FUNCTIONAL ANALYSIS OF PLAKIN FAMILY PROTEINS
Project/Area Number |
15591203
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Dermatology
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Research Institution | KURUME UNIVERSITY SCHOOL OF MEDICINE |
Principal Investigator |
KARASHIMA Tadashi KURUME UNIVERSITY SCHOOL OF MEDICINE, DEPERTMENT OF DERMATOLOGY, 医学部, 講師 (70211175)
|
Co-Investigator(Kenkyū-buntansha) |
HASHIMOTO Takashi KURUME UNIVERSITY SCHOOL OF MEDICINE, DEPERTMENT OF DERMATOLOGY, PROF., 医学部, 教授 (20129597)
|
Project Period (FY) |
2003 – 2004
|
Project Status |
Completed (Fiscal Year 2004)
|
Budget Amount *help |
¥3,400,000 (Direct Cost: ¥3,400,000)
Fiscal Year 2004: ¥1,700,000 (Direct Cost: ¥1,700,000)
Fiscal Year 2003: ¥1,700,000 (Direct Cost: ¥1,700,000)
|
Keywords | KERATINOCYTE / PLAKIN FAMILY / TRANSGLUTAMINASE |
Research Abstract |
Plakin family proteins have aroleascytolinker proteins, which includes desmoplakin, plectin, Bullous pemphigoid antigen 1(BPAG1), envoplakin, periplakin andepiplakin They have an amino-terminal globular domain, acentrarod domain and a carboxy-terminalglobular domain The an amino-terminal globular domain mediating the interaction with the plasma membrane and the carboxy-terminalglobular domain associating with intermediate filaments. We find that the envoplakin stably transfected mouse keratinocytes showed remarkable keratinisation/differentiation in culture system. This led us to propose that the plakin family proteins can mediates keratinisation/differentiation of keratinocyte. The aim of our experiments was to carryout amoredetailed study about the relationship of plakin family proteins and epidermal keratinocyte Keratinisation/differentiation. Results : 1.Envoplakin/Periplakin stably transfected mouse keratinocytes showed remarkable keratinisation/differentiation in 3-D keratinocyte culture system. About the other plakins, series of the experiment is now on the way. 2.In the epidermal malignant tumors, the localization of the plakin family proteins and in situ activity of transglutaminase were remarkably disturbed, but in the benign tumors were not.
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Report
(3 results)
Research Products
(2 results)