三种抗肝纤维化药物成本—效果分析

目的:探索不同抗肝纤维化药物治疗方案对肝纤维化的经济效果。方法:选择45例轻、中度肝纤维化患者,随机分组,给予不同的治疗方案(L1大黄蟅虫丸,L2安络化纤丸,L3复方鳖甲软肝片),选用药物经济学成本—效果分析方法进行评价。结果:L1,L2,L3三种方案总成本分别为210元,528.6元,718.5元。其效果分别为2.48,5.92,7.95。结论:L1方案为治疗最佳方案。

Regulation of activin receptor-interacting protein 2 expression in mouse hepatoma Hepa1-6 cells and its relationship with collagen type Ⅳ

AIM： To investigate the regulation of activin receptor-interacting protein 2 （ARIP2） expression and its possible relationships with collagen type Ⅳ （collagen Ⅳ） in mouse hepatoma cell line Hepal-6 cells. METHODS： The ARIP2 mRNA expression kinetics in Hepal-6 cells was detected by RT-PCR, and its regulation factors were analyzed by treatment with signal transduction activators such as phorbol 12-myristate 13-acetate （PMA）, forskolin and A23187. After pcDNA3- ARIP2 was transfected into Hepal-6 cells, the effects of ARIP2 overexpression on activin type Ⅱ receptor （ActRⅡ） and collagen Ⅳ expression were evaluated. RESULTS： The expression levels of ARIP2 mRNA in Hapel-6 cells were elevated in time-dependent manner 12 h after treatment with activin A and endotoxin LPS, but not changed evidently in the early stage of stimulation （2 or 4 h）. The ARIP2 mRNA expression was increased after stimulated with signal transduction activators such as PMA and forskolin in Hepal-6 cells, whereas decreased after treatment with A23187 （25.3% ± 5.7% vs 48.1% ± 3.6%, P 〈 0.01）. ARIP2 overexpression could remarkably suppress the expression of ActRⅡA mRNA in dose-dependent manner, but has no effect on ActRⅡB in Hepal-6 cells induced by activin A. Furthermore, we have found that overexpression of ARIP2 could inhibit collagen Ⅳ mRNA and protein expressions induced by activin A in Hapel-6 cells. CONCLUSION： These findings suggest that ARIP2 expression can be influenced by various factors. ARIP2 may participate in the negative feedback regulation of signal transduction in the late stage by affecting the expression of ActRIIA and play an important role in regulation of development of liver fibrosis induced by activin.

Idiopathic fistula-in-ano

Fistula-in-ano is the most common form of perineal sepsis.Typically,a fistula includes an internal opening,a track,and an external opening.The external opening might acutely appear following infection and/or an abscess,or more insiduously in a chronic manner.Management includes control of infection,assessment of the fistulous track in relation to the anal sphincter muscle,and finally,definitive treatment of the fistula.Fistulotomy was the most commonly used mode of management,but concerns about post-fistulotomy incontinence prompted the use of sphincter preserving techniques such as advancement flaps,fibrin glue,collagen fistula plug,ligation of the intersphincteric fistula track,and stem cells.Many descriptive and comparative studies have evaluated these different techniques with variable outcomes.The lack of consistent results,level I evidence,or long-term follow-up,as well as the heterogeneity of fistula pathology has prevented a definitive treatment algorithm.This article will review the most commonly available modalities and techniques for managing idiopathic fistula-in-ano.

Extraction and Isolation of Type Ⅰ,Ⅲ and Ⅴ Collagens and Their SDS-PAGE Analyses

Type Ⅰ Ⅲ and Ⅴ collagens were extracted from bovine dermis and cornea by using pepsin treatment in acetic acid solution, followed by salt precipitation and dialysis, to purify and isolate each type of collagens. The preparation process was analyzed by using sodium dodecyl sulfate polyacrylamide gel electrophoresis （SDS-PAGE）. A reducing agent, 2-mercaptoethanol, was used to remove disulfide bonds and analyze the structure of the bonds involved between α chains in some types of collagens. The use of delayed reducing methods resulted in the difference between α1 （Ⅲ） and α1 （ Ⅰ ） chains in a mixture containing type Ⅰ and Ⅲ collagens. The structure of disulfide bonds among α chains exists potentially in type V collagen prepared from the pepsin-treatment extraction at 4 ℃, which differs from type Ⅲ collagen in relation to the locations of disulfide bonds. Compared with pepsin-treated collagen at 4 ℃, the relative molecular weights of α1 （V） and α2 （V） chains treated at room temperature decrease by 4.6% and 6.0%, respectively. It is concluded that type Ⅰ Ⅲ and Ⅴ collagens can be prepared from bovine dermis and cornea by the use of pepsin treatment, salt precipitation and dialysis. The interchain disulfide bonds lie potentially near the edges of termini of type V collagen molecules in extracellular matrix, and a small number of interchain crosslinks exist in type V collagen.

Characterization and antioxidant activities of marine pepsin soluble collagen from the skin of yellow goosefish Lophius litulon

Characteristics and antioxidant activities of pepsin-soluble collagen （PSC） from yellow goosefish （Lophius litulon） skins were investigated. PSC was characterized as a type I collagen, and its imino acid content was 193 residues/1 000 residues. PSC＇s denaturation temperature was -17.56℃ and Fourier transform infrared spectra confirmed the presence of triple helices. Solubility analysis showed good solubility at acidic pH （1-6） or low NaCl concentrations （≤2%）. PSC showed scavenging activity against hydroxyl radicals and superoxide anions in a concentration-dependent manner. Furthermore, PSC could protect D-galactose-induced skin aging by significantly controlling malondialdehyde formation and improving the activity of superoxide dismutase, glutathione peroxidase, catalase, glutathione, and hydroxyproline. PSC may be a promising antioxidant in appropriate applications.

Extraction of TypeⅤCollagen From Bovine Cornea and Its Structural Analysis

We used bovine cornea as starting material, pepsin treatment in acetic acid solution to extract the mixture of type I and V collagens, and salt precipitation and dialysis to purify and isolate each type of the collagens. The preparation was analyzed using sodium dodecyl sulphate polyacrylamide gel electrophoresis. 2-mercaptoethanol used as reducing agent cut off the disulfide bonds, which was utilized to analyze the structure of disulfide bonds involved between α chains in some types of collagens. At the same time, we discovered that the structure of disulfide bonds among α chains potentially existed in the type V collagen prepared from the pepsin-treatment extraction at 4℃. Through quantitative analysis, we obtained that, compared with those pepsin-treated at 4℃, the relative molecular weights of α1 （V） and α 2 （V） subunits pepsin-treated at room temperature decreased by 4.6% and 6.0%, respectively. It is concluded that type V collagen can be prepared from bovine coruea by use of pepsin treatment, salt precipitation and dialysis. The interchain and/or intermolecular disulfide bonds potentially lie near the edges of termini of type V collagen molecules existing in extracellular matrix, and there are few of the intermolecular and/or intramolecular crosslinks formed by lysine or hydroxylysine or histidine residues in type V collagen.