No abstract available.
Humans ; Hyperthyroidism* ; Procollagen*

No abstract available.
Humans ; Kidney Diseases* ; Kidney* ; Procollagen*

BACKGROUND: Many treatment modalities for wrinkle reduction have been developed in the field of dermatology. Hydroxyproline plays a critical role in stabilizing the triple helix of collagen. The triple-helical conformation gives collagen most of its unique properties and is essential for normal fibrillogenesis. OBJECTIVE: This study was performed to investigate the effect of hydroxyproline on the improvement of wrinkles in vitro and in vivo. METHODS: Cultured fibroblasts and 25 human volunteers were used for in vitro and in vivo studies respectively. Hydroxyproline was administered to a fibroblast culture system and was also applied to periorbital wrinkle lesions twice daily for 12 weeks. The effect of hydroxyproline was examined by using an image analysis system with skin replica, and subjective and objective assessment of wrinkles were evaluated. RESULTS: With the in vitro study, the number of cultured fibroblasts did not increase in the 10(-4), 10(-6) and 10(-8)microgram/ ml hydroxyproline groups compared to the control groups. Procollagen Type 1 C-peptide of cultured fibroblasts did increase in the 10(-8)microgram/ml hydroxyproline group compared to the control group (p<0.05). With the in vivo study, there was a significant decrease in wrinkles at 8 and 12 weeks after application in the 0.5% hydroxyproline applied group compared to the control group (p<0.001). In the subjective visual assessment by the investigator and the subjects at 8 and 12 weeks after application, the 0.5% hydroxyproline treated group showed a significant improvement of wrinkles and more personal satisfaction than the control group (p<0.05). CONCLUSION: 0.5% hydroxyproline had an effect in vivo and in vitro on wrinkle improvement. It is suggested that hydroxyproline might be a candidate compound for treatment or reduction of wrinkles.
C-Peptide ; Collagen ; Dermatology ; Fibroblasts ; Healthy Volunteers ; Humans ; Hydroxyproline* ; Personal Satisfaction ; Procollagen ; Research Personnel ; Skin

Scleroderma is a connective tissue disease characterized by excessive accumulation of collagen in skin and visceral organs due to increased collagen production by scleroderma fibroblasts. The basic etiology of this collagen accumulation is not known. We examined the expression of various extracellular matrix genes in cultured fibrolasts using Northern blot and slot-blot hybridization. The scleroderma fibroblasts exhibited characteristic mRNA size of extracellular matrix genes and prominanty increased type I and III procollagen mRNAs levels compared to control fibroblasts cultures from univolved skin. The ratios of type I /IE procollagen in scleroderma cell lines were not so much different to the controls. These results indicate that increases of collagen biosynthesis in scleroderma can be a accounted for, at least in part, by an increased content of transcriptable type I and type JE procollagen mRNAs, both.
Blotting, Northern ; Cell Line ; Collagen ; Connective Tissue Diseases ; Extracellular Matrix ; Fibroblasts* ; Procollagen ; RNA, Messenger ; Skin

PURPOSE: To investigate the effect of human serum on corneal epithelial cells. METHODS: Changes of corneal epithelial cells were evaluated after 1, 4, 12, and 24 hours (hrs) of exposure to various concentrations of human serum (3, 5, 8, and 16%). Cellular metabolic activity and the extent of cellular damage were measured. Effect of human serum on cell migration was also examined. Concentration of procollagen type-I COOH-terminal peptide (PIP), epidermal growth factor (EGF), and laminin after exposure to human serum was further observed. RESULTS: In every concentration of human serum, metabolic activity of the corneal epithelial cells temporarily decreased at 4 hrs of exposure and recovered to baseline levels afterward. With the same exposure time, there was no statistically significant difference in metabolic activity between the human serum-exposed group and the control group. Cellular toxicity of human serum exhibited a time- and dose-dependent relationship. Cellular migration was observed after 24 hrs of exposure to 5% concentration of human serum and after 12 hrs of exposure to 8% and 16% concentration of human serum. The PIP, EGF, and laminin titers increased in time- and dose-dependent manners. CONCLUSIONS: Human serum does not decrease the metabolic activity of corneal epithelial cells as the concentration and exposure time increase, but it can induce cytotoxicity. Considering cellular migration, a serum concentration of 5% or higher should be used.
Cell Movement ; Epidermal Growth Factor ; Epithelial Cells* ; Epithelium, Corneal ; Humans* ; In Vitro Techniques* ; Laminin ; Procollagen

