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Type V Collagen (type + v_collagen)
Selected AbstractsEFFECT OF SLAUGHTER METHOD ON DEGRADATION OF INTRAMUSCULAR TYPE V COLLAGEN DURING SHORT-TERM CHILLED STORAGE OF CHUB MACKEREL SCOMBER JAPONICUSJOURNAL OF FOOD BIOCHEMISTRY, Issue 5 2002KENJI SATO ABSTRACT The present paper demonstrates that a nonstntggling slaughter method can delay degradation of type V collagen in meat of chub mackerel Scomber japonicus and softening of the meat during postharvest chilled storage. The fish were slaughtered by piercing a knife into nape (nonstruggling method) or by leaving on ground (struggling method) and then stored in an ice box. Sensory study revealed that the postharvest softening of the meat was moderated at 4 and 8 h by the non-struggling slaughter method in comparison with the struggling method. On the basis of the specific solubilization of type V collagen and reduced tyrosine content in it, a cleavage of the nonhelical regions (telopeptides) of the type V collagen occurred during the chilled storage in the fish slaughtered by the struggling method. The degradation of type V collagen was also slower in the meat of the fish slaughtered by the nonstruggling method, which can be directly linked to the moderation of the postharvest softening. [source] Silencing S1P1 Receptors Regulates Collagen-V Reactive Lymphocyte-Mediated Immunobiology in the Transplanted LungAMERICAN JOURNAL OF TRANSPLANTATION, Issue 3 2008M. Chiyo Type V collagen (col[V])-reactive lymphocytes contribute to lung transplant rejection, but the mechanisms for emigration into the graft are unknown. Sphingosine-1-phosphate-1 receptors (S1P1R) are believed to be required for lymphocyte emigration in other studies, but their role in col(V)-reactive lymphocyte rejection responses is not known. Utilizing small interfering RNA (siRNA) to reduce S1P1R expression on col(V)-reactive lymphocytes, we examined the role of S1P1R in the rejection response. Quantitative polymerase chain reaction (PCR) revealed strong expression of S1P1R messenger RNA (mRNA)on col(V)-reactive lymphocytes isolated from immunized rats. S1P1R -specific siRNA (S1P1R siRNA) reduced expression of S1P1R mRNA and protein, whereas scramble siRNA (SC siRNA) had no effect. Adoptive transfer of lymphocytes treated with S1P1R siRNA to rat Wistar Kyoto (WKY) lung isograft recipients resulted in retention of cells within the liver with fewer cells in mediastinal lymph nodes when compared to cells exposed to SC siRNA. S1P1R -deficient cells proliferated in response to alloantigens, but not in response to col(V), and produced less interferon (IFN)-, in response to col(V) compared to controls. Downregulating S1P1R did not affect production of interleukin (IL)-10and tumor necrosis factor (TNF)-,, or expression of adhesion molecules critical for migration, but prevented rejection pathology and lowered local levels of IFN-, post adoptive transfer. These data demonstrate novel roles of S1P1R, which include regulating emigration and modulating lymphocyte activation. [source] COL5A1 signal peptide mutations interfere with protein secretion and cause classic Ehlers-Danlos syndrome,HUMAN MUTATION, Issue 2 2009Sofie Symoens Abstract Classic Ehlers-Danlos syndrome (EDS) is a heritable connective tissue disease characterized by skin hyperextensibility, atrophic scarring, joint hypermobility and generalized tissue fragility. Mutations in COL5A1 and COL5A2, encoding the type V collagen pro,1- and pro,2-chain, are found in ,50% of patients with classic EDS. The majority of mutations lead to a non-functional COL5A1 allele, as a result of the introduction of a premature stopcodon in one COL5A1 transcript. A minority of mutations affect the structure of the type V collagen central helical domain. We show that mutations in the signal peptide (SP) domain of the preproá1(V)-collagen chain cause classic EDS. The missense mutations (p.L25R and p.L25P) are located in the crucial hydrophobic SP core, which is indispensible for preprotein translocation into the endoplasmic reticulum. As a result, mutant type V procollagen is retained within the cell, leading to a decreased amount of type V collagen in the extracellular matrix and disturbed collagen fibrillogenesis. Our findings further support the observation that decreased availability of type V (pro)collagen is a key factor and a shared mechanism in the pathogenesis of classic EDS. © 2008 Wiley-Liss, Inc. [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] 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. [source] EFFECT OF SLAUGHTER METHOD ON DEGRADATION OF INTRAMUSCULAR TYPE V COLLAGEN DURING SHORT-TERM CHILLED STORAGE OF CHUB MACKEREL SCOMBER JAPONICUSJOURNAL OF FOOD BIOCHEMISTRY, Issue 5 2002KENJI SATO ABSTRACT The present paper demonstrates that a nonstntggling slaughter method can delay degradation of type V collagen in meat of chub mackerel Scomber japonicus and softening of the meat during postharvest chilled storage. The fish were slaughtered by piercing a knife into nape (nonstruggling method) or by leaving on ground (struggling method) and then stored in an ice box. Sensory study revealed that the postharvest softening of the meat was moderated at 4 and 8 h by the non-struggling slaughter method in comparison with the struggling method. On the basis of the specific solubilization of type V collagen and reduced tyrosine content in it, a cleavage of the nonhelical regions (telopeptides) of the type V collagen occurred during the chilled storage in the fish slaughtered by the struggling method. The degradation of type V collagen was also slower in the meat of the fish slaughtered by the nonstruggling method, which can be directly linked to the moderation of the postharvest softening. [source] Collagen types I, III, and V constitute the thick collagen fibrils of the mouse deciduaMICROSCOPY RESEARCH AND TECHNIQUE, Issue 1 2007Karin Spiess Abstract A mammal's endometrium is deeply remodeled while receiving and implanting an embryo. In addition to cell proliferation and growth, endometrial remodeling also comprises synthesis and degradation of several molecular components of the extracellular matrix. All of these events are orchestrated by a precise sequence of ovarian hormones and influenced by several types of cytokines. As we have previously reported, an intriguing and rapid increase in collagen fibril diameter occurs in the decidualized areas of the endometrium, surrounding the implantation crypt, whereas collagen fibrils situated far from the embryo remain unchanged. Collagen fibrilogenesis is a complex molecular process coordinated by a number of factors, such as the types and amounts of glycosaminoglycans and proteoglycans associated with collagen molecules. Collagen genetic type, mechanical stress, aging, and other factors not yet identified also contribute to this development. A recent study suggests that thick fibrils from mouse decidua are formed, at least in part, by aggregation of thin fibrils existing in the stroma before the onset of decidualization. In the present ultrastructural study using single and double immunogold localization, we showed that both thin and thick collagen fibrils present in the mouse pregnant endometrium endometrium are heterotypic structures formed at least by type I, type III, and type V collagens. However, type V collagen predominates in the thick collagen fibrils, whereas it is almost absent of the thin collagen fibrils. The putative role of type V homotrimer in the rapid increase of the diameter of collagen fibrils of the mouse decidua is discussed. Microsc. Res. Tech., 2006. © 2006 Wiley-Liss, Inc. [source] | ||||||||||