scholarly journals INTESTINAL CAPILLARIES

1969 ◽  
Vol 41 (1) ◽  
pp. 33-58 ◽  
Author(s):  
F. Clementi ◽  
G. E. Palade
Keyword(s):  
Electron Microscopy ◽  
Horseradish Peroxidase ◽  
Intestinal Mucosa ◽  
Intercellular Junctions ◽  
Post Injection ◽  
Pore System ◽  
Blood Capillaries ◽  
Large Pore ◽  
Small Pore ◽  
Histochemical Procedure

Horseradish peroxidase (mol. diam. ≃50 A) and ferritin (mol. diam. ≃110 A) were used as probe molecules for the small and large pore system, respectively, in blood capillaries of the intestinal mucosa of the mouse. Peroxidase distribution was followed in time, after intravenous injection, by applying the Graham-Karnovsky histochemical procedure to aldehyde-fixed specimens. The tracer was found to leave the plasma rapidly and to reach the pericapillary spaces 1 min post injection. Between 1 min and 1 min 30 sec, gradients of peroxidase reaction product could be demonstrated regularly around the capillaries; their highs were located opposite the fenestrated parts of the endothelium. These gradients were replaced by even distribution past 1 min 30 sec. Ferritin, followed directly by electron microscopy, appeared in the pericapillary spaces 3–4 min after i.v. injection. Like peroxidase, it initially produced transient gradients with highs opposite the fenestrated parts of the endothelium. For both tracers, there was no evidence of movement through intercellular junctions, and transport by plasmalemmal vesicles appeared less efficient than outflow through fenestrae. It is concluded that, in the blood capillaries of the inintestinal mucosa, the diaphragms of the endothelial fenestrae contain the structural equivalents of the small pore system. The large pore system seems to be restricted to a fraction of the fenestral population which presumably consists of diaphragm-free or diaphragm-deficient units.

Plasmalemmal vesicles represent the large pore system of continuous microvascular endothelium

1993 ◽  
Vol 265 (2) ◽  
pp. H725-H733 ◽  
Author(s):  
D. Predescu ◽  
G. E. Palade
Keyword(s):  
Intercellular Junctions ◽  
Pore System ◽  
Microvascular Endothelium ◽  
Plasmalemmal Vesicles ◽  
Morphological Studies ◽  
Large Pore ◽  
In Transit

In the capillary physiology literature, molecules and particles larger than 10 nm are assumed to leave the plasma mostly through large pores located at the level of intercellular junctions in microvessels lined with a continuous endothelium. In morphological studies of similar microvessels, outgoing particles > 10 nm were detected in endothelial plasmalemmal vesicles not in intercellular junctions. Because the probes may not be found in transit through the junctions because they may be swept away by strong currents generated by Starling forces, we have examined a large number of junctions in arteriolar, capillary, and venular segments of bipolar vascular fields of mouse diaphragms collected after perfusion with large pore probes. The results presented in this study indicate that 1) the perfused probes accumulate in the luminal introits of the junctions as filtration residues that decrease in size and frequency from arterioles to venules, and 2) large pore probes move across the endothelium exclusively through plasmalemmal vesicles.

Transport properties of alveolar epithelium measured by molecular hetastarch absorption in isolated rat lungs

2001 ◽  
Vol 91 (4) ◽  
pp. 1730-1740 ◽  
Author(s):  
Robert L. Conhaim ◽  
Kal E. Watson ◽  
Stephen J. Lai-Fook ◽  
Bruce A. Harms
Keyword(s):  
Molecular Weight ◽  
Transport Properties ◽  
High Molecular Weight ◽  
Pore Radius ◽  
Alveolar Epithelium ◽  
Low Molecular Weight ◽  
Pore System ◽  
Large Pore ◽  
Small Pore ◽  
Isolated Rat

To evaluate the transport properties of the alveolar epithelium, we instilled hetastarch (Het; 6%, 10 ml, 1 − 1 × 104kDa) into the trachea of isolated rat lungs and then measured the molecular distribution of Het that entered the lung perfusate from the air space over 6 h. Het transport was driven by either diffusion or an oncotic gradient. Perfusate Het had a unique, bimodal molecular weight distribution, consisting of a narrow low-molecular-weight peak at 10–15 kDa (range, 5–46 kDa) and a broad high-molecular-weight band (range 46–2,000 kDa; highest at 288 kDa). We modeled the low-molecular-weight transport as (passive) restricted diffusion or osmotic flow through a small-pore system and the high-molecular-weight transport as passive transport through a large-pore system. The equivalent small-pore radius was 5.0 nm, with a distribution of 150 pores per alveolus. The equivalent large-pore radius was 17.0 nm, with a distribution of one pore per seven alveoli. The small-pore fluid conductivity (2 × 10−5ml · h−1 · cm−2 · mmHg−1) was 10-fold larger than that of the large-pore conductivity.

