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J Biol Chem, Vol. 274, Issue 41, 29251-29259, October 8, 1999
From the Departments of The metalloprotease disintegrin cysteine-rich
(MDC) proteins are a recently identified family of transmembrane
proteins that function in proteolytic processing of cell surface
molecules and in cell adhesion. Since lymphocytes must interact with a
constantly changing environment, we hypothesized that lymphocytes would
express unique MDC proteins. To identify MDC proteins expressed in
human lymph node, a polymerase chain reaction-based strategy combined with degenerate oligonucleotide primers was employed. We report here
the identification of MDC-L (ADAM 23), a novel member of the MDC
protein family. The results obtained from cDNA cloning and Northern
blot analysis of mRNA isolated from various lymphoid tissues
indicate that a 2.8-kilobase mRNA encoding a transmembrane form,
MDC-Lm, and a 2.2-kilobase mRNA encoding a secreted form, MDC-Ls,
are expressed in a tissue-specific manner. MDC-L mRNA was shown to
be predominantly expressed in secondary lymphoid tissues, such as lymph
node, spleen, small intestine, stomach, colon, appendix, and trachea.
Furthermore, immunohistochemical staining with an anti-MDC-L antibody
demonstrated that cells with typical lymphocyte morphology are
responsible for expression of the MDC-L antigen in these lymphoid
tissues. MDC-Lm was found to be expressed on the surface of human
peripheral blood lymphocytes and transformed B- and T-lymphocyte cell
lines as an 87-kDa protein. Thus, we have identified a novel
lymphocyte-expressed MDC protein family member.
MDC-L, a Novel Metalloprotease Disintegrin Cysteine-rich
Protein Family Member Expressed by Human Lymphocytes
,,,
Biochemistry and Molecular
Biology and § Pathology, University of Oklahoma Health
Sciences Center, Oklahoma City, Oklahoma 73190
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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