Dissociation of neurite-promoting activity and protease-inhibiting function of alpha 2-macroglobulin in culture
| Autor: | Noboru Iijima, Toshio Mori, Shinichi Kohsaka, Katsuaki Kitabatake, Yutaka Miyamoto |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Neurite
medicine.medical_treatment Alpha (ethology) Receptors Cell Surface Biology chemistry.chemical_compound Amyloid beta-Protein Precursor medicine Neurites Animals Aprotinin Protease Inhibitors alpha-Macroglobulins Molecular Biology Cells Cultured Cerebral Cortex Protease Kunitz STI protease inhibitor General Neuroscience Leupeptin Rats Inbred Strains Stimulation Chemical Cell biology Macroglobulin Rats Protease Nexins Plasminogen Inactivators chemistry Immunology Antipain Electrophoresis Polyacrylamide Gel Neurology (clinical) Carrier Proteins Developmental Biology medicine.drug |
| Zdroj: | Brain research. 567(2) |
| ISSN: | 0006-8993 |
| Popis: | The relationship between the neurite-promoting effect and the protease-inhibiting function of alpha 2-macroglobulin (alpha 2M) was examined in a culture of dissociated neurons from embryonic rat neocortical tissue. The neurite-promoting effect of various protease inhibitors (soybean trypsin inhibitor, alpha 1-antitrypsin, aprotinin, phenylmethanesulfonyl fluoride, leupeptin, antipain, human alpha 2M and purified rat alpha 2M) was investigated. At lower concentrations, only alpha 2M significantly promoted neurite outgrowth. Furthermore, alpha 2M-trypsin complexes, which had lost their protease-inhibiting function and exposed their receptor-recognition site, promoted neurite outgrowth more efficiently than native alpha 2M. These results indicate the possibility that the neurite-promoting effect of alpha 2M is mediated by its receptor-binding activity but is not directly related to its protease-inhibiting function. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|