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Skin Collagen (skin + collagen)
Selected AbstractsComplete primary structure of rainbow trout type I collagen consisting of ,1(I),2(I),3(I) heterotrimersFEBS JOURNAL, Issue 10 2001Masataka Saito The subunit compositions of skin and muscle type I collagens from rainbow trout were found to be ,1(I),2(I),3(I) and [,1(I)]2,2(I), respectively. The occurrence of ,3(I) has been observed only for bonyfish. The skin collagen exhibited more susceptibility to both heat denaturation and MMP-13 digestion than the muscle counterpart; the former had a lower denaturation temperature by about 0.5 °C than the latter. The lower stability of skin collagen, however, is not due to the low levels of imino acids because the contents of Pro and Hyp were almost constant in both collagens. On the other hand, some cDNAs coding for the N-terminal and/or a part of triple-helical domains of pro,(I) chains were cloned from the cDNA library of rainbow trout fibroblasts. These cDNAs together with the previously cloned collagen cDNAs gave information about the complete primary structure of type I procollagen. The main triple-helical domain of each pro,(I) chain had 338 uninterrupted Gly-X-Y triplets consisting of 1014 amino acids and was unique in its high content of Gly-Gly doublets. In particular, the bonyfish-specific ,(I) chain, pro,3(I) was characterized by the small number of Gly-Pro-Pro triplets, 19, and the large number of Gly-Gly doublets, 38, in the triple-helical domain, compared to 23 and 22, respectively, for pro,1(I). The small number of Gly-Pro-Pro and the large number of Gly-Gly in pro,3(I) was assumed to partially loosen the triple-helical structure of skin collagen, leading to the lower stability of skin collagen mentioned above. Finally, phylogenetic analyses revealed that pro,3(I) had diverged from pro,1(I). This study is the first report of the complete primary structure of fish type I procollagen. [source] Characteristics of skin aging in Korean men and womenINTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Issue 1 2005J. H. Chung Introduction Korea is located between Japan and Mainland China. The people of these three countries have similar appearances and it is difficult to differentiate between them. Although the population of Asia is more than half of the total population of the Earth, the inherent characteristics of Asian skin have not been well investigated. Commercial markets for cosmetics and drugs for photoaged skin are rapidly expanding in many Asian countries. Therefore, many investigators in the field of dermatology and cosmetology have become interested in brown Asian skin. Clinical characteristics of skin aging and photoaging in Asians Skin aging can be divided into two basic processes: intrinsic aging and photoaging [1]. Intrinsic aging is characterized by smooth, dry, pale, and finely wrinkled skin, whereas photoaging, which indicates premature skin aging in chronically photodamaged skin, is characterized by severe wrinkling and irregular pigmentation. The pattern of wrinkling in Asians seems to differ from that in Caucasians. Asians have coarser, thicker and deep wrinkles, particularly in the forehead, perioral and Crow's foot areas. In contrast, Caucasians usually have relatively fine cheek and Crow's foot wrinkles. The reasons for these differences are not known and need further investigation. There are racial, ethnic and genetic differences, and differences of skin structure and function, between the brown skin of Asians and the white skin of Caucasians. As Asian skin is more pigmented, acute and chronic cutaneous responses to UV irradiation differ from those in white skin. Many people believe, based on clinical impressions, that the main process of photoaging in Asians involves pigmentary changes, rather than wrinkling. However, no study has been performed to confirm this belief. Risk factors for skin wrinkles and their relative risks in Korean skin [2] Various factors such as age, sun-exposure, and smoking are known to be important risk factors for wrinkles. However, the relative risks of each factor on wrinkles in the brown skin of Asians have not been investigated, and they could differ from those in Caucasians. An evaluation system for skin wrinkling is necessary for Asian skin [3]. Thus, we developed an eight-point photographic scale for assessing wrinkles in both Korean genders [2]. This scale can probably be applied to the populations of other Asian countries, at least to the Japanese and Chinese. The pattern of wrinkles in both genders appears to be similar. Age Age is an important risk factor for wrinkling in Asians, as in Caucasians. Korean subjects in their 60s showed a 12-fold increased risk of wrinkling, while subjects in their 70s have a 56-fold increased risk compared with young age group. UV light It is well known that the UV component in sunlight can cause and accelerate photoaging. The pigmented skin of Asian may better protect skin from acute and chronic UV damage. However, we found a strong association between sun-exposure and the development of wrinkling in Koreans. It was found that sun exposure of more than 5 h per day was associated with a 4.8-fold increased risk in wrinkling versus less than 2 h of sun-exposure in Koreans. Estrogen deficiency Korean females have more wrinkles than men, after controlling for