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1.
Annals of Dermatology ; : 315-320, 2013.
Article in English | WPRIM | ID: wpr-131880

ABSTRACT

BACKGROUND: The fibrous proteins of extracellular matrix (ECM) produced by dermal fibroblast contributes to the maintenance of connective tissue integrity. OBJECTIVE: This study is carried out to identify the bioactive ingredient from natural products that enhances ECM production in dermal fibroblasts. METHODS: Bioassay-directed fractionation was used to isolate the active ingredient from natural extracts. The effects of rasatiol (isolated from Raphanus sativus) on ECM production in primary cultured human dermal fibroblasts was investigated by enzyme linked immunosorbent assay and western blot analysis. RESULTS: Rasatiol accelerated fibroblast growth in a dose-dependent manner and increased the production of type 1 collagen, fibronectin and elastin. Phosphorylation of p42/44 extracellular signal-regulated kinase, p38 mitogen-activated protein kinase, and Akt was remarkably increased by rasatiol, indicating that enhanced ECM production is linked to the activation of intracellular signaling cascades. CONCLUSION: These results indicate that rasatiol stimulates the fibrous components of ECM production, and may be applied to the maintenance of skin texture.


Subject(s)
Humans , Biological Factors , Blotting, Western , Collagen Type I , Connective Tissue , Elastin , Enzyme-Linked Immunosorbent Assay , Extracellular Matrix , Fibroblasts , Fibronectins , Phosphorylation , Phosphotransferases , Protein Kinases , Raphanus , Scleroproteins , Skin
2.
Annals of Dermatology ; : 315-320, 2013.
Article in English | WPRIM | ID: wpr-131877

ABSTRACT

BACKGROUND: The fibrous proteins of extracellular matrix (ECM) produced by dermal fibroblast contributes to the maintenance of connective tissue integrity. OBJECTIVE: This study is carried out to identify the bioactive ingredient from natural products that enhances ECM production in dermal fibroblasts. METHODS: Bioassay-directed fractionation was used to isolate the active ingredient from natural extracts. The effects of rasatiol (isolated from Raphanus sativus) on ECM production in primary cultured human dermal fibroblasts was investigated by enzyme linked immunosorbent assay and western blot analysis. RESULTS: Rasatiol accelerated fibroblast growth in a dose-dependent manner and increased the production of type 1 collagen, fibronectin and elastin. Phosphorylation of p42/44 extracellular signal-regulated kinase, p38 mitogen-activated protein kinase, and Akt was remarkably increased by rasatiol, indicating that enhanced ECM production is linked to the activation of intracellular signaling cascades. CONCLUSION: These results indicate that rasatiol stimulates the fibrous components of ECM production, and may be applied to the maintenance of skin texture.


Subject(s)
Humans , Biological Factors , Blotting, Western , Collagen Type I , Connective Tissue , Elastin , Enzyme-Linked Immunosorbent Assay , Extracellular Matrix , Fibroblasts , Fibronectins , Phosphorylation , Phosphotransferases , Protein Kinases , Raphanus , Scleroproteins , Skin
3.
Journal of the Philippine Dermatological Society ; : 10-13, 2013.
Article in English | WPRIM | ID: wpr-632961

ABSTRACT

Hair has a significant physical, psychological and social impact on an individual's daily life and well being. Understanding the basic structure and the factors that affect hair fiber integrity leads to better handling and care of our hair.Hair is a slowly renewable protein fiber which grows at a rate of about 1 cm per month. Once hair emerges from the scalp, it is a non living matter.' From the scalp exit point to the distal portion of the hair strand, any injury to the hair structure is irreversible. Subjecting the hair fiber to the least amount of dailytrauma helps to minimize any damage to the hair fiber.Hair fiber is mainly keratin protein and a small amount of lipid and other components. It is made up of an inner cortex, medulla and an external cuticle layer. The hair cuticle is made up of overlapping cell layers (approximately 5-10 layers) which covers the entirehair fiber. Each cuticular cell has inner layers (A layer and the endocuticle), outer sublamellar structures and an outer membrane, containing lipids mainly 18-methyl eicosanoic acid which imparts a hydrophobic nature to the cuticle.' The condition of the cuticle mainly determines the cosmetic appearance of the hair and being the most external layer, is the part of the hair most vulnerable to the effects of daily grooming, cosmetic treatments and the environment.The cortex has a winded helical configuration of long microfibers linked to each other to form larger structures which gives the hair its tensile strength and elasticity." The inner location of the cortex makes it less prone to damage thus injury to the cortex signifies more severe damage to the outer cuticles allowing extension to the inner cortex. The medulla is the innermost cylindrical part of the hair fiber whose function is not as clear as the other two structures.


