Dilution-induced enhancement of the blocking temperature in exchange-bias heterosystems

The temperature dependence of the exchange bias field is investigated by superconducting quantum interference device magnetometry in Fe1-xZnxF2(110)/Fe14 nm/Ag35 nm, x=0.4. Its blocking temperature exhibits a significant enhancement with respect to the global ordering temperature TN=46.9 K, of the bulk antiferromagnet Fe0.6Zn0.4F2. The enhancement is attributed to fluctuations of the diamagnetic dilution which creates clusters on all length scales having a Zn dilution of 0\u3c~x\u3c~1. While the infinite clusters give rise to the well-known Griffiths phase, finite clusters also provoke a local enhancement of the exchange bias. The temperature dependence of the integral exchange bias effect is modeled by averaging all local contributions of the antiferromagnetic surface magnetization which exhibit a surface critical behavior

Training of the exchange-bias effect in NiO-Fe heterostructures

The training effect of a NiO(001)/Fe(110) heterostructure is studied from magnetic hysteresis loops measured by superconducting quantum interference device magnetometry. Consecutive hysteresis loops exhibit a decreasing exchange bias effect. This behavior is known as the training effect, which reflects the dependence of the exchange bias field on the antiferromagnetic interface magnetization. In order to evidence this dependence, we study the decrease of the total saturation magnetization of the heterostructure for an increasing number of hysteresis cycles. Assuming proportionality between the interface magnetization and the total saturation magnetization, the description of the data is consistent within the phenomenological Meiklejohn Bean approach

Electrically controlled exchange bias for spintronic applications

Exchange coupling between a magnetoelectric (111)-oriented Cr2O3 single crystal and a CoPt multilayer with perpendicular anisotropy exhibits an exchange bias field proportional to the applied axial electric field. Extrapolation from bulk to thin film magnetoelectric pinning system suggests promising spintronic applications due to coupling between the electric field-controlled magnetization and the magnetization of a neighbor ferromagnetic layer. Pure voltage control of magnetic configurations of tunneling magnetoresistance spin valves is an attractive alternative to current-induced magnetization switching. ©2005 American Institute of Physic

Increased Collagen Turnover Impairs Tendon Microstructure and Stability in Integrin alpha 2 beta 1-Deficient Mice

Integrins are a family of transmembrane proteins, involved in substrate recognition and cell adhesion in cross-talk with the extra cellular matrix. In this study, we investigated the influence of integrin alpha 2 beta 1 on tendons, another collagen type I-rich tissue of the musculoskeletal system. Morphological, as well as functional, parameters were analyzed in vivo and in vitro, comparing wild-type against integrin alpha 2 beta 1 deficiency. Tenocytes lacking integrin alpha 2 beta 1 produced more collagen in vitro, which is similar to the situation in osseous tissue. Fibril morphology and biomechanical strength proved to be altered, as integrin alpha 2 beta 1 deficiency led to significantly smaller fibrils as well as changes in dynamic E-modulus in vivo. This discrepancy can be explained by a higher collagen turnover: integrin alpha 2 beta 1-deficient cells produced more matrix, and tendons contained more residual C-terminal fragments of type I collagen, as well as an increased matrix metalloproteinase-2 activity. A greatly decreased percentage of non-collagenous proteins may be the cause of changes in fibril diameter regulation and increased the proteolytic degradation of collagen in the integrin-deficient tendons. The results reveal a significant impact of integrin alpha 2 beta 1 on collagen modifications in tendons. Its role in tendon pathologies, like chronic degradation, will be the subject of future investigations

Increased Collagen Turnover Impairs Tendon Microstructure and Stability in Integrin α2β1-Deficient Mice

Integrins are a family of transmembrane proteins, involved in substrate recognition and cell adhesion in cross-talk with the extra cellular matrix. In this study, we investigated the influence of integrin α2β1 on tendons, another collagen type I-rich tissue of the musculoskeletal system. Morphological, as well as functional, parameters were analyzed in vivo and in vitro, comparing wild-type against integrin α2β1 deficiency. Tenocytes lacking integrin α2β1 produced more collagen in vitro, which is similar to the situation in osseous tissue. Fibril morphology and biomechanical strength proved to be altered, as integrin α2β1 deficiency led to significantly smaller fibrils as well as changes in dynamic E-modulus in vivo. This discrepancy can be explained by a higher collagen turnover: integrin α2β1-deficient cells produced more matrix, and tendons contained more residual C-terminal fragments of type I collagen, as well as an increased matrix metalloproteinase-2 activity. A greatly decreased percentage of non-collagenous proteins may be the cause of changes in fibril diameter regulation and increased the proteolytic degradation of collagen in the integrin-deficient tendons. The results reveal a significant impact of integrin α2β1 on collagen modifications in tendons. Its role in tendon pathologies, like chronic degradation, will be the subject of future investigations