationic Peptides ; biosynthesis ; Hepacivirus ; pathogenicity ; Hepcidins ; Iron ; metabolism ; Liver ; chemistry ; metabolism ; pathology

Hepcidin is a small cystein-rich cationic peptide produced mainly by the liver. It was initially isolated from human plasma and exhibited antimicrobial activity. Recently, several lines of evidence have suggested that hepcidin is a key regulator of iron metabolism at the whole body level and is relative to inflammation, infection, hypoxia and anemia. Hepcidin, is implicated in duodenal iron absorption and iron mobilization from reticuloendothelial macrophages. The major mechanism of hepcidin function seems to be the regulation of transmembrane iron transport. As both iron deficiency and iron excess are associated with cellular dysfunction, so hepcidin or hepcidin-related therapeutics could find a place in the treatment of various diseases such as hemochromatosis and anemia of chronic disease. To elucidate biological function of hepcidin further and use it for other research, it is necessary to produce enough hepcidin through DNA recombinant technique. As a highly successful system for the production of a variety of heterologous proteins, the methylotrophic Pichia pastoris system has the probability for a high level production of hepcidin. The subject of this paper is to summarize the regulation of hepcidin gene expression and the understanding of functions of hepcidin. At last, giving a prospect of production hepcidin by gene engineer.
Antimicrobial Cationic Peptides ; biosynthesis ; genetics ; physiology ; Hepcidins ; Humans ; Iron ; metabolism ; Protein Engineering ; methods

Due to their potential application as novel antibiotics, antimicrobial peptides are attracting much attention. Large quantities of highly purified peptides are crucial to basic and clinical studies. Natural resources of antimicrobial peptides are limited and hard to purify, chemical synthesis is of high-cost and unstable, so recombinant expression of antimicrobial peptides is a cost-effective way. Escherichia coli has been the most widely used as host to express antimicrobial peptides with fusion protein, which can not only avoid the lethal effect towards the host, but also protect the peptide from degradation by proteases. Combined with our research, the present article reviews the progress of fusion vector, cleavage methods and optimization options for antimicrobial peptides production with fusion protein in Escherichia coli.
Antimicrobial Cationic Peptides ; biosynthesis ; Escherichia coli ; metabolism ; Genetic Vectors ; Recombinant Fusion Proteins ; biosynthesis

Antimicrobial Cationic Peptides ; metabolism ; Fermentation ; Food Microbiology ; India ; Lactobacillales ; isolation & purification ; metabolism ; Microbial Sensitivity Tests ; Vegetables ; microbiology

In order to investigate the effect of degradable products on degradable property of PGLA in vitro, two kinds of media-PBS and artificial plasma were prepared for immersing PGLA under changing or non-changing media condition. The mass loss rate of PLGA was calculated and the pH value in the non-changing media was measured before and after immersing 2 w, 3 w, 4 w, 6 w, 8 w and 10 w respectively. The results showed that there was almost no statistically significant difference of mass loss rate of PGLA immersing in two kinds of media at 2 w (P > 0.05). But from 2 w to 6 w, the degradation of PGLA immersing in both media under non-changing media group was remarkably faster than those at the same period of changing media group (P < 0.01). During the whole degradable period, the pH value in PBS kept stable around 7.0-7.4, while the pH value in artificial plasma showed gradually decreased as the degradation of PGLA from 7.5 to 5.7. The change of pH values had statistically significant difference between two degradable media (P < 0.01). It was implied that the degradable products existed in immersing media had an effect on degradable speed of PGLA itself if the media was unchanged. It could accelerate the mass loss of material. The pH value also affected the degradable property of PGLA, the lower the pH value, the slower the degradable speed.
Antimicrobial Cationic Peptides ; metabolism ; Biocompatible Materials ; metabolism ; Biodegradation, Environmental ; Blood Substitutes ; Hydrogen-Ion Concentration ; In Vitro Techniques ; Materials Testing

BACKGROUNDAntimicrobial peptides, including cathelicidin LL-37, human beta defensin (HBD)-2, and HBD-3, are important elements of the innate immune response and involved in modulation of the adaptive immunity, and they also play an important role in cutaneous defense against Mycobacterium tuberculosis.

METHODSThe fresh skin tissues and paraffin-embedded biopsy samples from three cutaneous tuberculosis, two tuberculids, and ten healthy individuals were collected. The expressions of LL-37, HBD-2, and HBD-3 mRNA in the lesions of three cutaneous tuberculosis and two tuberculids were detected by quantitative real-time polymerase chain reaction; the protein expressions were detected by immunohistochemistry and Western blotting methods.

RESULTSThe expressions of LL-37 mRNA and protein in the lesions of cutaneous tuberculosis and tuberculids were similar to that of normal skin. The expression of HBD-2 mRNA had an increasing trend in the lesions of cutaneous tuberculosis and tuberculids compared with that of normal skin; however, the expression of HBD-2 protein in the lesions of cutaneous tuberculosis had a decreasing trend compared with that of normal skin, and the expression of HBD-2 protein in the lesions of tuberculids was similar to that of normal skin. The expressions of HBD-3 mRNA and protein in lesions of cutaneous tuberculosis and tuberculids were similar to that of normal skin.

CONCLUSIONSOur study indicated that the expression of HBD-2 and HBD-3 mRNA and protein in lesions of cutaneous tuberculosis may be not consistent with that of tuberculids. However, an inherent limitation of the present study was that the sample size was small, and the roles and regulation mechanisms of LL-37, HBD-2, and HBD-3 in cutaneous tuberculosis and tuberculids need to be further investigated.

Adult ; Aged ; Antimicrobial Cationic Peptides ; genetics ; Female ; Humans ; Male ; Middle Aged ; RNA, Messenger ; analysis ; Tuberculosis, Cutaneous ; metabolism ; beta-Defensins ; genetics

This study was aimed to evaluate the cyto-compatibility of PGLA film for periodontal guided tissue regeneration (GTR) and their degradable products. Different extraction temperature, time and ratio were used to assess the cell relative growth rate (RGR) for PGLA. The degradable solution were brought into contact with cultured cells in vitro to observe the effects of cytotoxicity at 2, 4, 6, 8 and 10 weeks. The results showed when the extraction ratio was 0.1 g/ml, the extraction time has no effects on cytotoxicity at 37 degrees C. When the ratio was 0.1 cm2/ml, slight cytotoxic reaction appeared with the increase of extraction temperature (50 degrees C or 70 degrees C). When the extraction ratio was 0.5 cm2/ml in contract with the degradable solution at 37 degrees C for 72 h, the cell growth rate decreased. When the ratio was 6 cm2/ml, the cytotoxicity existed in some degree even if the temperature was at 37 degrees C for 24 h. After 2-4 w, the degradable solution had no obvious toxic effects on cells. However, the RGR gradually decreased as the degradation period increased. In conclusion, the effects of the extraction temperature, time, ratio and the degradation products accumulating in solution on RGR may exist. PGLA film has a good cytocompatibility.
Animals ; Antimicrobial Cationic Peptides ; metabolism ; pharmacology ; Biodegradation, Environmental ; Cell Division ; drug effects ; Cells, Cultured ; Guided Tissue Regeneration ; Materials Testing ; Mice