A subchronic study of the toxicity of an orally administered benzoquinolizinyl derivative in the rat and dog

Hartnagel, Ralph E.; Phillips, Barrie M.; Kraus, P.; Kowalski, Robert L.; Fonseca, Emma H.

doi:10.1016/0300-483x(75)90101-8

Cited by 5 publications

(2 citation statements)

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“…SAP isoenzymes appear to be modified when compared to tissue AP, particularly in regard to molecular size and, in some cases, carbohydrate structure. indicated by histopathology [7,10,15], sug gesting that there may be other mechanisms leading to high SAP levels that are not re lated to hepatotoxicity.To better understand drug-associated, non-hepatotoxicological SAP elevations in the adult dog, it is first necessary to deter mine the normal composition of canine SAP. Human serum, for example, is known to contain SAP isoenzymes of hepatic, intes tinal, osseous, renal, and pulmonary origin [2], But sera of normal dogs have variously been described as containing SAP only of osseous origin [4], primarily of hepatic ori gin [3], or of both hepatic and osseous origin…”

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confidence: 99%

Characterization of Alkaline Phosphatase in Canine Serum

Amacher¹,

Smith²,

Martz³

et al. 1987

Enzyme

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On the basis of carbohydrate structure, normal dog serum contains three basic types of serum alkaline phosphatase (SAP) corresponding to (1) highly branched complex (non-concanavalin A-binding), (2) complex, or (3) high-mannose (both concanavalin Abinding) oligosaccharide structures. Subsequent binding experiments with monoclonal antibody to intestinal alkaline phosphatase (AP) and bromotetramisole inhibition studies clearly indicated the presence of intestinal-like SAP. Concanavalin A (Con-A) binding characteristics suggested the presence of a bone-like SAP. Con-A-binding and isoelectric focusing results revealed the presence of two (type lb and lib) major SAP isoenzymes thought to be of hepatic origin. SAP isoenzymes appear to be modified when compared to tissue AP, particularly in regard to molecular size and, in some cases, carbohydrate structure.

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confidence: 99%

Characterization of Alkaline Phosphatase in Canine Serum

Amacher¹,

Smith²,

Martz³

et al. 1987

Enzyme

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“…The elevation of serum alkaline phospha tase (AP) has been noted in a number of experimental studies when dogs were treated with compounds that caused few if any toxi cological effects [1][2][3], Although elevated se rum AP has long been known to accompany drug-induced cholestasis in various species [4], its significance in the absence of histopathologically detectable liver damage is not clear. The interpretation of serum AP eleva tions observed in experimental studies is hindered by a general lack of information on but the organ sources of two of the AP enzymes could only be identified by indirect methods.…”

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confidence: 99%

Further Characterization of Serum Alkaline Phosphatase from Male and Female Beagle Dogs

Amacher

Higgins²,

Schomaker³

et al. 1989

Enzyme

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Alkaline phosphatase (AP) from the sera of both male and female beagle dogs was partially purified and then analyzed for the presence of AP isoenzymes having intestinal or osseous characteristics as detected by bromotetramisole inhibition or wheat germ lectin agarose electrophoresis, respectively. The sera from both sexes were similar in regard to the presence of AP isoenzymes with intestinal (16 vs. 20%) or osseous (19 vs. 23%) characteristics, but serum AP from the male had a greater sialic acid content and only the male serum contained a detectable constitutive acidic (pI = 3.4) AP isoenzyme. This was similar to a serum AP isoenzyme previously found elevated in the sera of dogs afflicted with hyperadrenocorticalism or of dogs treated with certain corticosteroids.

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