Adenosine Triphosphatase Activity of the Vascular System.

Cj, Carr; Fk, Bell; Jc, Krantz

doi:10.3181/00379727-80-19611

Cited by 13 publications

(6 citation statements)

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“…Separate determinations on individual layers of blood vessel walls were seldom carried out. With respect to dephosphorylating enzymes, the large arteries were found to have very low alkaline phosphatase activity (12)(13)(14)(15)(16)(17)(18) and high acid phosphatase (13,18), 5nucleotidase (14)(15)(16)(17)(18)23), and adenosinetriphosphatase (16)(17)(18)(19)(20)(21)(22) activities. Of these, only adenosinetriphosphatase was determined in veins and arteries of various sizes (18,20,22), the highest activity being found in muscular arteries (18,20) or in the aorta (22).…”

Section: Figurementioning

confidence: 99%

“…Of these, only adenosinetriphosphatase was determined in veins and arteries of various sizes (18,20,22), the highest activity being found in muscular arteries (18,20) or in the aorta (22). No activity was found in veins (22). These quantitative results are concordant with the histochemical demonstration of high acid phosphatase (61,62), 5-nucleotidase (16,(63)(64)(65)(66)(67)(68)(69), and adenosinetriphosphatase (16,(67)(68)(69)(70) activities in the media of arteries.…”

Section: Figurementioning

confidence: 99%

“…Quantitative chemical studies of non-specific alkaline phosphatase have been limited to large blood vessels (12)(13)(14)(15)(16)(17)(18). The activity of this group of enzymes in such vessels was found to be very low and certainly disproportionate to that of other phosphatases (13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23).…”

Section: Introductionmentioning

confidence: 99%

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Localized Areas of High Alkaline Phosphatase Activity in the Terminal Arterial Tree

Romanul

Bannister

1962

The Journal of Cell Biology

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Fresh frozen skeletal muscles of rats, rabbits, and humans were sectioned in a cryostat. Sections 12 to 32 micra thick were incubated in a substrate solution for the histochemical demonstration of non-specific alkaline phosphatase activity. A modified azo dye coupling technique was used at pH 9.5. Localized areas of high enzymatic activity were found in specific and well defined areas along the terminal arterial tree, in addition to the activity which has been previously described in capillary endothelium. Arterial branches with luminal diameters of 25 micra or less showed staining of their endothelium starting abruptly at their origin from the parent vessel and fading distally. Smaller arterial branches showed the same localization of enzymatic activity and stained more intensely. Other organs of rats surveyed showed arterial branches with the same pattern of staining. Identical results were obtained using the Gomori technique for alkaline phosphatase. Extensive saline perfusion of the vascular tree did not affect the observed localization of enzymatic activity. The enzymatic activity described may be part of the mechanism regulating the blood flow.

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Section: Figurementioning

confidence: 99%

Section: Figurementioning

confidence: 99%

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Localized Areas of High Alkaline Phosphatase Activity in the Terminal Arterial Tree

Romanul

Bannister

1962

The Journal of Cell Biology

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“…The sodium-potassium (Na/-K*)-dependent ATP-ase enzyme is one of this family which is difficult to demonstrate by the conventional method of histochemistry, though several methods have been developed to localize it in recent years. Carr et al (1952) demonstrate the presence of ATP-ase enzyme in the dog, frog, chicken, guinea pig, and rabbit aorta. In addition.…”

Section: Introductionmentioning

confidence: 85%

“…The venous system, however, is devoid of the enzymic activity. The aorta has greater ATP-ase activity than the coronary, carotid and renal arteries, which seemingly share equal amounts (Carr et al, 1952). Further, Balo et al (1948) report the presence of soluble ATP-ase in the aortic tissue which is different from the ATP-ase of the myosin of the muscle.…”

Section: Introductionmentioning

confidence: 99%

Morphologic studies of the carotid rete-cavernous sinus complex and its functional significance in sheep and goat

Khamas

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The carotid rete-cavernous sinus complex of sheep and goat (adult and feti) was investigated. Intra-vascular injection materials (Latex, Batson's #17 and Decopour) were employed to describe the blood vessels of this structure. Further, paraffin embedded sections were stained with Harris' hematoxylin and eosin. Van Gieson's, Gomori one-step trichrome and Weigert. After maceration, some injected vessels were used to study the carotid rete-cavernous sinus complex with scanning electron micro scope (SEM). In addition, aldehyde fixed, cryofractured complexes were studied with the SEM. The complex was sectioned with the cryostat and several laboratory procedures were performed to detect the presence of alkaline phosphatase (A.P.), 5~-nucleotidase (5"-N) and adenosine triphosphatase (ATP-ase) enzymes. Gross study revealed that the carotid rete was supplied with blood by one caudal rete branch, and two to four rostral rete branches which were normally found. The extracranial portion of the internal carotid artery was postnatally absent in both sheep and goat specimens. Light microscopic examination showed that the carotid rete branches were mediumsized, muscular arteries. These arterial branches shared a common tunica adventitia with the cavernous sinus. The carotid body cells were observed in an aberrant position (intracranially in the wall of the internal carotid artery) due to regression of the extracranial portion of the in ternal carotid artery after birth. The cavernous sinus, on the other hand, showed variations in thickness of the wall from region to region. In

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