Abstract

This project explores the hypothesis that a calcium-activated neutral proteinase(s) (CANP) is associated with myelin and/or localized in axons and glial cells. This thesis has been developed from our demonstration of a calcium-mediated degradation of cytoskeletal as well as myelin proteins by a proteinase(s) present in spinal cord and brain white matter. Thus our detailed studies will be 1) to establish that CANP is associated with myelin: we plan to examine the enzyme (CANP) activity in different regions of brain, in myelin and subcellular fractions of brain during development and myelin from CNS and PNS of different species, and 2) to examine the localization of CANP by immunocytochemical technique after antisera is raised from purified CANP (which we have recently purified from bovine brain). The presence of this enzyme in myelin and related structures or cells may play a crucial role in the breakdown of myelin in demyelinating diseases (e.g. MS).

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Neurological Disorders and Stroke (NINDS)
Type
Research Project (R01)
Project #
5R01NS021353-03
Application #
3402434
Study Section
Neurological Sciences Subcommittee 1 (NLS)
Project Start
1986-02-01
Project End
1989-01-31
Budget Start
1988-02-01
Budget End
1989-01-31
Support Year
3
Fiscal Year
1988
Total Cost
Indirect Cost

  Institution

Name
Medical University of South Carolina
Department
Type
Schools of Medicine
DUNS #
183710748
City
Charleston
State
SC
Country
United States
Zip Code
29425

  Publications

Chakrabarti, A K; Dasgupta, S; Gadsden Sr, R H et al. (1996) Regulation of brain m calpain Ca2+ sensitivity by mixtures of membrane lipids: activation at intracellular Ca2+ level. J Neurosci Res 44:374-80
Chakrabarti, A K; Banik, N L; Lobo, D C et al. (1993) Calcium-activated neutral proteinase (calpain) in rat brain during development: compartmentation and role in myelination. Brain Res Dev Brain Res 71:107-13
Banik, N L; Chakrabarti, A K; Hogan, E L (1992) Effects of detergents on Ca(2+)-activated neural proteinase activity (calpain) in neural and non-neural tissue: a comparative study. Neurochem Res 17:797-802
Banik, N L; Chakrabarti, A K; Konat, G W et al. (1992) Calcium-activated neutral proteinase (calpain) activity in C6 cell line: compartmentation of mu and m calpain. J Neurosci Res 31:708-14
Banik, N L (1992) Pathogenesis of myelin breakdown in demyelinating diseases: role of proteolytic enzymes. Crit Rev Neurobiol 6:257-71
Bong, M; Chakrabarti, A; Banik, N et al. (1991) Differential regulation of myelin gene expression in SV40 T antigen-transfected rat glioma C6 cells. Metab Brain Dis 6:7-17
Banik, N L; DeVries, G H; Neuberger, T et al. (1991) Calcium-activated neutral proteinase (CANP;calpain) activity in Schwann cells: immunofluorescence localization and compartmentation of mu- and mCANP. J Neurosci Res 29:346-54
Chakrabarti, A K; Dasgupta, S; Banik, N L et al. (1990) Regulation of the calcium-activated neutral proteinase (CANP) of bovine brain by myelin lipids. Biochim Biophys Acta 1038:195-8
Banik, N L; Chakrabarti, A K; Hogan, E L (1990) Purification of an endogenous 68 kD inhibitor of calcium-activated neutral proteinase (CANP) from bovine brain: immunoblot identification and characterization. J Neurosci Res 25:119-24
Chakrabarti, A K; Dasgupta, S; Banik, N L et al. (1990) Ganglioside-modulated proteolysis by Ca2(+)-activated neutral proteinase (CANP): a role of glycoconjugates in CANP regulation. J Neurochem 54:1816-9

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