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Release of Proteolytic Enzyme from Cat Brain During Stimulation
LORING F. CHAPMAN, Ph.D.;
ARMANDO RAMOS, M.D.;
ALEXANDRE CORRADO, M.D.;
VIRGILIO FORTES, M.D.;
DAVID SYMMES, Ph.D.
Arch Neurol. 1960;3(1):43-45.
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Introduction
Reversible chemical changes in rapidly frozen homogenate have been described by other investigators which indicate that stimulation of the brain, either directly or indirectly through afferent nerves, induces a state of excitation in which the rate of protein breakdown increases, proteolytic enzymes are activated, and partial protein denaturation occurs; with intense and prolonged stimulation the denaturation may be irreversible.1-3 The observation that certain proteolytic enzymes when incubated with plasma globulin form polypeptides4,5 that can be assayed readily in minute amounts, offers a method for observing small increases of proteolytic enzymes in dilute solutions such as perfusate collected before and during excitation. A vasodilator polypeptide formed by the action of a proteolytic enzyme on plasma globulin has been shown to be an important mediator of local vasomotor control in the salivary gland.6 Also, human cerebrospinal fluid collected from patients with disorders of the central nervous system forms
. . . [Full Text PDF of this Article]
Author Affiliations
New York; Ribeirao Preto, Brazil; New Haven, Conn.
From the New York Hospital and Department of Medicine (Neurology), Cornell University Medical College (Dr. Chapman); Department of Pharmacology, University of São Paulo (Drs. Ramos, Corrado and Fortes); Department of Physiology, Yale University School of Medicine (Dr. Symmes).
Footnotes
Received for publication April 8, 1960.
We are indebted to Professor Mauricio Rocha e Silva for his advice and encouragement. These studies were supported in part by C.A.P.E.S., Rio de Janeiro, Brazil, and by the Society for the Investigation of Human Ecology, New York. A preliminary report of the data was presented to the XVI International Congress of Physiological Sciences, Buenos Aires, Argentina, Aug. 15, 1959.
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