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Pt Linder

Publications and source records attributed to Pt Linder.

2 recordsLinked to original sources

Decrease in extracellular collagen crosslinking after NMR magnetic field application in skin fibroblasts.

Although biological effects of electromagnetic fields were investigated intensively, there is still no agreement on the significance of their effects. The underlying mechanisms and therapeutic importance are still mostly unknown too. In this study, primary cultures of human dermal fibroblasts were exposed to magnetic field at nuclear magnetic resonance (NMR) conditions for in total 5 days and 4 h/day. Among the investigated parameters were: cell proliferation rate, cell morphology, total protein concentration as well as content of skin-specific collagen types I, III, IV. NMR exposure induced distinct changes both in cellular and extracellular components. The extracellular matrix (ECM) of NMR-exposed cells had less cross-linked collagen. In particular, the increase of collagen of the soluble fraction was at 17.2 +/- 2.9% for type I, 27.0 +/- 1.86% for type III, 17.3 +/- 1.46% for type IV (N = 6). In the absence of resonance frequency, the effects of magnetic field on ECM were less profound.

Body Water↗

Body temperature-related structural transitions of monotremal and human hemoglobin.

In this study, temperature-related structural changes were investigated in human, duck-billed platypus (Ornithorhynchus anatinus, body temperature T(b) = 31-33 degrees C), and echidna (Tachyglossus aculeatus, body temperature T(b) = 32-33 degrees C) hemoglobin using circular dichroism spectroscopy and dynamic light scattering. The average hydrodynamic radius (R(h)) and fractional (normalized) change in the ellipticity (F(obs)) at 222 +/- 2 nm of hemoglobin were measured. The temperature was varied stepwise from 25 degrees C to 45 degrees C. The existence of a structural transition of human hemoglobin at the critical temperature T(c) between 36-37 degrees C was previously shown by micropipette aspiration experiments, viscosimetry, and circular dichroism spectroscopy. Based on light-scattering measurements, this study proves the onset of molecular aggregation at T(c). In two different monotremal hemoglobins (echidna and platypus), the critical transition temperatures were found between 32-33 degrees C, which are close to the species' body temperature T(b). The data suggest that the correlation of the structural transition's critical temperature T(c) and the species' body temperature T(b) is not mere coincidence but, instead, is a more widespread structural phenomenon possibly including many other proteins.

Adult↗