TY - JOUR
T1 - Polymorphism of Acetylcholinesterase in Discrete Regions of the Developing Human Fetal Brain
AU - Zakut, Haim
AU - Matzkel, Avi
AU - Schejter, Eduardo
AU - Avni, Adi
AU - Soreq, Hermona
PY - 1985/8
Y1 - 1985/8
N2 - Abstract: The molecular forms and membrane association of acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7) and pseudocholinesterase (acylcholine acylhydrolase, EC 3.1.1.8) were determined in the presence of protease inhibitors in dissected regions of developing human fetal brain, as compared with parallel areas from mature brain. All areas contained substantial cholinesterase activities, of which acetylcholinesterase accounted for almost all the activity. Two major forms of acetylcholinesterase activity, sedimenting at 10–11S and 4–5S, respectively, were detected on sucrose gradients and possessed similar catalytic properties, as judged by their individual Km values toward [3H]acetylcholine (ca. 4 × 10−4M). The ratio between these forms varied by up to four‐ to fivefold, both between different areas and within particular areas at various developmental stages, but reached similar values (about 5:2) in all areas of mature brain. Acetylcholinesterase activity was ca. 35–50% lowsalt‐soluble and 45–65% detergent‐soluble in various developmental stages and brain areas, with an increase during development of the detergent‐soluble fraction of the light form. In contrast, pseudocholinesterase activity was mostly low‐salt‐soluble and sedimented as one component of 10–11S in all areas and developmental stages. Our findings suggest noncoordinate regulation of brain acetylcholinesterase and pseudocholinesterase, and indicate that the expression of acetylcholinesterase forms within embryonic brain areas depends both on cell type composition and on development.
AB - Abstract: The molecular forms and membrane association of acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7) and pseudocholinesterase (acylcholine acylhydrolase, EC 3.1.1.8) were determined in the presence of protease inhibitors in dissected regions of developing human fetal brain, as compared with parallel areas from mature brain. All areas contained substantial cholinesterase activities, of which acetylcholinesterase accounted for almost all the activity. Two major forms of acetylcholinesterase activity, sedimenting at 10–11S and 4–5S, respectively, were detected on sucrose gradients and possessed similar catalytic properties, as judged by their individual Km values toward [3H]acetylcholine (ca. 4 × 10−4M). The ratio between these forms varied by up to four‐ to fivefold, both between different areas and within particular areas at various developmental stages, but reached similar values (about 5:2) in all areas of mature brain. Acetylcholinesterase activity was ca. 35–50% lowsalt‐soluble and 45–65% detergent‐soluble in various developmental stages and brain areas, with an increase during development of the detergent‐soluble fraction of the light form. In contrast, pseudocholinesterase activity was mostly low‐salt‐soluble and sedimented as one component of 10–11S in all areas and developmental stages. Our findings suggest noncoordinate regulation of brain acetylcholinesterase and pseudocholinesterase, and indicate that the expression of acetylcholinesterase forms within embryonic brain areas depends both on cell type composition and on development.
KW - Acetylcholinesterase
KW - Fetal human brain
KW - Molecular forms
KW - Polymorphism
KW - Protease inhibitors
KW - Pseudocholinesterase
UR - http://www.scopus.com/inward/record.url?scp=0022004819&partnerID=8YFLogxK
U2 - 10.1111/j.1471-4159.1985.tb03999.x
DO - 10.1111/j.1471-4159.1985.tb03999.x
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C2 - 4009167
AN - SCOPUS:0022004819
SN - 0022-3042
VL - 45
SP - 382
EP - 389
JO - Journal of Neurochemistry
JF - Journal of Neurochemistry
IS - 2
ER -