Chemical heterogeneity of the striosomal compartment in the human striatum.
The neurochemical organization of the striosomal compartment in the human striatum was analyzed by histochemical and immunohistochemical techniques applied to postmortem tissue from normal individuals. The striosomes were delineated by using the following markers: acetylcholinesterase (AChE), enkephalin (ENK), substance P (SP), calbindin-D28k (CB), parvalbumin (PV), calretinin (CR), limbic system-associated membrane protein (LAMP), choline acetyltransferase (ChAT), tyrosine hydroxylase (TH), and NADPH-diaphorase. Comparisons were made between striosomal boundaries, as outlined by each marker applied on adjacent sections, and particular attention was paid to possible variations in the chemical features of striosomes along the rostrocaudal extent of the striatum. The main findings of this study are as follows: 1) the striosomal compartment is composed of two chemically distinct domains: a core and a peripheral region; 2) the core is largely devoid of CB and displays a less intense staining for ENK and LAMP than the peripheral region; 3) although striosomes are largely devoid of AChE, the activity of this enzyme is slightly higher in the core than in the peripheral region; 4) the core and peripheral regions are weakly stained for PV and intensely stained for SP; 5) ChAT-, CR- and NADPH-diaphorase-positive neurons are preferentially distributed in the peripheral region; 6) at rostral striatal levels, striosomes are largely devoid of TH, whereas the inverse is true caudally; and 7) at caudal striatal levels, the peripheral region of striosomes is intensely stained for CB and ChAT. These results demonstrate that the striosomes in human display a strikingly complex and heterogeneous chemical architecture.
Prensa
L
L
Laboratoire de Neurobiologie, Centre de Recherche Université Laval Robert-Giffard, Beauport, Québec G1J 2G3, Canada.
Giménez-Amaya
J M
JM
Parent
A
A
D000110:Acetylcholinesterase / Q000032:analysis; D000328:Adult; D000368:Aged; D064092:Calbindin 1; D064032:Calbindin 2; D064026:Calbindins; D015816:Cell Adhesion Molecules, Neuronal / Q000032:analysis; D002795:Choline O-Acetyltransferase / Q000032:analysis; D002799:Cholinergic Fibers / Q000737:chemistry / Q000201:enzymology; D003342:Corpus Striatum / Q000737:chemistry* / Q000166:cytology / Q000201:enzymology*; D004745:Enkephalins / Q000032:analysis; D005260:Female; D058851:GPI-Linked Proteins; D006651:Histocytochemistry; D006801:Humans; D007150:Immunohistochemistry; D008297:Male; D008875:Middle Aged; D009252:NADPH Dehydrogenase / Q000032:analysis; D010320:Parvalbumins / Q000032:analysis; D064030:S100 Calcium Binding Protein G / Q000032:analysis; D013373:Substance P / Q000032:analysis; D014446:Tyrosine 3-Monooxygenase / Q000032:analysis
C576498:CALB1 protein, human; C576764:CALB2 protein, human; D064092:Calbindin 1; D064032:Calbindin 2; D064026:Calbindins; D015816:Cell Adhesion Molecules, Neuronal; D004745:Enkephalins; D058851:GPI-Linked Proteins; D010320:Parvalbumins; D064030:S100 Calcium Binding Protein G; C095362:limbic system-associated membrane protein; D013373:Substance P; D014446:Tyrosine 3-Monooxygenase; D009252:NADPH Dehydrogenase; D002795:Choline O-Acetyltransferase; D000110:Acetylcholinesterase