Histochemical identification of the vascular endothelial isoenzyme of alkaline phosphatase.

Zoellner, Hans; Hunter, Norvell W.

doi:10.1177/37.12.2584695

Cited by 33 publications

(17 citation statements)

References 9 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This result differs from the general idea that the two TNAP isoforms are expressed independently, except in the diaphragm in which the liver transcript has been reported contemporaneously with the bone transcript (Studer et al 1991). Second, with respect to endothelial cells, AP activity detected in brain vessels has, until now, been attributed to TNAP on an indirect basis (Zoellner and Hunter 1989). We have shown here that brain endothelial cells, either of mouse (pMBMEC) or human (hCMEC/D3) origin, specifically express the TNAP isoform driven by the promoter specific for bone exon 1A.…”

Section: Discussioncontrasting

confidence: 77%

Differential expression of the bone and the liver tissue non-specific alkaline phosphatase isoforms in brain tissues

et al. 2010

View full text Add to dashboard Cite

The enzyme tissue non-specific alkaline phosphatase (TNAP) belongs to the ectophosphatase family. It is present in large amounts in bone in which it plays a role in mineralization but little is known about its function in other tissues. Arguments are accumulating for its involvement in the brain, in particular in view of the neurological symptoms accompanying human TNAP deficiencies. We have previously shown, by histochemistry, alkaline phosphatase (AP) activity in monkey brain vessels and parenchyma in which AP exhibits specific patterns. Here, we clearly attribute this activity to TNAP expression rather than to other APs in primates (human and marmoset) and in rodents (rat and mouse). We have not found any brain-specific transcripts but our data demonstrate that neuronal and endothelial cells exclusively express the bone TNAP transcript in all species tested, except in mouse neurons in which liver TNAP transcripts have also been detected. Moreover, we highlight the developmental regulation of TNAP expression; this also acts during neuronal differentiation. Our study should help to characterize the regulation of the expression of this ectophosphatase in various cell types of the central nervous system.

show abstract

Section: Discussioncontrasting

confidence: 77%

Differential expression of the bone and the liver tissue non-specific alkaline phosphatase isoforms in brain tissues

et al. 2010

View full text Add to dashboard Cite

show abstract

“…1A-B; central areas shaded in light gray). Although little is known about the specific function of hepatic alkaline phosphatase, 29 the heterogeneity of sinusoidal endothelial cells correlates with structural differences among sinusoids of different origin 9 and thus supports a differentiation of "portal" and "septal" sinusoids in human liver. [16][17][18] General Organization of the Parenchyma.…”

Section: Resultsmentioning

confidence: 97%

The modular microarchitecture of human liver†

Teutsch

2005

Hepatology

View full text Add to dashboard Cite

The morphological homogeneity of the liver parenchyma has represented a major obstacle in finding an acceptable definition of the structural/functional units of the liver. Concepts such as the "lobule," the "portal unit" and the "acinus" remain debatable. This study investigates the modular microarchitecture on the basis of the lobular concept. Using alkaline phosphatase activity as a histochemical marker, modules could be recognized clearly. In autopsy specimens of human liver, modules were traced through sequential cryosections, and a "secondary" module having a height of 1.9 mm, a surface of 14.7 mm 2 , and a volume of 5.1 mm 3 was reconstructed three-dimensionally. It was subdivided into 14 "primary" modules by portal tracts and vascular septa and by a common draining central venular tree. Primary modules were polyhedral, with seven to nine facets, having heights from 0.3 to 0.9 mm, surface areas from 1.7 to 5.0 mm 2 , and volumes from 0.1 to 0.9 mm 3 . Such variation in shape and size is considered an important part of the modular organization of the human liver. In conclusion, the findings on the three-dimensionality and microcirculation of liver modules support and extend the lobular concept and, at the same time, make apparent the shortcomings of the concepts of acinar and portal units. The results of this study should permit a better interpretation of histological sections of normal and pathological liver and provide a basis for understanding the metabolic heterogeneity of liver cells and their functional integration into parenchymal units. (HEPATOLOGY 2005;42:317-325.)

show abstract

“…Several major isoenzymes of AlPase are distinguishable on the basis of biochemical and antigenic characteristics (Harris, 1982;Henthorn et al, 1987;Kam et al, 1985;Weiss et al, 1988). In the present study, we dealt with the vascular isoenzyme of AlPase (Schultz-Hector et al, 1993;Zoellner and Hunter, 1989) because its reactivity was confined exclusively to the capillary network. We observed a significant induction of AlPase reactivity after exposure to LPS manifested by an increase of the number of enzymatically positive capillaries and intensity of their cytochemical reaction.…”

Section: Discussionmentioning

confidence: 99%

Lipopolysaccharide administration increases acid and alkaline phosphatase reactivity in the cardiac muscle

Okada

Zinchuk

Seguchi

2002

Microscopy Res & Technique

View full text Add to dashboard Cite

The effect of lipopolysaccharide (LPS) administration on the in situ distribution of the reaction product of acid phosphatase (AcPase) and alkaline phosphatase (AlPase) activity was examined in the rat cardiac muscle using catalytical cytochemistry. Tissues of the heart were fixed and then incubated in reaction media for detection of AcPase and AlPase reactivity. In normal hearts, reaction product of AcPase activity was observed in lysosomes. AlPase reactivity was detected at the extracellular surface of the capillary endothelilal cells and in their caveolae. Following LPS administration, the number and the size of lysosomes possessing AcPase reactivity as well as their electron density significantly increased. Furthermore, they tended to form groups consisting of three to five lysosomes. Cytochemical reaction 2 and 24 hours after injection was similar. One week later, the reaction returned to its normal pattern. As in the case with AcPase, the first changes of the distribution of the reaction product of AlPase activity were detected 2 hours after injection. The changes included a remarkable increase of the number of enzymatically positive capillaries, intensified cytochemical reaction in endothelial cells, and an increased number of caveolae. Again, no noticeable differences in reactivity were observed 2 and 24 hours after injection and the reaction returned to normal one week later. Collectively, our data indicate that both cardiac AcPase and AlPase are affected early after injection of LPS. Although the pattern of cytochemical reaction of both phosphatases was restored one week later, it is believed that the altered distribution of their reactivity in early periods after LPS administration may be a factor contributing to the development of pathological changes in this organ at a later stage.

show abstract

Histochemical identification of the vascular endothelial isoenzyme of alkaline phosphatase.

Cited by 33 publications

References 9 publications

Differential expression of the bone and the liver tissue non-specific alkaline phosphatase isoforms in brain tissues

Differential expression of the bone and the liver tissue non-specific alkaline phosphatase isoforms in brain tissues

The modular microarchitecture of human liver†

Lipopolysaccharide administration increases acid and alkaline phosphatase reactivity in the cardiac muscle

Contact Info

Product

Resources

About