Surface charge distribution on the endothelial cell of liver sinusoids.

Ghitescu, Lucian; Fixman, A

doi:10.1083/jcb.99.2.639

Cited by 53 publications

(35 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Although nonspecific uptake of particulate substances could conceivably occur in the liver endothelium (Ghitescu and Fixman, 1984) as it occurs in other sinusoidal endothelia (DeBruyn et al, 1975;Hudson and Yoffey, 19681, this uptake appears to be concentration-dependent. Nonspecific uptake of gold-labeled particles is unlikely to have occurred in this study because gold-BSA in a similar concentration was not taken up significantly.…”

Section: Discussionmentioning

confidence: 97%

Transendothelial transport (transcytosis) of iron‐transferrin complex in the rat liver

Kishimoto

Tavassoli

1987

Am. J. Anat.

View full text Add to dashboard Cite

To determine the transport pathway of iron-transferrin complex (Fe-TF) into the hepatocyte, we labeled Fe-TF with colloidal gold and perfused rat liver through the portal vein with this probe under different conditions. The tissue was then studied by transmission electron microscopy. At a cold temperature (approximately 4 degrees C), the probe bound to the luminal surface of sinusoidal endothelium without internalization. The binding was limited to the endothelium and there was no binding to Kupffer cells or hepatocytes. The binding was inhibitable in the presence of excess soluble Fe-TF, indicating the specificity of the bindings. At 37 degrees C the probe was internalized via a system of coated pits and vesicles. Morphometric analyses of the temporal sequence of events suggested that the probe was transported, in part, across the endothelium via a system of tubules and vesicles and externalized on the abluminal side via a system of coated pits. The probe was then taken up by hepatocytes. Only minimal uptake was noted when gold-labeled bovine serum albumin was used either at the low temperature or at 37 degrees C. The findings suggest that the liver uptake of Fe-TF complex by hepatocytes is a transendothelial phenomenon (transcytosis).

show abstract

Section: Discussionmentioning

confidence: 97%

Transendothelial transport (transcytosis) of iron‐transferrin complex in the rat liver

Kishimoto

Tavassoli

1987

Am. J. Anat.

View full text Add to dashboard Cite

show abstract

“…Previous work with cationized ferritin, pI 8.4, and alcian blue (17-19, 20, 22), as well as with HUP, colloidal goldconjugated albumin (1,8), or hydrazinated ferritin (V. Muresan and M. Constantinescu, Institute of Cellular Biology, Bucharest, manuscript submitted for publication), have established that cell surface of capillary endothelium contains differentiated microdomains generated by the preferential distribution of anionic sites and some glycoconjugates. In our present experiments, the results obtained with the cHUP of pI 9.0 were similar to those previously reported for cationized ferritin ofpI 8.4 (17-19, 20, 22), i.e., both ligands decorated plasmalemma, coated pits, and fenestral diaphragms but failed to label the membrane and the diaphragm of plasmalemmal vesicles and vesicle-derived channels.…”

Section: Discussionmentioning

confidence: 99%

Anionized and cationized hemeundecapeptides as probes for cell surface charge and permeability studies: differentiated labeling of endothelial plasmalemmal vesicles.

Ghinea¹,

Simiónescu²

1985

The Journal of Cell Biology

View full text Add to dashboard Cite

TO obtain small membrane markers easily accessible to the charged groups of the cell surface, we prepared, from hemeundecapeptide (HUP), three derivatives that maintain the peroxidatic activity: (a) the anionized hemeundecapeptide, Mr 1,963, estimated diameter 1.68 nm, pl 3.5, for the detection of basic groups; and both (b) a cationized hemeundecapeptide containing predominantly tertiary amino groups, Mr 2,215, estimated diameter 1.75 nm, pl 9.0, and (c) a cationized hemeundecapeptide containing only primary amino groups, Mr 2,271, estimated diameter 1.75 nm, pl 10.6, for labeling acidic residues. The markers were perfused in situ in mice to label the luminal surface of fenestrated endothelium of pancreatic capillaries. Specimens were processed through the cytochemical reaction for peroxidatic activity and examined by electron microscopy. The anionized HUP and HUP (pl 4.85) marked the plasmalemma proper, the coated pits, and the membrane and diaphragms of plasmalemmal vesicles and transendothelial channels. The cationized HUP containing predominantly tertiary amino groups (pl 9.0) decorated all cell surface components with the exception of plasmalemmal vesicles and channels; the latter were, however, labeled by the cationized HUP containing only primary groups (pl 10.6), which suggests that these structures contain on their luminal surface very weak acidic residues of high pKa values. The fact that the membrane of plasmalemmal vesicles can discriminate against permeant cationic macromolecules only up to a pl of ~9.0 indicates that in the electrostatic restriction there is a charge limit. In the case of fenestrated capillary endothelium, the upper charge limit seems to be a pl of ~9.0. In these vessels, the charge discrimination is effective for molecules as small as 2 nm.Several markers have been used to gain information about the cell surface charge. They have the limitation of either requiring prefixation (e.g., by colloidal iron), or concomitant fixation (e.g., by ruthenium red), or of being large enough (e.g., cationized ferritin) to raise the problem of their accessibility to the cell surface moieties. In order to circumvent these limitations, we prepared from hemeundecapeptide (HUP) ~ (microperoxidase M-11) two groups of derivatives that maintain their peroxidatic activity: anionized hemeundecapeptide J Abbreviations used in this paper: aHUP, anionized hemeundecapeptide; cHUP, cationized hemeundecapeptide; cHUPp, cationized hemeundecapeptide (pl 10.6) containing primary amino groups only; cHUPt, cationized hemeundecapeptide (pl 9.0) containing predominantly tertiary amino groups; HUP, hemeundecapeptide (microperoxidase-11 ).(aHUP) for the detection of basic residues, and two cationized hemeundecapeptides (cHUP) for the detection of acidic groups. These compounds have the following advantages: (a) they can be applied to fresh tissues in vivo, in situ, and in vitro; (b) owing to their small size (about 2 nm in diameter), their access to the groups of cell surface is assumed to be easier than that of...

