Injury to lungs or brain (e.g.

, brain injury such

as trauma, stroke, or bleeding in the brain, lung
injury due to a pulmonary embolism, brain
cancer, electroconvulsive therapy, pulmonary
infarction, seizures
choline acetyltransferase, a key brain enzyme.
Cytochrome oxidase (CO) is a mitochondrial energy-generating enzyme used
in brain studies as a marker of neural functional activity. The activity of CO in
different brain regions, revealed histochemically, is distributed nonhomogeneously but in
distinct patterns.

(CO)
. CO
,
.

Localized differences in CO activity could arise from localized differences in

enzyme amount or from localized regulation of enzyme turnover number
(molecular activity). Todistinguish between these alternatives, we used antibodies
against purified calf brain CO to assess the immunohistochemical distribution of
CO amount (protein immunoreactivity) in several brain regions.
a

.
, CO
CO
.
Calf brainmitochondria (synaptic and nonsynaptic populations) were isolated
from gray matter homogenates by differential centrifugation. CO was purified
from detergent extracts of the mitochondria by cytochrome c-Sepharose
4B affinity chromatography. Antisera against the purified CO were raised
in rabbits. The antibodies reacted specifically with CO, predominantly subunit IV,
in SDS immunoblots. The antibodies did not react in SDS immunoblots with any
other proteins solubilized from mitochondria or caudate nucleus but did crossreact with brain CO from other mammalian species and with bovine heart CO.
The immunohistochemical distribution of CO amount matched the histochemical
distribution of CO activity in all regions tested, including the monkey
hippocampus and the mouse olfactory bulb, somatosensory (barrel) cortex, and
cerebellum. Thus, the amount of CO in neural tissue is distributed in the same

nonhomogeneous pattern as the histochemical activity of CO. The results

suggest that mechanisms exist by which CO molecules are selectively distributed
within neurons to meet local metabolic demands posed by neural functional
activity.
Functional aspects of creatine kinase in brain.
Hemmer W, Wallimann T.
Institute for Cell Biology, Swiss Federal Institute of Technology, Zrich.

Abstract
The distinct isoenzyme-specific localization of creatine kinase (CK) isoenzymes found recently in brain
suggests an important function for CK in brain energetics and points to adaptation of the CK system to the
special energy requirements of different neuronal and glial cell types. For example, the presence of braintype B-CK in Bergmann glial cells and astrocytes is very likely related to the energy requirements for ion
homeostasis (K(+)-resorption) in the brain, as well as for metabolite and neurotransmitter trafficking between
glial cells and neurons. In contrast, the presence of muscle-type M-CK, found exclusively in Purkinje
neurons which also express other muscle-specific proteins, is very likely related to the unique calcium
metabolism of these neurons. In addition, the developmentally late appearance of mitochondrial CK (Mi-CK)
during brain development indicates an important function for Mi-CK in the oxidative energy metabolism of
the brain. The physiological importance of the phosphocreatine circuit fully operating in adult brain has been
corroborated by recent data from in vivo 31P-NMR magnetization transfer measurements. Future
investigations should concentrate on the possible involvement of CK in diseases of the CNS with altered
energy metabolism, aspects of which are also discussed here.

acetylcholinesterase

Acetylcholinesterase is an enzyme found in the basement membrane around cholinergic nerve

terminals. It is fixed by virtue of it being a membrane-bound protein. It is also found in
erythrocytes.
AChE cleaves the neurotransmitter acetylcholine into an acetic acid and choline moieties. It has
little activity for other esters.
The enzyme is a target for anticholinesterase drugs. It is also attacked irreversibly by
organophosphate pesticides; this is also the basis for the use of phosphorous compounds as
weapons of war.
Cholinesterases are enzymes which hydrolyse the neurotransmitter acetylcholine.
There are two main groups:

true cholinesterase:
o localised to cholinergic synapses
o specific for acetylcholine
o membrane-bound

pseudocholinesterase:
o hydrolyses butyrylcholine faster than acetylcholine
o non-specific
o important in the metabolism of drugs such as suxamethonium
o found soluble in the plasma