scholarly journals PERMEABILITY OF MUSCLE CAPILLARIES TO EXOGENOUS MYOGLOBIN

1973 ◽  
Vol 57 (2) ◽  
pp. 424-452 ◽  
Author(s):  
Nicolae Simionescu ◽  
Maia Simionescu ◽  
George E. Palade
Keyword(s):  
Gel Filtration ◽  
Intercellular Junctions ◽  
Cell Periphery ◽  
Pore System ◽  
Regional Heterogeneity ◽  
Plasmalemmal Vesicles ◽  
Small Pore ◽  
Perinuclear Cytoplasm ◽  
Muscle Capillaries

Whale skeletal muscle myoglobin (mol wt 17,800; molecular dimensions 25 x 34 x 42 Å) was used as a probe molecule for the pore systems of muscle capillaries. Diaphragms of Wistar-Furth rats were fixed in situ at intervals up to 4 h after the intravenous injection of the tracer, and myoglobin was localized in the tissue by a peroxidase reaction. Gel filtration of plasma samples proved that myoglobin molecules remained in circulation in native monomeric form. At 30–35 s postinjection, the tracer marked ∼75% of the plasmalemmal vesicles on the blood front of the endothelium, 15% of those located inside and none of those on the tissue front. At 45 s, the labeling of vesicles in the inner group reached 60% but remained nil for those on the tissue front. Marked vesicles appeared on the latter past 45 s and their frequency increased to ∼80% by 60–75 s, concomitantly with the appearance of myoglobin in the pericapillary spaces. Significant regional heterogeneity in initial labeling was found in the different segments of the endothelium (i.e., perinuclear cytoplasm, organelle region, cell periphery, and parajunctional zone). Up to 60 s, the intercellular junctions and spaces of the endothelium were free of myoglobin reaction product; thereafter, the latter was detected in the distal part of the intercellular spaces in concentration generally equal to or lower than that prevailing in the adjacent pericapillary space. The findings indicate that myoglobin molecules cross the endothelium of muscle capillaries primarily via plasmalemmal vesicles. Since a molecule of this size is supposed to exit through both pore systems, our results confirm the earlier conclusion that the plasmalemmal vesicles represent the large pore system; in addition, they suggest that the same structures are, at least in part, the structural equivalent of the small pore system of this type of capillaries.

Comparative strengths and weaknesses of peroxidase and colloidal gold in pre- and post-embedding immunolabeling techniques

1987 ◽  
Vol 45 ◽  
pp. 1002-1005
Author(s):  
D. R. Abrahamson ◽  
P. L. St.John ◽  
E. W. Perry
Keyword(s):  
Electron Microscopy ◽  
Horseradish Peroxidase ◽  
Light Microscopy ◽  
Colloidal Gold ◽  
Light Microscope ◽  
Ultrastructural Localization ◽  
The Other ◽  
Quantitative Studies ◽  
Dense Suspension ◽  
Antigen Localization

Antibodies coupled to tracers for electron microscopy have been instrumental in the ultrastructural localization of antigens within cells and tissues. Among the most popular tracers are horseradish peroxidase (HRP), an enzyme that yields an osmiophilic reaction product, and colloidal gold, an electron dense suspension of particles. Some advantages of IgG-HRP conjugates are that they are readily synthesized, relatively small, and the immunolabeling obtained in a given experiment can be evaluated in the light microscope. In contrast, colloidal gold conjugates are available in different size ranges and multiple labeling as well as quantitative studies can therefore be undertaken through particle counting. On the other hand, gold conjugates are generally larger than those of HRP but usually can not be visualized with light microscopy. Concern has been raised, however, that HRP reaction product, which is exquisitely sensitive when generated properly, may in some cases distribute to sites distant from the original binding of the conjugate and therefore result in spurious antigen localization.

scholarly journals Uniform synthesis of palladium species confined in a small-pore zeolite via full ion-exchange investigated by cryogenic electron microscopy

2021 ◽  
Author(s):  
Yongwoo Kim ◽  
Jongbaek Sung ◽  
Sungsu Kang ◽  
Jaeha Lee ◽  
Min-Ho Kang ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Ion Exchange ◽  
Small Pore ◽  
Catalytic Applications

Uniformly dispersed palladium species in small-pore zeolite are successfully prepared for catalytic applications, and are investigated by advanced microscopic methods.

