1995 Fiscal Year Final Research Report Summary
Functional analysis of the intramembrane particles specific for astrocytes.
| Project/Area Number |
06680750
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
Nerve anatomy/Neuropathology
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| Research Institution | Kinki University |
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Principal Investigator |
SASAKI Hiroshi Kinki University, School of Medicine, Professor, 医学部, 教授 (10014177)
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| Co-Investigator(Kenkyū-buntansha) |
SHINODA Koh Kinki University, School of Medicine, Lecturer, 医学部, 講師 (40192108)
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| Project Period (FY) |
1994 – 1995
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| Keywords | astrocyte / intramembrane particles / extracellular matrix / cell culture / Na, K-ATPase / P glycoprotein |
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| Research Abstract |
Orthogonal aggregates of small intramembrane particles, termed "assemblies, " are concentrated especially in the cell membranes of atrocytic processes that form the glial limitans at the outersurface of the brain and the perivascular sheath surronding the parenchymal blood vessels. As an initial step to clarify the totally unknown biochemical nature of this intramembrane structure, we have devised a culture system which enhances the differentiation of assemblies in secondary cultures of astrocytes derived from neonatal mouse neopallium. Since assemblies are most concentrated in the plasma membranes attaching to the basement membrane, we expected that extracellular matrix (ECM) molecules constituting the basement membrane could be candidates suitable for our aim. As expected, we report here that a mixture of type IV collagen, laminin, and fibronectin, major components of the extracellular matrix, has the potency to increase assembly density in cultured astrocytes. The present study highly suggest that the ECM molecules also induce the formation of assemblies in some astrocytes with no assemblies. Moreover, we report that cells expressing strongly beta2 subunit of Na, K-ATPase or P glycoprotein are devoid of assemblies. This fact shows that assemblies are neither beta2 subunit of Na, K-ATPase nor P glycoprotein.
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