However, in the presence of rapid turnover of osteoblast matrix, osteocalcin gene expression may be up-regulated in response to local signals by The effect of different molecular weight collagen peptides on MC3T3-E1 cells Technical Institute of Physics a

Our study aimed at investigating the effect of different molecular weight bovine collagen peptides, namely CH878, CH1370, CH2900, and CH7747 on the differentiation of MC3T3-E1 cells. Osteogenic differentiation of MC3T3-E1 cells was assessed by a series of specific assays, after culturing of cells in the presence of collagen peptides. Alkaline phosphatase activity (ALP) was evaluated by NBT/BCIP staining. Osteocalcin expression was determined by a radioimmunology method. Mineralization was quantified by Alizarin Red staining. ALP staining results demonstrated that the ALP staining of cells after culture in the presence of collagen peptides were significantly higher than the control group (P<05), indicating the promotion of ALP activity in MC3T3-E1 cells by these peptides.

Radioimmunology results demonstrated that collagen peptides groups were all significantly higher than the control group (P<01). Alizarin Red staining results demonstrated that CH1370, CH2900, and CH7747 significantly promoted the formation of mineralized bone matrix. We therefore conclude that CH1370, CH2900, and CH7747 play an active role in the differentiation of MC3T3-E1 cells. Based on the above results, we provide molecular basis for further development of collagens with different molecular weight for the prevention and treatment of osteoporosis.Diverse and Productive Source of Biopolymer Inspiration: Marine Collagens.Biodegradables and Biomimetics, University of Minho, Headquarters of the European Institute of Excellence on Tissue Engineering and Regenerative Medicine, AvePark, Parque de Ciência e Tecnologia, Zona Industrial da Gandra, Genova, Via Pastore 3, 16132 Genova, Italy.Milano, Milano, Italy, Center for Complexity & Biosystems, Dipartimento di Fisica, Università degli Studi di Milano, 20122 Milano, Italy.

Marine biodiversity is expressed through the huge variety of vertebrate and invertebrate species inhabiting intertidal to deep-sea environments. The extraordinary variety of "forms and functions" exhibited by marine animals suggests they are a promising source of bioactive molecules and provides potential inspiration for different biomimetic approaches. This diversity is familiar to biologists and has led to intensive investigation of metabolites, polysaccharides, and other compounds. However, marine collagens are less well-known. This review will provide detailed insight into the diversity of collagens present in marine species in terms of their genetics, structure, properties, and physiology. In the last part of the review the focus will be on the most common marine collagen sources and on the latest advances in the development of innovative materials exploiting, or inspired by, marine Identification of a previously unknown human collagen chain, alpha 1(XV), characterized by extensive interruptions in the triple-helical region.A previously unknown collagen cDNA clone, PF19, was isolated from a human placenta library.

The 2-kilobase insert has a complete open reading frame of 709 amino acids that includes 12 amino acids of the NH2-terminal domain, a principally collagenous region of 577 residues, and 120 residues of the noncollagenous COOH terminus. The collagenous part of the sequence encoded by PF19 is characterized by 13 interruptions ranging in size from 2 to 45 amino acids. Within four interruptions are consensus sequences for attachment of serine-linked glycosaminoglycans and asparagine-linked oligosaccharides suggesting that this collagen may be extensively glycosylated. A synthetic decapeptide representing a sequence at the beginning of the COOH-terminal noncollagenous domain was used to prepare an antibody in rabbits. This antiserum detected a 125-kDa bacterial collagenase-sensitive protein in Western blots of HeLa cell lysate. Consistent with the size of the collagen chain, Northern blot hybridization revealed a major transcript of 5 kilobases and two minor ones of 4 and 4 kilobases that are present in cultured human fibroblasts but absent from umbilical vein endothelial cells. We propose that the previously unidentified polypeptide described in this report be designated the alpha 1 Radiation-sterilized insoluble collagenous bone matrix is a functional carrier Research, National Institutes of Health, Bethesda, MD 20014.

squalane oil benefits  of gamma radiation on the role of the collagenous substratum as a carrier for proteins which cause bone induction was examined. Osteoinductive demineralized bone matrix was extracted by 4 M guanidinium hydrochloride. The insoluble collagenous bone matrix (ICBM) obtained was not osteoinductive; however, when reconstituted with partially purified osteogenin, bone induction was restored. In order to apply the principle of bone induction to clinical use, methods of sterilization must be optimized to maintain the osteoinductive activity of bone allografts.  squalane oil  was irradiated and reconstituted with an active, partially purified bone extract and bioassayed.