age, sun exposure, and smoking, it was found that they have a 3.6-fold increased risk of developing wrinkles than their male counterparts [2]. It has also been reported, that the relative risk for wrinkling in women is higher than in men as for in white Caucasians [4]. The reason why women show more wrinkles remains to be determined. It is possible that a reduction in skin collagen because of estrogen deficiency in postmenopausal woman may aggravate wrinkling severity. Korean women with more than 10 years since menopause showed a 3.9-fold higher risk of wrinkling than the women 5 years of beyond menopause [5]. We demonstrated that women with a history of HRT have a significantly lower risk, more specifically, one fifth of the risk of facial wrinkling relative to those who had no history of HRT. Interestingly, we found that wrinkle severity significantly increased with an increasing number of full term pregnancies. The relative risk for severe wrinkling is increased by approximately 1.8-fold per full term pregnancy. Smoking It is known that smoking causes skin wrinkling in Caucasians, and that it plays no role in Blacks [6, 7]. Koreans with have a smoking history of more than 30 pack years showed a more than 2.8-fold increased risk of wrinkles [2]. The relative risks of wrinkles associated with a 30,50 pack-years history of smoking were 2.8- and 5.5-fold, respectively. Dyspigmentation in Asian skin To follow pigmentary changes, six photographic standards for both genders were developed for Korean skin, to produce a 6-point scale [2, 8]. Hyperpigmented spots, mostly lentigines, were prominent among women, while seborrheic keratosis tended to be more prominent in men. Seborrheic keratosis in Korean men Seborrheic keratoses (SKs) are benign cutaneous tumors. They have diverse clinical and histopathological appearances and are very common in the elderly (over 50 years old). The etiology of SKs is not well understood, although patients with a great number of lesionsshow a familial trait with an autosomal dominant pattern, and human papilloma virus has been suggested as possible cause because of verrucous appearance of the lesions. Exposure to sunlight has been suggested to be a risk factor for SKs. However, there is still some debate in terms of the role of sunlight. Recently, we have investigated the clinical characteristics of SKs and relationship between SKs and sunlight exposure in Korean males [9]. The prevalence of SKs in Koreans increases with age; it rose from 78.9% at 40 years, to 93.9% at 50 years and 98.7% in those over 60 years. Exposed areas, i.e. the face, neck and dorsum of the hands, demonstrate a significant increase in the prevalence of SKs by decade, whereas partly exposed areas, although SKs tended to increase in prevalence with age, this trend was not significant. When the estimated body surface area (BSA) is taken into account, the number of SKs on both the face and dorsum of the hands (0.51 ± 0.08 per 1% BSA) was over-represented compared with the trunk. SKs were also concentrated on the neck (0.38 ± 0.07 per 1% BSA) and in the V-area (0.47 ± 0.09 per 1% BSA). Outer forearms also showed 3-fold more SKs per unit area than neighboring arms and inner forearms, which are classified as partly exposed area (0.09 ± 0.02, 0.03 ± 0.01, respectively). The total area covered by SKs on exposed area also became significantly larger with aging than on intermittently exposed areas. These results indicate that exposure to sunlight might be related to SK growth. Our results indicated that excessive sun exposure is an independent risk factor of SKs. After controlling for age, smoking, and skin type, subjects with a sun exposure history of more than 6 hours per day showed a 2.28-fold increased risk of having severe SKs (n , 6) compared with those exposed for less that 3 h per day. These findings indicated that sun-exposure may play an important role in SK development. In summary, SKs are very common in Korean males and represent one of the major pigmentary problems. SKs concentrate on exposed skin, especially on the face and dorsum of the hands. Both age and lifetime cumulative sunlight exposure are important contributing factors and may work in a synergistic manner. Conclusion Many people tend to believe that wrinkles are not a prominent feature of Asian photoaged skin, and that dyspigmentation is a major manifestation in Asian skin. Contrary to this impression, wrinkling is also a major problem in the photoaged skin of Asians, and Korean people showing severe pigmentary changes usually tend to have severe wrinkles. In conclusion, the wrinkling patterns and pigmentary changes of photoaged skin in East Asians differ from those of Caucasians, and the relative risks of aggravating factors may be different from those of Caucasian skin. References 1.,Gilchrest, B.A. Skin aging and photoaging: an overview. J. Am. Acad. Dermatol. 21, 610,613 (1989). 2.,Chung, J.H. et al. Cutaneous photodamage in Koreans: influence of sex, sun exposure, smoking, and skin color. Arch. Dermatol. 137, 1043,1051 (2001). 3.,Griffiths, C.E. et al. A photonumeric scale for the assessment of cutaneous photodamage. Arch. Dermatol. 128, 347,351 (1992). 4.,Ernster, V.L. et al. Facial wrinkling in men and women, by smoking status. Am. J. Public Health. 85, 78,82 (1995). 5.,Youn, C.S. et al. Effect of pregnancy and menopause on facial wrinkling in women. Acta Derm. Venereol. 