Subject(s)
Humans , Male , Female , Eicosanoic Acids , Elasticity , Grooming , Hair , Keratins , Lipids , Scalp , Scleroproteins , Tensile Strength
4.
Medical Journal of Reproduction and Infertility. 2006; 7 (3): 198-208
in Persian | IMEMR | ID: emr-79144

ABSTRACT

Leukocytes and defective or dead spermatozoa in human semen are a source for the production of reactive oxygen species [ROS] and subsequent injury to intact sperms. Enzymatic and non-enzymatic defensive mechanisms in semen detoxify these compounds. Glutathione peroxidase-4 [GPX-4 or PHGPX] is a major selenoprotein in sperm and it is one of the enzymatic mechanisms that play multiple roles during spermatogenesis. Some of these roles are formation of the mitochondrial capsule, hydroperoxide detoxification and sperm chromatin condensation. Any decrease in the enzyme activity or content, may create disorders in spermatogenesis and sperm fertilizing ability. Considering defects in the expression of the enzyme gene or presence of mutations which may cause decreases in PHGPX activity or content, this study was carried out to identify a number of important mutations in GPX-4 gene by PCR-RFLP method in Iranian infertile men. This study was performed on 128 Iranian men who had been referred to Avesina Infertility Clinic, including 74 infertile men with defective sperm parameters, 18 normozoospermic and 36 fertile subjects as controls. Mean +/- SD for sperm parameters were determined. Genomic DNA was extracted using salting out procedure from peripheral blood leukocytes. PCR-RFLP was done by two sets of primers with 237 bp and 148 bp PCR products that were designed for 1A and 4 exons of GPX-4 gene covering nucleotides of+6 [C[right wards arrow]T], +17 [G[right wards arrow]A], +1725 [G[right wards arrow]A] by Mwol, PshAI and SatI enzymes. Digestion of a 237 bp intact PCR product by Mwol generates two fragments [151 bp and 86 bp]. When a mutation occurs in the restriction site +6 [C[right wards arrow]T], the enzyme would not recognize the sequence, therefore 237 bp segment remains undigested. Treatment of 237 bp segment with PshAI generates two fragments [161 bp and 76] in the intact gene but the same enzyme can not digest 237 bp segment when a mutation occurs in the restriction site +17 [G [right wards arrow] A]. Ultimately, digestion of 148 bp intact segment with SatI generates two fragments [108 bp and 40 bp] but when a mutation occurs in the restriction site +1725 [G [right wards arrow] A], the enzyme will not recognize the sequence; therefore 148 bp segment remains undigested. Enzymatic digestion evaluations of 237 bp and 148 bp segments in all participants revealed that neither of the examined mutations existed in GPX-4 gene. According to the results of this study, it is determined that the prevalence of these mutations in Iranian infertile men is probably low and it may have no association with the etiology of the disorder affecting sperm parameters. Hence, a study with a larger number of patients is suggested to determine the exact prevalence of these and other mutations of the gene in Iranian infertile men


Subject(s)
Humans , Male , Polymorphism, Genetic , Glutathione Peroxidase , Reactive Oxygen Species , Scleroproteins , Spermatozoa , Mutation/genetics , Prevalence
5.
Korean Circulation Journal ; : 426-439, 1993.
Article in Korean | WPRIM | ID: wpr-115428

ABSTRACT

BACKGROUND: It has been known that arteries of hypertensive animals and patients are generally thicker and more rigid than those of normal subjects, resulting from the morphological changes induced by an increased stress on the vessel wall. Factors proposed to be responsible for these changes are smooth muscle hypertrophy, increased amount of collagen, hyperplasia of smooth muscle cell and changes in cross-linkages of the fibrous proteins. The present study was conducted to define whether enalapril, a converting enzyme inhibitor of angiotensin II generation from angiotensin I, can restore the structural alterations of aortic media in spontaneously hypertensive rat(SHR). METHODS: For this purpose, SHR were treated for 22 weeks with 2mg/kg/day enalapril and morphologic changes were compared between enalapril-treated SHR and normotensive Wistar-Kyoto rats. RESULTS: The increased thickness of the aortic media in SHR was reduced and intervening elastic laminae were narrowed by enalapril treatment. Subcellular analysis of cytoplasmic composition and nucleus in the aorta of hypertensive rats revealed some modification with enalapril. Some irregularly arranged collagen fibrils in aortic media of SHR were regularly distributed and the periodic bands of the fibrils which were the fragmented were clearly apparent by enalapril treatmed SHR group. CONCLUSIONS: From the above experimental results, it is concluded that subcellular changes of smooth muscle cells and collage fibrils of aortic media in SHR could be repaired by long-term treatment with enalapril.


Subject(s)
Animals , Humans , Rats , Angiotensin I , Angiotensin II , Aorta , Arteries , Collagen , Cytoplasm , Enalapril , Hyperplasia , Hypertrophy , Muscle, Smooth , Myocytes, Smooth Muscle , Rats, Inbred SHR , Scleroproteins
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