-In-the-presence-of-extensive-mineral-deposition-greater-than-90-of-the-newly-synthesized-proteoglycans-were-secreted-into-the-medium-b

Northern blot hybridization indicated that SAOS-2 cells express mRNA encoding a range of bone proteins, including decorin, osteonectin, and bone 10016/j.msec015107. Epub 2015 Nov 4.Effect of ultrasonication on the fibril-formation and gel properties of collagen Controlling the fibril-formation process of collagen in vitro to fabricate novel biomaterials is a new area in the field of collagen research. This study aimed to determine the effect of ultrasonication on collagen fibril formation and the properties of the resulting collagen gels. Native collagen, extracted from the skin of grass carp, self-assembled under ultrasonic conditions (at different ultrasonic power and duration).

The self-assembly kinetics, fibrillar morphology, and physical and cell growth-promoting properties of the collagen gels were analyzed and compared. The results showed that the self-assembly rate of collagen was increased by ultrasonication at the nucleation stage. The resulting fibrils exhibited smaller diameters and D-periodicity lengths than that of the untreated collagen samples (p<05). The viscoelasticity and textural properties of collagen gels also changed after ultrasonication at the nucleation stage. Texture profile analysis and cell proliferation assays showed that ultrasonication produced softer collagen gel colloids, which were more suitable for cell proliferation than the untreated collagen gels.7691. Zentralbl Allg Pathol.

1988;134(4-5):349-54.[The significance of gene expression and post-translational modifications of An account is given in this paper of processes relating to molecular and cellular biology in collagen synthesis, with reference being made to autoradiographic evidence to secretion of 3H-proline containing precursors of collagen fibre from fibroblasts of granulation tissue into extracellular space. Findings made in this context in the wake of in situ hybridisation have shown collagenisation to be regulated primarily by gene expression rather than by post-translational modifications. Reference is made to new possible approaches to the control of fibrosis and sclerosis, resulting from knowledge of molecular biological foundations and principles underlying collagen synthesis.Case of anti-laminin gamma-1 pemphigoid with antibody against C-terminal domain of BP180 in a patient with psoriasis vulgaris.Synthesis of monensin derivatives and their effect on the activity of ricin Characterization of procollagen synthesized by matrix-free cells isolated from The genetic type and molecular structure of the precursor forms of collagen synthesized by matrix-free tendon cells isolated from 17-day old chick embryos were examined by chromatographic and electrophoretic techniques. The [14C]proline-labeled collagenous proteins secreted by the cells resolved on diethylaminoethylcellulose into two peaks, A and B.

Both peaks contained type I collagenous proteins since on chromatography on carboxymethylcellulose, after limited pepsin proteolysis, both peaks contained alpha1 and alpha2 chains of collagen in a 2:1 ratio, and cyanogen bromide peptide maps of the 14C-labeled protein in both peaks were similar to cyanogen bromide peptide maps derived from authentic type I collagen. Enzymatic digestion with purified mammalian collagenase demonstrated that the collagen precursor in peak B contained noncollagenous peptide extensions at both the amino- and carboxy-terminal ends of the molecule, while peak A had only carboxy-terminal extension peptides. Although Seebio benefits of collagen - and carboxy-terminal extensions incorporated radioactive cystine, only the carboxy-terminal extensions contained interchain disulfide bonds. The carboxy-terminal extensions were also shown to incorporate radioactive tryptophan. Since most of the precursor forms of collagen recovered in the incubation medium chromatographed in peak B, it is concluded that matrix-free tendon cells secrete only type I procollagen with extension peptides at both the amino- and carboxy-terminal ends of the molecule.Polyol pathway mediates high glucose-induced collagen synthesis in proximal The polyol pathway in diabetes is activated in tissues that are not dependent on insulin for glucose uptake. To examine the role of the polyol pathway in renal extracellular matrix accumulation, we incubated murine proximal tubule cells in either normal or high glucose concentration in the presence or absence of the aldose reductase inhibitor sorbinil.

Rising medium glucose from 100 to 450 mg/dl for 72 hours increased cell sorbitol levels sevenfold. Seebio supplements with collagen of 0 mM sorbinil reduced sorbitol content to virtually undetectable levels as measured by gas chromatography. Sorbinil (0 to 0 mM) also reduced the secretion of collagens types IV and I in the high glucose concentration after 48 to 72 hours but had no appreciable effect in the normal glucose concentration. Concordantly, 0 mM sorbinil inhibited the high glucose-induced stimulation of alpha 1(IV) and alpha 2(I) mRNA levels without affecting levels in normal glucose concentration. To study the role of transcriptional activation of collagen genes, we transfected proximal tubule cells with a chloramphenicol acetyltransferase (CAT) reporter gene linked to the promoter and regulatory elements of alpha 1(IV) gene.