Abstract
Effects of ischemia on the content of a ulinastatin (UT)-like substance in the murine cerebral cortex and hippocampus were studied. At 24 h post-ischemia, a significant (p < 0.05) decrease in the content of UT-like substance in the hippocampus but not the cerebral cortex and a concurrent increase in the activity of μ-calpain were observed. In in vitro experiments, a decrease was registered in the content of UT-like substance in the hippocampus in the presence of calcium. This decrease was inhibited by both EDTA and calpastatin treatments. These results implicate the destruction of UT-like substance by μ-calpain in the ischemic hippocampus.
Similar content being viewed by others
REFERENCES
Åkerström, B., and Lögdberg, L. 1990. An intriguing member of the lipocalin protein family: α1-microglobulin. Trends Biochem. Sci. 15:240-243.
Kitaguti, N., Takahashi, Y., Tokushima, Y., Shiojiri, S., and Ito, H. 1988. Novel precursor of Alzheimer's disease amyloid protein shows protease inhibitory activity. Nature (London) 331:530-532.
Ponte, P., Gonzalez-Dewhitt, P., Schilling, J., Miller, J., Hsu, D., Greenberg, B., Davis, K., Wallace, W., Lieberburg, I., Fuller, F., and Cordell, B. 1988. A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors. Nature (London) 331:525-527.
Tanzi, R. E., McClatchey, A. I., Lamperti, E. D., Villa-Komaroff, L., Gusella, J. F., and Neve, R. L. 1988. Protease inhibitor domain encoded by an amyloid protein precursor mRNA associated with Alzheimer's disease. Nature (London) 331:528-530.
Shikimi, T., Wessel, T., Joh, T. H., Takahashi, M., Kaneto, H., Hattori, K., and Takaori, S. 1993. Demonstration of a human urinary trypsin inhibitor (urinastatin)-like substance in the murine brain. Brain Res. 616:230-235.
Shikimi, T., Hattori, K., and Takaori, S. 1992. Existence of a human urinary trypsin inhibitor (urinastatin)-like substance in the rat brain. Jpn. J. Pharmacol. 60:97-103.
Kojima, M., and Kaneto, H. 1989. Preparation of cerebral ischemia-induced amnesic model in mice and ameliorative effects of several compounds on the model. Folia pharmacol. japon. 94:223-228.
Ishiura, S., Murofushi, H., Suzuki, K., and Imahori, K. 1978. Studies of a calcium-activated protease from chickin skeletal muscle. J. Biochem. 84:225-230.
Shikimi, T., Suzuki, S., Takahashi, M., and Kaneto, H. 1990. Sandwich enzyme-immunoassay of human urinary trypsin inhibitor (urinastatin) and urinastatin-like immunoreactive substance in mouse urine. Scand. J. Clin. Lab. Invest. 50:1-8.
Lowry, O. H., Rosebrough, N. J., Fall, A. L., and Randall, R. J. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:265-275.
Sugimachi, N., Nakamura, T., Takahashi, M., and Kaneto, H. 1993. Lack of the development of morphine tolerance in experimental amnesia: role of arginine vasopressin. Brain Res. 609:93-97.
Pulsinelli, W. A. 1985. Selective neuronal vulnerability: morphological and molecular characteristics. Progr. Brain Res. 63:29-37.
Monard, D. 1988. Cell-derived proteases and protease inhibitors as regulators of neurite outgrouth. Trends Neurosci. 11:541-544.
Defeudis, F. V. 1989. Neurotrophic, neurotoxic and mitogenic activities of “amyloid” proteins. Trends Pharmacol. Sci. 10:479-480.
Gopalakrishna, R., and Barsky, S. H. 1985. Quantitation of tissue calpain activity after isolation by hydrophobic chromatography. Anal. Biochem. 148:413-423.
Murachi, T., Hatanaka, M., Yasumoto, Y., Nakayama, N., and Tanaka, K. 1981. A quantitative distribution study on calpain and calpastatin in rat tissues and cells. Biochem. Int. 2:651-656.
Li, J., Grynspan, F., Berman, S., Nixon R., and Bursztajn, S. 1996. Regional differences in gene expression for calcium activated neutral proteases (calpains) and their endogenous inhibitor calpastatin in mouse brain and spinal cord. J. Neurobiol. 30:177-191 (1996).
Simonson, L., Baudry M., Siman R., and Lynch G. 1985. Regional distribution of soluble calcium activated proteinase activity in neonatal and adult rat brain. Brain Res. 327:153-159.
Sims, N. R. 1995. Calcium, energy metabolism and the development of selective neuronal loss following short-term cerebral ischemia. Metab. Brain Dis. 10:191-217.
Saido, T. C., Sorimachi, H., and Suzuki, K. 1994. Calpain: new perspectives in molecular diversity and physiological-pathological involvement. FASEB J. 8:814-822.
Silver, I. A., and Erecinska, M. 1990. Intracellular and extracellular changes of [Ca2+] in hypoxia and ischemia in rat brain in vivo. J. Gen. Physiol. 95:837-866.
Saido, T. C., Shibata, M., Takenawa, T., Murofushi, H., and Suzuki, K. 1992. Positive regulation of µ-calpain action by polyphosphoinositides. J. Biol. Chem. 267:24585-24590.
Lu, Y. M., Lu, B. F., Yan, Y. L., Yan, T. H., Ho, X. P., and Wang, W. J. 1993. Alteration of G-protein coupling function in phosphoinositide signalling pathways of rat hippocampus by ischaemic brain injury. Eur. J. Neurosci. 5:1334-1338.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Shikimi, T., Gonda, T., Takahashi, M. et al. Ischemia Induces a Reduction in the Content of Ulinastatin-Like Substance in the Murine Hippocampus. Neurochem Res 23, 69–72 (1998). https://doi.org/10.1023/A:1022453504527
Issue Date:
DOI: https://doi.org/10.1023/A:1022453504527