Glycosaminoglycan degradation reduces mineralized tissue-titanium interfacial strength.

Glycosaminoglycan degradation reduces mineralized tissue-titanium interfacial strength. Research Abstract Details 

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Glycosaminoglycan degradation reduces mineralized tissue-titanium interfacial strength. Abstract Text:

Hiromi Nakamura,Jaewoo Shim,Frank Butz,Hideki Aita,Vijay Gupta,Takahiro Ogawa,

Although the localization of the proteoglycan/glycosaminoglycan (GAG) complex at the bone-titanium implant interface has been implied, the role of proteoglycans on the establishment of bone-titanium integration is unknown. The hypothesis to be tested was that proteoglycans play an important role in establishing bone-titanium interfacial adhesion. The objective of this study is to investigate the effect of proteoglycan knockdown by GAG enzymatic degradation on the interfacial strength between mineralized tissue and titanium having different surface topographies. Rat bone marrow-derived osteoblastic cells were cultured on either a machined titanium disk or an acid-etched titanium disk. At day 21 of culture, one of the three following GAG degradation enzymes was added into the culture; chondroitinase AC, chondroitinase B, or keratanase. After 3 days of incubation (at day 24 of culture), the laser spallation technique was applied to the samples in order to assess the tissue-titanium interfacial strength. In this technique, a laser-generated stress wave is used to separate the tissue-titanium interface, and the interfacial strength is determined interferometrically by recording the transient free surface velocity of the tissue. Mineralized tissue cultured on the acid-etched titanium showed 20-30% higher tissue interfacial strength than that cultured on the machined titanium (p < 0.0001). For both the machined and acid-etched surface cultures, administration of the enzyme reduced the interfacial strength by 25-30% compared with the untreated control cultures (p < 0.0001). There were no differences in the effect among the three different enzymes tested. A nanoindentation study revealed that the enzyme treatment did not affect the elastic modulus of the mineralized tissue. Scanning electron microscopic and energy dispersive spectroscopic analyses revealed less post-spallation tissue remnant on the titanium substrates when treated with the enzymes. The tissue remnant was greater in amount on the acid-etched surface than on the machined surface. The results suggest that there exists not only mechanical interlocking but also biological interfacial adhesion between the mineralized tissue and titanium, in which the proteoglycan/GAG complex is involved.

Glycosaminoglycan degradation reduces mineralized tissue-titanium interfacial strength. Publishing Authors By Initials

H Nakamura,J Shim,F Butz,H Aita,V Gupta,T Ogawa,

For similar inorganic chemicals: elements: metals, light: titanium research abstracts see: inorganic chemicals: elements: metals, light: titanium research

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MEDLINE DATE:

Glycosaminoglycan degradation reduces mineralized tissue-titanium interfacial strength. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biomedical materials research. Part A

VOLUME: 77

Page Numbers: 478-86

Journal Abbreviation:

ISSN: 1549-3296

DAY: 1

MONTH: Jun

YEAR: 2006

Glycosaminoglycan degradation reduces mineralized tissue-titanium interfacial strength. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 101234237

Glycosaminoglycan degradation reduces mineralized tissue-titanium interfacial strength. Keywords Mesh Terms:

KEYWORDS: Titanium

MESH TERMS: metabolism

Chemical & Substance for Abstract: Glycosaminoglycan degradation reduces mineralized tissue-titanium interfacial strength. Information

Substance Name: Titanium

Registry Number: 7440-32-6

Grant and Affiliation Information for Glycosaminoglycan degradation reduces mineralized tissue-titanium interfacial strength.

AFFILIATION: The Weintraub Center for Reconstructive Biotechnology, UCLA School of Dentistry, Los Angeles, California 90095-1668, USA.

Country: United States

AGENCY: United States NIBIB

GRANT: EB004379

ACRONYM: EB

MEDLINETA: J Biomed Mater Res A

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