Recent studies have demonstrated that tumor necrosis factor-alpa(TNF-alpa) decreased production of type I and III procollagens and increased production of collagenase in cultured human dermal fibroblasts. The purpose of this study was to examine the effect of TNF-alpa on the level of expression of type I procollagen, collagenase mRNA in hypertrophic scar and keloid fibroblasts in culture. The cultured fibroblasts from normal skin, hypertrophic scar and keloid were exposed to 0, 1, 10, and 100 ng/ml of TNF-alpa for 24 hours. Then, type I procollagen mRNA and collagenase mRNA were measured by quantitative RT-PCR and quantified by computerized densitometry(TINA). In normal skin fibroblasts, TNF-alpa significantly decreased the level of type I procollagen mRNA and increased collagenase mRNA. The maximal inhibition for type I procollagen mRNA was noted at 100 ng/ml of TNF-alpa and maximal enhancement for collagenase mRNA was noted at 100ng/ml of TNF-alpa. In hypertrophic scar fibroblasts, TNF-alpa significantly decreased the level of type I procollagen mRNA and increased collagenase mRNA. The maximal inhibition for type I procollagen mRNA was noted at 100 ng/ml of TNF-alpa which was the same as normal skin fibroblasts but there were no significant differences among TNF-alpa treated groups for collagenase mRNA. In keloid fibroblasts, TNF-alpa also significantly decreased the level of type I procollagen mRNA and increased collagenase mRNA. The maximal inhibition for type I procollagen mRNA was noted at 100 ng/ml of TNF-alpa which was the same as normal skin and hypertrophic scar fibroblasts but there were no significant differences among TNF-alpa treated groups for collagenase mRNA. These results strongly suggested that TNF-alpa might have a role in preventing progression of fibroproliferative disease, such as hypertrophic scar or keloid, and that the most effective concentration of TNF-alpa was found in 100 ng/ml.
Cicatrix, Hypertrophic* ; Collagen Type I* ; Collagenases* ; Fibroblasts* ; Gene Expression* ; Humans ; Keloid* ; Necrosis* ; Procollagen ; RNA, Messenger ; Skin

Forkhead Transcription Factors ; genetics ; Gene Expression Regulation ; Humans ; Procollagen ; genetics ; Transcription, Genetic

OBJECTIVETo investigate the correlation between serum levels of follicle-stimulating hormone (FSH) and total procollagen I N-terminal propeptide (TP1NP) in perimenopausal women.

METHODSTotal 274 women aged 33~60 y with perimenopausal period were enrolled in this study. Serum levels of FSH and TP1NP were detected by electrochemiluminescence.

RESULTSIn 274 perimenopausal women, the average level of TP1NP was (48.99±20.31) ng/mL, which was positively correlated with FSH level (r=0.159, P=0.009). In 40-50 age group, TP1NP level in women with FSH<40 mIU/mL was lower than that in those with FSH≥40mIU/mL [(35.05±18.11) ng/mL vs (51.33±24.67) ng/mL; t=-2.954, P=0.004]. However, in <40 and 50-60 age groups, there were no significant differences in TP1NP levels between patients with FSH<40 mIU/mL and those with FSH≥40 mIU/mL (t=-0.063, P=0.950; t=1.177, P=0.242). Multiple linear regression analysis showed that standardized coefficients of age variable was 0.047 (P=0.448) and standardized coefficients of FSH variable was 0.146 (P=0.019).

CONCLUSIONTP1NP levels showed a certain correlation with FSH in perimenopausal women, especially for women aged 40-50, indicating that high FSH levels may be important factors for osteoporosis in postmenopausal women.

Adult ; Female ; Follicle Stimulating Hormone ; blood ; Humans ; Middle Aged ; Peptide Fragments ; blood ; Perimenopause ; blood ; Procollagen ; blood

Overexpression of procollagen gene can cause the extraordinary increase of collagen's synthesis and therefore lead to the keloid and hypertrophic scar. To utilize ribozyme to suppress the expression of procollagen genes, a eukaryotic expression recombinant plasmid containing a dual-ribozyme gene against alpha 1 (I) and alpha 1 (III) procollagen genes was constructed. The ribozyme from in vitro transcription was incubated with target transcripts from recombinant plasmids which separately contained the fragments of the second exons of pro alpha 1 (I) and pro alpha 1 (III) collagen genes under various experimental conditions. The results showed that the dual-ribozyme could efficiently catalyze the specific cleavage of the target RNAs at 37 degrees C, 42 degrees C, 50 degrees C and Mg2+ concentration from 10 mmol/L to 20 mmol/L. This work provided a basis for further study on the ribozyme to suppress the expression of procollagen genes and control the cicatrization.
Base Sequence ; Exons ; Molecular Sequence Data ; Procollagen ; genetics ; RNA ; metabolism ; RNA, Catalytic ; genetics ; metabolism ; Temperature

Pterygium, a disease of unknown origin and pathogennesis, is a chronic condition characterized by the encroachment of triangular portion of the bulbar conjunctiva onto the cornea. We have studied the expression of extracellular matrix genes and oncogenes in cultured pterygium using Northernm dot, and slot blot hybridizations. Northern hybridization with total RNA isolated from passaged (4-8 passages) cultures demonstrated expression of genes for alpha1(I) and alpha1(III) procollagen, fibronectin, and c-Ha-ras, but no expression of gene for c-myc was observed. The pterygium exhibited significantly increased expression of alpha1(I) and alphal(III) procollagen genes when compared with normal control cells(p<0.01). And We observed there were no differences between pterygium and normal control cells in the expression of genes for fibronectin and c-Ha-ras. According to these results we thought that the causes of pterygium may be related to the increased expression of alpha1(I) and alphal(III) procollagen genes but may not be related to c-Ha-ras, c-myc, and fibronectin genes.
Conjunctiva ; Cornea ; Extracellular Matrix* ; Fibroblasts* ; Fibronectins ; Genes, myc* ; Oncogenes ; Procollagen ; Pterygium ; RNA