Intestinal Lesions Containing Coronavirus-like Particles in Neonatal Necrotizing Enterocolitis: An Ultrastructural Analysis

PEDIATRICS ◽  
1984 ◽  
Vol 73 (2) ◽  
pp. 218-224
Author(s):  
S. Rousset ◽  
O. Moscovici ◽  
P. Lebon ◽  
J. P. Barbet ◽  
P. Helardot ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Small Intestine ◽  
Necrotizing Enterocolitis ◽  
Intestinal Mucosa ◽  
Light And Electron Microscopy ◽  
Anaerobic Bacteria ◽  
Intestinal Lesions ◽  
Maternity Hospitals ◽  
Neonatal Necrotizing Enterocolitis

Since the outbreaks of neonatal necrotizing enterocolitis occurring in maternity hospitals of Paris and suburbs in 1979-1980, it has been possible to examine by light and electron microscopy gut specimens from ten newborns with this illness. Coronavirus-like particles, enclosed in intracytoplasmic vesicles of damaged epithelial cells of the intestinal mucosa, were observed in the small intestine, appendix, and colon. The ultrastructural study, supported by bacteriologic findings, suggests the role of coronavirus-like particles in the appearance of the lesions. Secondary proliferation of mainly anaerobic bacteria, probably responsible for pneumatosis, may aggravate the disease.

Abstract 15925: Localization of Nav1.5 at the Intercellular Junctions Resolved by Diffraction-Unlimited Microscopy in Three Dimensions and by Correlative Light-Electron Microscopy

Circulation ◽  
2014 ◽  
Vol 130 (suppl_2) ◽  
Author(s):  
Alejandra Leo-Macias ◽  
Esperanza Agullo-Pascual ◽  
Eli Rothenberg ◽  
Mario Delmar
Keyword(s):  
Electron Microscopy ◽  
Sodium Channel ◽  
Ventricular Myocytes ◽  
Sodium Current ◽  
Intercellular Junctions ◽  
Three Dimensions ◽  
Macromolecular Complex ◽  
Adult Heart ◽  
Mechanical Coupling ◽  
Cardiac Sodium Channel

Sodium current amplitude, kinetics and regulation depend on the properties of the pore-forming protein (mostly NaV1.5 in adult heart) and on the specific molecular partners with which the channel protein associates. The composition of the voltage-gated sodium channel macromolecular complex is location-specific; yet, the exact position of NaV1.5 in the subcellular landscape of the intercalated disc (ID), remains unclear. We implemented diffraction unlimited microscopy (direct stochastic optical reconstruction microscopy, or “dSTORM”) to localize the pore-forming subunit of the cardiac sodium channel NaV1.5 with a resolution of 20nm on the XY plane. In isolated adult ventricular myocytes, NaV1.5 was found in distinct semi-circular clusters. When the entire population of clusters within a 500 nm window from the ID was considered (more than 350 individual clusters analyzed), 75% of them localized to N-cadherin rich sites. NaV1.5-distal clusters were found at an average 313±15 nm from the cell end. Introducing an astigmatic lens in the light path allowed us to solve cluster location in three dimensions, at resolutions of 20 nm in XY and 40 nm in the z plane. Three-dimensional images confirmed the preferential localization at or near N-cadherin plaques, and further suggested that NaV1.5 arrives to the membrane via N-cadherin-anchored paths, most likely microtubules. In additional experiments, we developed a novel approach to correlate the image of NaV1.5 clusters by dSTORM with the cellular ultrastructure as resolved by electron microscopy on the same sample. This “correlative light-electron microscopy” method confirmed the preference of NaV1.5 clusters at sites of mechanical coupling. Overall, we provide the first ultrastructural description of NaV1.5 at the cardiac ID and its relation with the major electron-dense domains of the adult heart. Our data support a model by which microtubule-mediated delivery of NaV1.5 anchors at N-cadherin-rich sites, likely “mixed junctions” also containing desmosomal molecules (such as plakophilin-2; see Cerrone et al; Circulation 129:1092-1103, 2014) and connexin43. These findings have major implications to the understanding of sodium current disruption in diseases affecting the integrity of the ID.

CTAB-assisted size controlled synthesis of SAPO-34 and its contribution toward MTO performance

2018 ◽  
Vol 47 (29) ◽  
pp. 9861-9870 ◽  
Author(s):  
Syed ul Hasnain Bakhtiar ◽  
Xiaotong Wang ◽  
Sher Ali ◽  
Fulong Yuan ◽  
Zhibin Li ◽  
...  
Keyword(s):  
Controlled Synthesis ◽  
Pore System ◽  
Light Olefin ◽  
Diffusion Limitations ◽  
Small Pore ◽  
Methanol To Olefin ◽  
Olefin Selectivity ◽  
Size Controlled

SAPO-34 shows higher light olefin selectivity in the reaction of methanol to olefin (MTO), but its small pore system implies diffusion limitations to bigger molecular products and results in coking too.

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