Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P00790 (PGA)
 2,475 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The major collagenous component secreted into the medium of cultured HT-1080 tumor cells was identified as type IV procollagen by specific antibodies and characteristic ratios of incorporated labeled 3-hydroxyproline and 4-hydroxyproline. The disulfide-bonded molecules consisted of two subunits, pro-alpha 1(IV) and pro-alpha 2(IV) chains with apparent molecular weights of 180 000 and 165 000. No conversion of the procollagen to collagen or to procollagen intermediates was detected in the cell cultures. The two subunits apparently represent different gene products, since enzymatic digestion of the separated chains produced quite different peptide maps. Pepsin degraded native type IV procollagen successively into several fragments, some still disulfide-linked, giving rise to a complex set of polypeptide chains (Mr = 30 000-140 000). This agrees with similar diverse patterns produced by pepsin from authentic type IV collagens. The ratio between the pro-alpha 1(IV) and pro-alpha 2(IV) chains varied in several experiments between 1.3 and 1.8, suggesting that the two chains belong to different triple-helical molecules. The cells also produced distinct amounts of fibronectin (subunit Mr = 230 000) and of the basement membrane glycoprotein laminin. The latter showed three subunits with Mr = 220 000, 210 000, and 400 000. A further disulfide-bonded, non-collagenous polypeptide (Mr = 160 000) was detected but not yet identified. Immunofluorescence demonstrated these proteins within the cells but not in a pericellular matrix. The production of basement membrane components by HT-1080 cells and lack of interstitial collagens disagree with the original classification of the cell line as a fibrosarcoma.
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PMID:Biosynthesis of two subunits of type IV procollagen and of other basement membrane proteins by a human tumor cell line. 625 Aug 36

Prolyl hydroxylase activity, hydroxyproline content and solubility of collagen in the human pregnant and post-partum uterus were studied. The results were as follows: 1. Prolyl hydroxylase activity in the uterine cervix was slightly elevated during pregnancy, and the highest level was observed on the 4th day post-partum. On the other hand, in the uterine body the highest activity was observed immediately after delivery. 2. Hydroxyproline content in the pregnant uterine cervix was slightly less than that of nonpregnant control and the lowest level was observed immediately after delivery, but on the 4th day post-partum it increased slightly. In the uterine body, there were no remarkable changes in content during pregnancy, but immediately after delivery it decreased remarkably. 3. Pepsin-soluble collagen in the uterine cervix increased significantly from an early pregnancy to immediately after delivery compared with nonpregnant control, but on the 4th day post-partum it decreased significantly compared with that immediately after delivery. In the uterine body, no significant changes in solubility were observed throughout pregnancy. 4. Comparing these data obtained on the cervix and the body at different stages of nonpregnancy, pregnancy and post-partum, enzyme activities in the body were always higher. Hydroxyproline content in the body of nonpregnant uterus showed a lower value than that in the cervix, but no remarkable differences were found between the cervix and the body throughout pregnancy and immediately after delivery. The significant decrease in pepsin-soluble collagen in the body was observed immediately after delivery.
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PMID:[Studies on prolyl hydroxylase activity, hydroxyproline content and solubility of collagen in the human uterus during pregnancy, delivery and postpartum involution (author's transl)]. 627 84

Several surgical disciplines apply cartilage grafts for reconstructive purposes and have to overcome the scarcity of donor sites for this unique tissue. Employing the techniques of tissue engineering, cartilage might be generated in reasonable amounts for clinical purposes. Application of growth factors together with biochemical and biomechanical scaffold properties influence the process of ex vivo transplant production. The aims of this study are: 1) to investigate the influence of IGF-1 and TGFbeta-2 on tissue engineered human septal cartilage in vitro and in vivo after transplantation in nude mice; 2) to analyse the effect of the polydioxanone (PDS) content of the biodegradable Ethisorb E210 scaffold on the properties of the implanted constructs. Cells were three-dimensionally cultured on biodegradable Ethisorb E210 (PGA-PLA-copolymer fleeces with polydioxanone (PDS) adhesions), or on E210 scaffolds with a reduced polydioxanone content. Wet weight (ww), GAG-, and hydroxyprolin-content, as well as the cellularity of the neocartilage constructs were quantitatively evaluated. Additionally, the in vivo resorption of the two types of cell carriers was monitored. Addition of growth factors clearly increased the wet weight of the in vitro cultured constructs before transplantation. After transplantation, high PDS content improved the in vivo stability and macroscopic morphometric appearance of the tissue engineered specimens and led to enhanced deposition of glycosaminoglycans in transplanted constructs. Hydroxyproline content of the implants was not affected by either growth factors or PDS content. These data suggest a role for IGF-1 and TGFbeta-2 in preparative in vitro culture of chondrocytes before implantation, while PDS content of the scaffold is important for in vivo properties of the implanted material.
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PMID:Growth factors and scaffold composition influence properties of tissue engineered human septal cartilage implants in a murine model. 1914 66