|
||
Original Article |
Correspondence to: Carl G. Gahmberg, Department of Biosciences, Division of Biochemistry, Viikinkaari 5, University of Helsinki, Helsinki 00014, Finland. Tel:358-9-19159028 Fax:358-9-19159068 E-mail:carl.gahmberg{at}helsinki.fi.
Intercellular adhesion molecule-5 (ICAM-5) is a dendritically polarized membrane glycoprotein in telencephalic neurons, which shows heterophilic binding to leukocyte ß2-integrins. Here, we show that the human ICAM-5 protein interacts in a homophilic manner through the binding of the immunoglobulin domain 1 to domains 45. Surface coated ICAM-5-Fc promoted dendritic outgrowth and arborization of ICAM- 5expressing hippocampal neurons. During dendritogenesis in developing rat brain, ICAM-5 was in monomer form, whereas in mature neurons it migrated as a high molecular weight complex. The findings indicate that its homophilic binding activity was regulated by nonmonomer/monomer transition. Thus, ICAM-5 displays two types of adhesion activity, homophilic binding between neurons and heterophilic binding between neurons and leukocytes.
Key Words: leukocyte, integrin, adhesion, dendrite, neuron
This article has been cited by other articles:
|
|