83, 419,424 (2003). 6.,Kadunce, D.P. et al. Cigarette smoking: risk factor for premature facial wrinkling. Ann. Intern. Med. 114, 840,844 (1991). 7.,Allen, H.B., Johnson, B.L. and Diamond, S.M. Smoker's wrinkles? JAMA. 225, 1067,1069 (1973). 8.,Chung, J.H. Photoaging in Asians. Photodermatol. Photoimmunol. Photomed. 19, 109,121 (2003). 9.,Kwon, O.S. et al. Seborrheic keratosis in the Korean males: causative role of sunlight. Photodermatol. Photoimmunol. Photomed. 19, 73,80 (2003). [source] CHARACTERIZATION AND COMPARISON OF COLLAGENS EXTRACTED FROM THE DIGESTIVE TRACT AND SKIN OF A JAPANESE AMBERJACK SERIOLA QUINQUERADIATAJOURNAL OF FOOD BIOCHEMISTRY, Issue 6 2009MAKI NISHIMOTO ABSTRACT Collagen was extracted from the digestive tract and skin of a Japanese amberjack (Seriola quinqueradiata) by acid extraction and limited pepsin digestion. The amounts of collagen solubilized from the digestive tract were smaller than those from the skin. Based on the solubility in NaCl solution, electrophoretic and peptide map patterns, and amino acid composition, the main digestive tract collagen was identified as type I, having characteristics different from those of the body wall collagen in cyclostome intestine. Further, the degree of hydroxylation of prolyl and lysyl residues in the type I collagen of the digestive tract is significantly higher than that of the skin. Collagen preparations from the digestive tract have a higher ratio of type V collagen than those from the skin. Hence, the digestive tract collagen differs from that in the skin in the degree or property of intermolecular crosslinking, posttranslational modification, and molecular species composition. PRACTICAL APPLICATIONS Partial hydrolyzate of gelatin, in other word collagen peptide, has gained popularity as a food ingredient, as it has been suggested to have health benefits, such as improvement of skin and joint conditions. Recently, attention toward collagen derived from marine origin such as fish skin increased because of the outbreak of bovine spongiform encephalopathy. Large amounts of the digestive tract, stomach, intestine and adhesion tissues are generated by fishery industries and most of them are by-products of low value. Although these organs are also rich in collagen, the collagen in fish digestive tract has not been characterized. The present study demonstrates that the collagen in digestive tract differs from the skin collagen in the solubility, posttranslational modification and molecular species composition. These facts suggest that modified collagen peptides might be obtained from the digestive tract. [source] Correlated changes in skeletal muscle connective tissue and flesh texture during starvation and re-feeding in brown trout (Salmo trutta) reared in seawaterJOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, Issue 11 2004Jérôme Bugeon Abstract Quantitative and qualitative changes to muscle and collagen were analysed following starvation and re-feeding of brown trout (Salmo trutta) reared in seawater. Fish were submitted to starvation for 2 months followed by re-feeding for 1 month and compared with a control group continuously fed. Classical effects of starvation on growth and morphometrics traits were observed with only a partial recovery of these parameters after 1 month of re-feeding. Muscle composition of starved fish was significantly affected (lower dry matter content and higher post-mortem pH) compared with control fish and was partially recovered in re-fed fish compared with continuously fed fish. Muscle structure and composition were affected with thinner muscle fibre and higher connective tissue content for the starved fish but similar thickness of myosepta compared with the control group. No difference was observed after 1 month of re-feeding. Characteristics of the connective tissue were significantly affected by starvation (more high weight molecular collagen form, higher thermal stability of skin collagen). These differences remained significant after the re-feeding period. Starved fish showed also higher mechanical resistance of the raw flesh compared with the control group, but no difference in rheological measurements was observed after 1 month of re-feeding. The changes in texture and their relationships with muscle composition, muscle structure and collagen characteristics are discussed. Copyright © 2004 Society of Chemical Industry [source] Effect of UV irradiation on type I collagen fibril formation in neutral collagen solutionsPHOTODERMATOLOGY, PHOTOIMMUNOLOGY & PHOTOMEDICINE, Issue 3 2001Julian M. Menter Background: Collagens have the well-known ability to spontaneously self-associate to form fibrils at physiological temperature and neutral pH in vitro and in vivo. Because solar UV may photochemically alter collagen, the kinetics of fibril formation may be modified. Thus, we have begun a systematic study of the effect of various UV wavebands on fibril formation. Methods: Citrate-soluble calf skin collagen (Elastin Products) was dissolved at 0.05% in 0.5 M HOAc, dialyzed over 2 days into two changes of 0.0327 M phosphate buffer, pH 7.0 at 4 °C, and centrifuged at 48 000×g. Photolysis was carried out at 4 °C with either (a) UVC (UVG,11 lamp), (b) filtered solar-simulating radiation (SSR) or UVA (SSR or UVL,21 lamp filtered with a 2.0 mm Schott WG 345 filter). Gelation was