show abstract

“…attenuated the anionic endothelial surface charge in cremaster muscle venules, illustrated by diminished deposition of the cationic dye Alcian blue, which binds to the glycocalyx in a chargedependent fashion [23][24][25] ( Figure 4I). BLOOD, 27 JANUARY 2011 ⅐ VOLUME 117, NUMBER 4 For personal use only.…”

Section: Amentioning

confidence: 99%

Myeloperoxidase attracts neutrophils by physical forces

Klinke¹,

Nußbaum

Kubala

et al. 2011

Blood

157

View full text Add to dashboard Cite

Recruitment of polymorphonuclear neutrophils (PMNs) remains a paramount prerequisite in innate immune defense and a critical cofounder in inflammatory vascular disease. Neutrophil recruitment comprises a cascade of concerted events allowing for capture, adhesion and extravasation of the leukocyte. Whereas PMN rolling, binding, and diapedesis are well characterized, receptor-mediated processes, mechanisms attenuating the electrostatic repulsion between the negatively charged glycocalyx of leukocyte and endothelium remain poorly understood. We provide evidence for myeloperoxidase (MPO), an abundant PMN-derived heme protein, facilitating PMN recruitment by its positive surface charge. In vitro, MPO evoked highly directed PMN motility, which was solely dependent on electrostatic interactions with the leukocyte's surface. In vivo, PMN recruitment was shown to be MPOdependent in a model of hepatic ischemia and reperfusion, upon intraportal delivery of MPO and in the cremaster muscle exposed to local inflammation or to intraarterial MPO application. Given MPO's affinity to both the endothelial and the leukocyte's surface, MPO evolves as a mediator of PMN recruitment because of its positive surface charge. This electrostatic MPO effect not only displays a so far unrecognized, catalysis-independent function of the enzyme, but also highlights a principal mechanism of PMN attraction driven by physical forces. (Blood. 2011; 117(4):1350-1358) IntroductionRecruitment of polymorphonuclear neutrophils (PMNs) is considered a hallmark in host defense. 1 With vessel-and tissue-infiltrating PMNs also being mechanistically linked to a broad range of vascular inflammatory diseases including coronary artery disease, heart failure and ischemia/reperfusion injury, the pathophysiologic significance of PMN motility reaches far beyond innate immunity. [2][3][4] So far, PMN migration is primarily viewed to be energydependent and cytoskeleton-dependent with G-protein coupled receptors and integrins initiating and orchestrating signaling pathways obligatory for neutrophil adhesion, spreading, diapedesis and chemotactic agitation. [5][6][7] On activation, PMN releases myeloperoxidase (MPO), an abundant heme protein in PMN with potent bactericidal and vascular-inflammatory properties. The enzyme accumulates along the endothelium and in the subendothelial space, 8 where it binds to anionic glycocalyx residues such as heparan sulfate glycosaminoglycans. Given the affinity of MPO to both PMN and endothelial cells, we evaluated whether MPO affects PMN locomotion and recruitment. Methods Isolation of PMNPeripheral blood was drawn from healthy human volunteers and heparinized, and isolation of PMN was performed as previously described. 9 In brief, after sedimentation in dextran solution (45 mg/mL), the supernatant was placed over Histopaque 1077 (Sigma-Aldrich) for density gradient centrifugation. Remaining red blood cells were eliminated by hypotonic lysis and the pellet was resuspended in Hanks balanced salt solution (HBSS; Invitrogen) containing 0...

show abstract

Surface charge distribution on the endothelial cell of liver sinusoids.

Cited by 53 publications

References 20 publications

Transendothelial transport (transcytosis) of iron‐transferrin complex in the rat liver

Transendothelial transport (transcytosis) of iron‐transferrin complex in the rat liver

Anionized and cationized hemeundecapeptides as probes for cell surface charge and permeability studies: differentiated labeling of endothelial plasmalemmal vesicles.

Myeloperoxidase attracts neutrophils by physical forces

Contact Info

Product

Resources

About