Neuronal expression of mint1 and mint2, novel multimodular proteins, in adult murine brain.
Mints are multimodular adapter proteins in functioning membrane transport and organization. Mint1 and mint2 are neuron-specific. We localized these isoforms in mouse brain. By in situ hybridization, mRNA encoding mint1 or mint2 was expressed in neurons throughout the brain. Mint1 mRNA expression was greatest in the limbic system including cingulate cortex, hippocampus, anterior thalamic nuclei, medial habenular nucleus, and mammillary body. Mint2 mRNA was rich in cerebral cortex, entorhinal cortex, and hippocampus, but less prominent in other limbic structures. Mint1 mRNA and mint2 mRNA were distributed among hippocampal pyramidal neurons, while mint2 mRNA was especially abundant in CA3. Mint1, but not Mint2 mRNA was abundant in the substantia nigra pars compacta. Immunohistochemistry visualized mint proteins in axon terminals and neuronal somata, generally following mRNA distribution. In the hippocampus, mint1 was rich in the entorhinal projections and mossy fibers of the dentate gyrus, while mint2 was rich in commisural fibers from the contralateral hippocampus and in CA1. Mint1 intensely stained catecholamine-containing neurons such as the substantia nigra pars compacta, ventral tegmental area, and locus ceruleus. Mint2 protein was ubiquitous in these regions. Mint1 and mint2 distribution also differed elsewhere in the brainstem and in the cerebellum. Central nervous system neurons, then, predominantly express either mint1 or mint2. Mints may be involved in synaptic vesicle transport toward the active zone, also participating in transport of certain membrane proteins toward the postsynaptic density. Mint1 and mint2 may divide roles either regionally or depending on neuronal functional characteristics.
Nakajima
Y
Y
Department of Internal Medicine, Hyogo College of Medicine, 1-1 Mukogawacho, Nishinomiya 663-8501, Japan.
Okamoto
M
M
Nishimura
H
H
Obata
K
K
Kitano
H
H
Sugita
M
M
Matsuyama
T
T
D048868:Adaptor Proteins, Signal Transducing; D000818:Animals; D001692:Biological Transport; D001921:Brain / Q000166:cytology / Q000378:metabolism*; D015820:Cadherins; D002352:Carrier Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D002395:Catecholamines / Q000032:analysis; D019084:Fluorescent Antibody Technique, Indirect; D020869:Gene Expression Profiling; D006624:Hippocampus / Q000166:cytology / Q000378:metabolism; D007124:Immunoenzyme Techniques; D017403:In Situ Hybridization; D046911:Macromolecular Substances; D008297:Male; D008565:Membrane Proteins / Q000737:chemistry; D051379:Mice; D008810:Mice, Inbred C57BL; D051938:Munc18 Proteins; D009419:Nerve Tissue Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D009474:Neurons / Q000145:classification / Q000378:metabolism*; D009928:Organ Specificity; D020033:Protein Isoforms / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D017434:Protein Structure, Tertiary; D050765:Qa-SNARE Proteins; D012333:RNA, Messenger / Q000096:biosynthesis; D009435:Synaptic Transmission; D013572:Synaptic Vesicles / Q000378:metabolism; D033921:Vesicular Transport Proteins
D048868:Adaptor Proteins, Signal Transducing; C513072:Apba1 protein, mouse; C491635:Apba2 protein, mouse; D015820:Cadherins; D002352:Carrier Proteins; D002395:Catecholamines; D046911:Macromolecular Substances; D008565:Membrane Proteins; D051938:Munc18 Proteins; D009419:Nerve Tissue Proteins; D020033:Protein Isoforms; D050765:Qa-SNARE Proteins; D012333:RNA, Messenger; D033921:Vesicular Transport Proteins