Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0393754 (HSA)
 2,996 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Heat-stable antigen (HSA/mouse CD24) is expressed in both haematopoietic and neural cells. The small core protein of the molecule is extensively glycosylated and anchored to the membrane via glycosylphosphatidylinositol. The role of HSA in the developing brain as well as its functional properties are poorly understood. Here we show that the brain HSA is associated with N- and O-linked oligosaccharide moieties and decorated with the HNK-1 sulfated carbohydrate epitope. It can bind P-selectin but not E-selectin and this interaction requires divalent cations and is sensitive to high salt. Brain derived HSA is also capable of binding to the L1 adhesion molecule. This interaction is distinct from the P-selectin binding as it is resistant to high salt and does not require bivalent cations. Treatment of HSA with OSGE significantly reduced binding of both P-selectin and I.1. Our data suggest that HSA can bind P-selectin and I.1 by distinct mechanism and that the binding epitopes on HSA are in close proximity.
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PMID:Heat-stable antigen (mouse CD24) in the brain: dual but distinct interaction with P-selectin and L1. 904 6

The maximum capacity of a hydrophobic adsorbent is interpreted in terms of square or hexagonal (cubic and face-centered-cubic, FCC) interfacial packing models of adsorbed blood proteins in a way that accommodates experimental measurements by the solution-depletion method and quartz-crystal-microbalance (QCM) for the human proteins serum albumin (HSA, 66 kDa), immunoglobulin G (IgG, 160 kDa), fibrinogen (Fib, 341 kDa), and immunoglobulin M (IgM, 1000 kDa). A simple analysis shows that adsorbent capacity is capped by a fixed mass/volume (e.g. mg/mL) surface-region (interphase) concentration and not molar concentration. Nearly analytical agreement between the packing models and experiment suggests that, at surface saturation, above-mentioned proteins assemble within the interphase in a manner that approximates a well-ordered array. HSA saturates a hydrophobic adsorbent with the equivalent of a single square or hexagonally-packed layer of hydrated molecules whereas the larger proteins occupy two-or-more layers, depending on the specific protein under consideration and analytical method used to measure adsorbate mass (solution depletion or QCM). Square or hexagonal (cubic and FCC) packing models cannot be clearly distinguished by comparison to experimental data. QCM measurement of adsorbent capacity is shown to be significantly different than that measured by solution depletion for similar hydrophobic adsorbents. The underlying reason is traced to the fact that QCM measures contribution of both core protein, water of hydration, and interphase water whereas solution depletion measures only the contribution of core protein. It is further shown that thickness of the interphase directly measured by QCM systematically exceeds that inferred from solution-depletion measurements, presumably because the static model used to interpret solution depletion does not accurately capture the complexities of the viscoelastic interfacial environment probed by QCM.
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PMID:Volumetric interpretation of protein adsorption: interfacial packing of protein adsorbed to hydrophobic surfaces from surface-saturating solution concentrations. 2103 80