[PDF] The «6/M (VLA-6) and a6/J4 protein complexes: tissue distribution

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The "6/M (VLA-6) and a6/J4 protein complexes: tissue distribution and biochemica l propertie s A

SONNENBERG*

C J T

LINDER

S

Department

of

Immunohaematology,

Central

Laboratory of the Netherlands Red Cross Blood Transfusion Service and Laboratory for

Experimental

and Clinical Immunology, University of Amsterdam, the Netherlands J H DAAM S

Division of Tumor Biology, the Netherlands Cancer Institute, Antoni van Leeuwenhoekhuis, Plesmanlaan 121, 1066 CX Amsterdam,

the

Netherlands

an d S . J. KENNEL

Biology

Division,

Oak Ridge

National

Laboratory,

Oak

Ridge, Tennessee 37831, USA

•Autho

r for correspondence: c/o Publication Secretariat, Central Laboratory of the Netherlands Red Cross Blood Transfusion

Service

P

O Box 9406, 1006 AK Amsterdam, the Netherlands

Summar

y A membe r o f th e integri n family th

e a6fH complexwas previously identified on human and mouse carci-noma cell lines by using a rat monoclonal antibody to

a6. Here we describe two monoclonal antibodies thatrecognize epitopes on the 04 subunit of the humanand mouse a6/J4 complexes. The monoclonal anti-bodies against 04 were able to preclear

ec604

, but nota601 from cell line extracts. A substantial fraction ofthe total 04 subunits present on the cell surface wasnot associated with a6, as it could not be removed byanti-"6 antibodies, but remained precipitable withanti-04 antibodies. There was no evidence for novel asubunits associated with 04.

Th e aQ subunit consists of disulfide-linked heavyand light chains. The variability in size of these two

Introductio

n Th e ver y lat e activatio n antige n (VLA ) subfamily of integrin s is a group of heterodimeric adhesion receptorsthat function i n cell-cell and cell-matrix interactions(Hynes, 1987; Ruoslahti and Pierschbacher, 1987; Hemler, 1988)
. Six different VLA member proteins have beenidentified (Hemler et al. 1987
, 1988; Takada et al. 1987).Some of these bind to a single ligand while others are morepromiscuous i n their ligand recognition and can bind two o r mor e adhesiv e glycoproteins VLA-6 als o know n as platele t glycoprotei n Ic-ll a (Sonnenber g et al. 1987), func-tions a s a specific laminin receptor (Sonnenberg et al.

19886)

. In addition to its expression on platelets, the a6 subuni t of VLA-6 is also present on epithelial cells of a variet

y of tissues (Sonnenberg et al. 1986). Biochemicalstudies indicated that on these cells the a6 subunit was notassociated with

th e classical VLA /31 subunit, but with a nove l alternat e /3 subunit, now named /34 (Sonnenberg et

Journa

l o f Cel l

Scienc

e 96

207-21

7 (1990

Printe

d i n Great Britain © The Company of Biologists Limited 1990 chain s fro m differen t cel l type s i s largel y du e t o difference s i n modification s o f

N-linke

d glycans Ad ditiona l heterogeneit y ma y b e cause d b y differentia l proteolyti c cleavag e o f th e a 6 precursor

.Immunoperoxidase staining of tissue sections ofneonatal and adult mice revealed that 04 expressionis limited to epithelial tissues and peripheral nerves.The a6 subunit has a wider distribution that includesall tissues and cells stained by antibodies against 04.Cells and tissue that are positive for a6, but negativefor 04, may express the a601 complex.

Ke y words integrin immunoperoxidase tissu e distribution al. 1988a
Hemle r et al. 1989). The n6/34 complex bears aquotesdbs_dbs35.pdfusesText_40

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