commenced by rapidly raising the temperature from 8 °C to 33 °C. Nucleation and growth were followed by turbidimetric measurements at 400 nm. Results: UVC radiation (0,17.3 J/cm2) resulted in a dose-dependent decrease in the rate of fibril growth. Under these conditions, concomitant collagen cross-linking and degradation occurred. Fibril nucleation, a prerequisite for growth, was rapid (threshold , 2 min) and was not affected by UVC, UVA or SSR. SSR (0,1320 J/cm2) caused a small decrease in growth rate and in the degree of fibril formation. UVA radiation (0,1080 J/cm2) had a similar effect. "Direct" photochemical damage thus paralleled absorption via various collagen chromophores, with UVC>SSR,UVA. The presence of riboflavin (RF) resulted in ground-state interactions that markedly altered both nucleation and growth kinetics. Irradiation with 29.6 J/cm2 UVA in the presence of RF photosensitizer caused relatively minor additional changes in fibrillation kinetics. Conclusions: These results collectively indicate that fibril formation is markedly dependent on specific ground state interactions and relatively insensitive to nonspecific UV damage. On the other hand, fibrils thus formed from photochemically altered collagen may have altered structural properties that could have subtle but unfavorable effects on the local dermal milieu in vivo. Notwithstanding, the relative insensitivity of fibrillogenesis to non-specific photochemical damage probably represents a favorable adaptation, overall, which tends to conserve the mechanical integrity of the skin. [source] Polymerization and matrix physical properties as important design considerations for soluble collagen formulationsBIOPOLYMERS, Issue 8 2010S. T. Kreger Abstract Despite extensive use of type I collagen for research and medical applications, its fibril-forming or polymerization potential has yet to be fully defined and exploited. Here, we describe a type I collagen formulation that is acid solubilized from porcine skin collagen (PSC), quality controlled based upon polymerization potential, and well suited as a platform polymer for preparing three-dimensional (3D) culture systems and injectable/implantable in vivo cellular microenvironments in which both relevant biochemical and biophysical parameters can be precision-controlled. PSC is compared with three commercial collagens in terms of composition and purity as well as polymerization potential, which is described by kinetic parameters and fibril microstructure and mechanical properties of formed matrices. When subjected to identical polymerization conditions, PSC showed significantly decreased polymerization times compared to the other collagens and yielded matrices with the greatest mechanical integrity and broadest range of mechanical properties as characterized in oscillatory shear, uniaxial extension, and unconfined compression. Compositional and intrinsic viscosity analyses suggest that the enhanced polymerization potential of PSC may be attributed to its unique oligomer composition. Collectively, this work demonstrates the importance of standardizing next generation collagen formulations based upon polymerization potential and provides preliminary insight into the contribution of oligomers to collagen polymerization properties. © 2010 Wiley Periodicals, Inc. Biopolymers 93: 690,707, 2010. This article was originally published online as an accepted preprint. The "Published Online" date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com [source] PREPARATION AND CHARACTERIZATION OF PEPSIN-SOLUBILIZED TYPE I COLLAGEN FROM THE SCALES OF SNAKEHEAD (OPHIOCEPHALUS ARGUS)JOURNAL OF FOOD BIOCHEMISTRY, Issue 1 2009WENTAO LIU ABSTRACT Pepsin-solubilized collagen prepared from the scales of snakehead (Ophiocephalus argus) was separated into two fractions, major and minor, by NaCl precipitation. The results of sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), amino acid composition, and secondary structure showed that the major collagen was typical type I collagen; in contrast, the minor collagen might be classified as type V collagen from the SDS-PAGE patterns and precipitation properties by NaCl. A sharp decrease in solubility of type I collagen was observed at the NaCl concentration of 40 g/L. The maximum and the minimum solubilities of collagen were observed at pH 3 and 8, respectively. Peptide maps of type I collagen digested by trypsin and V8 protease were different from those of calfskin and fish skin collagens. The imino acid content of type I collagen was lower than those of mammalian collagens and so did its denaturation temperature that was 30.3C obtained by viscosity measurement. PRACTICAL APPLICATIONS Collagen has been widely utilized as a material for foods, cosmetics, and pharmaceuticals. However, the use of collagen-derived products from land animals (e.g., bovine and pig) has been called into question because of foot-and-mouth disease crisis etc. Aquatic animal offals, which are readily available and inexpensive, seem to be safe sources for extraction of collagen. This work reports on preparation and characterization of collagen from snakehead scales, which will have potential in supplementing the skins and bones of land animals as an important collagen resource for use in functional food, biomedical, and cosmetic industries. 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