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(Received for publication, June 18, 1996, and in revised form, October 17, 1996)
From the We have isolated cDNA encoding human
telencephalin (TLN), a brain segment-specific neuronal adhesion
molecule. Human TLN comprises an NH2-terminal signal
peptide, an extracellular region with nine Ig-like domains, a single
transmembrane region, and a COOH-terminal cytoplasmic tail. The
NH2-terminal five Ig-like domains of TLN were closely
related to those of intercellular adhesion molecules (ICAMs)-1 and -3. The TLN gene was mapped to the human chromosome 19p13.2,
where the ICAM-1, -3, and -4 (LW) genes are located. Furthermore, we observed lymphocyte
function-associated antigen-1 (LFA-1)-mediated adhesion of HL-60 cells
on recombinant TLN protein, as well as on ICAM-1. However, the
interaction of TLN with LFA-1 on HL-60 cells was divalent
cation-independent and phorbol 12-myristate 13-acetate
stimulation-independent. We conclude that TLN is a unique neuronal
member of ICAM subgroup of the Ig superfamily and propose a novel type
of interaction between the Ig superfamily molecule and integrin, which
does not require the activation of integrin. TLN on the surface of
telencephalic neurons may be a target molecule in the brain for
LFA-1-expressing microglia and leukocytes in physiological or
pathological conditions.
Volume 272, Number 2,
Issue of January 10, 1997
pp. 1156-1163
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
§
,§
,
,**
Department of Neuroscience, Osaka Bioscience
Institute, 6-2-4 Furuedai, Suita, Osaka 565, the
§ Department of Biochemistry, Osaka Medical College,
Takatsuki, Osaka 569, the 
Department of Hygiene, Kyoto
Prefectural University of Medicine, Kamigyo-ku, Kyoto 602, and the
** Laboratory for Neuronal Recognition Molecules, Frontier Research
Program, RIKEN, Wako, Saitama 351-01, Japan
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