Literature DB >> 2581414

The effect of myelin basic protein on the protease inhibitors alpha 1 antitrypsin and alpha 2 macroglobulin.

R C van der Veen, C J Brinkman, O R Hommes, K J Lamers.   

Abstract

The effect of myelin basic protein (MBP) of central nervous tissue on the protease inhibitors, alpha 1 antitrypsin (a1AT) and alpha 2 macroglobulin (a2M) was studied in vitro. For this purpose, 2 characteristics of the protease inhibitors were used, viz. their pattern after isoelectric focusing and their trypsin-binding capacity. Both features of purified a2AT disappeared in the presence of MBP. The tests with a2M revealed that the formation and stability of the complex between a2M and protease were reduced. The results of this study suggest that MBP causes an increase in proteolytic activity by inactivating protease inhibitors. The potential relevance of these results for demyelinating processes in man and animal is discussed.

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Year:  1985        PMID: 2581414     DOI: 10.1111/j.1600-0404.1985.tb03189.x

Source DB:  PubMed          Journal:  Acta Neurol Scand        ISSN: 0001-6314            Impact factor:   3.209


  2 in total

1.  Interaction and complex-formation between the eosinophil cationic protein and alpha 2-macroglobulin.

Authors:  C G Peterson; P Venge
Journal:  Biochem J       Date:  1987-08-01       Impact factor: 3.857

2.  Binding of lipoprotein lipase to alpha 2-macroglobulin.

Authors:  E Vilella; G Bengtsson-Olivecrona; T Stigbrand; P E Jensen
Journal:  Biochem J       Date:  1994-06-01       Impact factor: 3.857

  2 in total

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