Specificity of a cysteine proteinase of Entamoeba histolytica towards the α1-CB2 peptide of bovine collagen type I

The adhesion of bovine collagen type I, bovine serum albumin, bovine IgG, 1 % and 10 % (v/v) human serum to hydroxyapatite (HA), silicon-substituted hydroxyapatite (Si-HA) and tissue culture plastic were studied. The materials were incubated at 37 °C for 30 minutes, after which the protein solution was removed and analyzed. The adsorbed protein was evaluated by electrophoresis and immunoassay after extraction from the materials. The degree of adhesion was higher for collagen, followed by IgG and albumin on all materials. However there was no difference in the amount of collagen adsorbed onto the surface of each material and this was also the finding with albumin and IgG. These results suggest that the increased bioactivity seen with Si-HA is not due to the degree of protein adhesion, but may possibly be due to changes in the conformation of the bound proteins.

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P128 Cultivation of human meniscus cells on porous bovine collagen type I scaffolds

Osteoarthritis and Cartilage ◽

10.1016/s1063-4584(07)61483-6 ◽

2007 ◽

Vol 15 ◽

pp. B120

Author(s):

O. Kessler ◽

A. Thomsen ◽

C. Falco ◽

S. Thoma

Keyword(s):

Collagen Type ◽

Collagen Type I ◽

Type I ◽

Bovine Collagen ◽

Meniscus Cells

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Model for human skin reconstructed in vitro composed of associated dermis and epidermis

Sao Paulo Medical Journal ◽

10.1590/s1516-31802006000200005 ◽

2006 ◽

Vol 124 (2) ◽

pp. 71-76 ◽

Cited By ~ 27

Author(s):

Luís Ricardo Martinhão Souto ◽

Jussara Rehder ◽

José Vassallo ◽

Maria Letícia Cintra ◽

Maria Helena Stangler Kraemer ◽

...

Keyword(s):

Human Skin ◽

Collagen Type ◽

Human Fibroblasts ◽

Skin Grafting ◽

Human Keratinocytes ◽

Collagen Type I ◽

Type I ◽

Bovine Collagen

CONTEXT AND OBJECTIVE: The technique of obtaining human skin with dermis and epidermis reconstructed from cells isolated from patients can enable autologous skin grafting on patients with few donor sites. It also enables in vitro trials on chemicals and drugs. The objective of this work was to demonstrate a method for obtaining human skin composed of associated dermis and epidermis, reconstructed in vitro. DESIGN AND SETTING: Experimental laboratory study, in the Skin Cell Culture Laboratory of Faculdade de Ciências Médicas, Universidade Estadual de Campinas. METHODS: Cells from human fibroblast cultures are injected into bovine collagen type I matrix and kept immersed in specific culturing medium for fibroblasts. This enables human dermis reconstruction in vitro. On this, by culturing human keratinocytes and melanocytes, differentiated epidermis is formed, leading to the creation of human skin composed of associated dermis and epidermis, reconstructed in vitro. RESULTS: We showed that human skin composed of associated dermis and epidermis can be successfully reconstructed in vitro. It is histologically formed in the same way as human skin in vivo. Collagen tissue can be identified in the dermis, with cells and extracellular matrix organized in parallel to multilayer epidermis. CONCLUSIONS: It is possible to obtain completely differentiated human skin composed of associated dermis and epidermis, reconstructed in vitro, from injection of human fibroblasts into bovine collagen type I matrix and culturing of human keratinocytes and melanocytes on this matrix.

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IDENTIFICATION OF A SECOND COLLAGEN-BINDING DOMAIN IN HUMAN VON WILLEBRAND FACTOR

10.1055/s-0038-1642877 ◽

1987 ◽

Cited By ~ 1

Author(s):

F I Pareti ◽

K Nliya ◽

P J Kostel ◽

J M McPherson ◽

T S Zimmerman ◽

...

Keyword(s):

Collagen Type ◽

Collagen Type I ◽

Binding Domain ◽

Type I ◽

Collagen Binding ◽

Tryptic Fragment ◽

Binding Domains ◽

Bovine Collagen ◽

Von Willebrand ◽

Willebrand Factor

We have recently reported (Journal of Biological Chemistry 261: 15310-15315, 1986) that von Willebrand factor (vWF) possesses a collagen-binding domain localized in a reduced and alkylated tryptic fragment of apparent 52/48 kDa molecular weight extending between residues Val (449) and Lys (728) of the constituent subunit. This proteolytic fragment of vWF also contains a glycoprotein lb-binding domain and a heparin-binding domain. We have now identified a second collagen-binding domain in the Staphylococcus aureus V8 protease-generated fragment I that extends from residue Gly (911) to Glu (1365). The two binding domains exhibit different interaction with collagens of different origin. The reduced and alkylated 52/48 kDa tryptic fragment was a potent inhibitor of vWF binding to equine collagen type I, but had no effect on the binding to bovine collagen type I and III. In contrast, a purified fraction containing the unreduced 52/48 kDa domain inhibited vWF binding to all types of collagen, as did anti-52/48 kDa monoclonal antibodies. Some of these antibodies, however, were more effective in inhibiting binding to equine collagen. On the other hand, fragment I markedly inhibited the binding of vWF to bovine collagen type I and III, but was less effective with equine collagen type I. Direct binding studies using 425j_qabeled fragment I demonstrated that the association constant was 5 to 10 times greater with the bovine collagens than with the equine collagen. The Staphylococcus aureus V8 protease-generated fragment III, which extends from residue Ser (1) to Glu (1365) and contains both collagen-binding domains, was the most potent inhibitor of vWF binding to all types of collagen tested. Thus, vWF has at least two collagen-binding domains. Native conformation appears to be necessary for binding of the 52/48 kDa domain to bovine collagen type I and III, but not to the equine collagen type I tested. The two domains appear to function concurrently in mediating vWF binding to collagen.

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