The relationships between human serum pseudocholinesterase, lipoproteins, and apolipoproteins (APOHDL)

Ryhänen, Reijo; Jauhianen, M.; Laitinen, Matti; Puhakainen, E.

doi:10.1016/0006-2944(82)90076-x

Cited by 13 publications

(7 citation statements)

References 17 publications

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“…This explains the second factor. The mechanism by which the serum cholinesterase activity level varies is extremely complex but it is certain that at least protein and lipid metabolism are related in the fluctuations of the level of this enzyme (Chu et al, 1978;Cucuian et al, 1975;Kutty et al, 1981;Ryhsnen et al, 1982). In the present study, the group with a high cholinesterase level also exhibited increases in the serum lipid contents (such as serum total cholesterol and triglyceride contents).…”

Section: ) Subjectssupporting

confidence: 45%

Evaluation of the Effects of Various Factors on the Serum Cholinesterase Activity Level

Imaki¹,

Ohguri²,

Iuchi

et al. 1995

Jpn. J. Health Hum. Ecol

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Section: ) Subjectssupporting

confidence: 45%

Evaluation of the Effects of Various Factors on the Serum Cholinesterase Activity Level

Imaki¹,

Ohguri²,

Iuchi

et al. 1995

Jpn. J. Health Hum. Ecol

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“…On the other hand, the HDL-associated acetylhydrolase is exclusively found in the HDL2 subfraction which is known to be contami nated by apo B-containing lipoproteins [22], There is also evidence that the lipopro tein-mediated hydrolysis of PAF is caused by a unique enzyme which is distinct from other lipoprotein-associated enzymes with hydrolase activity, e.g. phospholipase A2 [23], LCAT [24], and pseudocholinesterase [25]. In spite of the unique nature of the lipo protein-associated acetylhydrolase different kinetic properties were obtained with differ ent lipoprotein classes.…”

Section: Discussionmentioning

confidence: 99%

The Contribution of Individual Lipoproteins to the Degradation of Platelet-Activating Factor in Human Serum

Ostermann

Kostner²,

Gries³

et al. 1989

Pathophysiol Haemos Thromb

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Platelet-activating factor (PAF) is rapidly degraded in vivo by the action of a specific acetylhydrolase. Measuring the PAF-acetylhydrolase activity in serum from 12 healthy volunteers a maximum velocity of 67.2 ± 11.8 nmol/min × ml and a K_m value of 15.8 ± 2.9 μmol/l were ascertained. More than 90% of the activity was found to be associated with lipoproteins. It was detected in isolated VLDL, LDL, Lp(a) as well as HDL₂ but not in HDL₃. The PAF-acetylhydrolase activities associated with the various lipoproteins were shown to behave like a unique enzyme with distinct kinetic properties. Because VLDL and LDL were found to take up about 5 and 2.5 times more PAF with respect to their mass than HDL, it is concluded that lipoproteins affect the PAF-acetylhydrolase activity at the level of substrate presentation. As a consequence of the distinct kinetic properties, the lipoprotein-associated PAF-acetylhydrolase activities do not contribute proportionately to the degradation of PAF in serum. The latter is shown to depend primarily on the amount of PAF-acetylhydrolase bound to the apoprotein B-containing lipoproteins.

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“…Although the physiological role of BChE remains unknown, its participation in lipid metabolism has been suggested by different types of data. It was shown that subcutaneous fat and BChE activity are positively correlated (Berry et al, 1954), and a physical association between BChE and lipoproteins such as LDL (Lawrence and Melnick, 1961;Dubbs, 1966;Kutty and Acharya, 1972;Kutty et al, 1973Kutty et al, , 1975Kutty et al, , 1977Ryhä nen et al, 1982) as well as HDL (Ryhä nen et al, 1982) was reported. Positive associations of BChE activity and body weight are wellknown (Simpson, 1966;Cucuianu et al, 1968;Stueber-Odebrecht et al, 1985;Brock and Brock, 1990;Chautard-Freire-Maia et al, 1990).…”

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confidence: 99%

Possible influence of BCHE locus of butyrylcholinesterase on stature and body mass index

Souza

Picheth

Allebrandt

et al. 2004

American J Phys Anthropol

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Butyrylcholinesterase activity has been shown to be positively associated with weight and body mass index (BMI). The present study was carried out to search for an association between variants of the BCHE gene and weight, stature, and BMI on the basis of means and variances compared between nonusual variants and their respective usual controls. Individuals bearing the atypical mutation (N = 52) did not differ from their usual phenotype controls (N = 104) in these parameters. The BCHE*U/BCHE*K individuals (N = 222) presented a significantly higher BMI variance than their BCHE*U/BCHE*U controls (N = 222, F = 1.40, P = 0.012). This higher BMI variance does not seem to be an isolated effect of the K mutation, but appears to be the result of an interaction between the K allele and the usual allele, since no such difference in variance was detected between BCHE*K/BCHE*K individuals (N = 23) and their BCHE*U/BCHE*U (N = 23) controls. These data may suggest a relation between variability in the BCHE locus itself and BMI. Individuals with the BCHE UF phenotype (N = 45) showed a significantly higher mean stature (about 3 cm more; P = 0.02) than their controls with the usual phenotype (N = 135). A role in cell proliferation has been proposed for BCHE, and since growth depends on the number of mitoses, it is not unexpected that variants of this enzyme may influence body stature in different ways. This study reports the first data on the relation of BCHE alleles to anthropometric characters.

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The relationships between human serum pseudocholinesterase, lipoproteins, and apolipoproteins (APOHDL)

Cited by 13 publications

References 17 publications

Evaluation of the Effects of Various Factors on the Serum Cholinesterase Activity Level

Evaluation of the Effects of Various Factors on the Serum Cholinesterase Activity Level

The Contribution of Individual Lipoproteins to the Degradation of Platelet-Activating Factor in Human Serum

Possible influence of BCHE locus of butyrylcholinesterase on stature and body mass index

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