On clot-promoting surfaces, intact normal blood or plasma deposits fibrinogen and then supplants it with high molecular weight kininogen (HMWK). On glass, plasma layers of less than about 25 micron thick, while still containing enough fibrinogen to coat the surrounding surfaces, lack sufficient HMWK per surface area to remove this fibrinogen deposit. Thus normal intact citrated plasma allowed to enter the space between a glass slide and a convex lens resting belly-down on the slide will leave a disc of fibrinogen where the thickness of plasma layer was below this "critical height" H. The discs of fibrinogen left by plasma that lacks HMWK pathologically or by activation or dilution, are larger--the required H being greater. The present study shows that plasma dilution (final volume divided by original plasma volume) plotted against H yields a straight line. In preliminary series, the slope of this line increases with the atomic weight of five metals whose oxidized surfaces were used as substrates. In whole blood collected in either heparin or ACD, a circle of platelets adheres to oxidized silicon, anodized tantalum, or glass; this circle is similar in size to the one of fibrinogen left by plasma.

Blood Cells↗

PubMedDate not supplied

Effects of secondary flow caused by a curved channel on plasma protein adsorption to artificial surfaces.

The effects of secondary flow induced by a curved channel on fibrinogen deposition and replacement on a glass surface were studied. Platelet adhesion to surface-bound fibrinogen was also studied to indicate how secondary flow may affect thrombogenesis on artificial surfaces. A saline pre-wetted channel with straight and curved sections was exposed to flowing plasma at a Reynolds number of 28.6. Results show that fibrinogen deposited on the surface at a shear rate of 175 s-1 was replaced faster in regions of secondary flow (Dean numbers from 11 to 19) than in adjacent regions of shear flow. Platelets adhered only to those surfaces where fibrinogen had been detected.

Adsorption↗

PubMedDate not supplied

Separated flows in artificial organs. A cause of early thrombogenesis?

Separated flow is unavoidable in artificial blood-wetted devices. Surfaces bound by separated flows cause abnormal protein adsorption, then platelet adhesion and activation, and eventually thrombogenesis and embolization. A prolonged abnormal adsorption pattern is expected, especially in separated flows, as blood first displaces a wetting liquid during start-up of a device. The authors obtained patterns of immunoglobulin G (IgG), fibrinogen, and high molecular weight kininogen (HMK) adsorption in and near a separated flow. The flow was induced in flowing saline, replaced at time zero by plasma. The separated flow was induced behind a 4 mm bar introduced into a steady shear flow (Re = 26.4) in an apparatus designed so that the surface behind the bar was a standard glass microscope slide. The staining technique revealed the distribution of each protein of interest over the surface of the slide, and was applied to slides residing in the flow for 1, 5, 10, 30, and 60 min after the introduction of plasma (final dilution, 3.5% and 8.5%). Results show the expected, rapid disappearance of fibrinogen from surfaces near (but not in) the separated region, and prolonged appearance and even more prolonged disappearance of fibrinogen from the surface bounding the separated region. Slides removed from the apparatus, when exposed to a platelet suspension, showed that platelets adhered where fibrinogen was present on the surface.

Adsorption↗

PubMedDate not supplied

Problems in the development of materials that are compatible with blood.

A comprehensive outlook of blood-material interaction is presented with an emphasis on the activation of clotting and platelet adhesion via fibrinogen at the interface. Further limitations and suggestions of interrelating the invitro investigations to invivo conditions are discussed.

Biocompatible Materials↗

PubMedDate not supplied

Interactions among human blood proteins at interfaces.

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Adsorption↗

PubMedDate not supplied

Summation: protein at the interface.

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Adsorption↗