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*
Intramural Research Support Program, Science Applications International Corporation-Frederick,
Laboratory of Experimental Immunology, Division of Basic Sciences, National Cancer Institute, and
Veterinary and Tumor Pathology Section, Office of Laboratory Animal Resources, Division of Basic Sciences, National Cancer Institute, Frederick Cancer Research and Development Center, Frederick, MD 21702; and
Cellular Cytotoxicity Laboratory, The Austin Research Institute, Heidelberg, Victoria, Australia
We have analyzed the expression of human granzyme M (Gzm M) in
various human leukocyte subsets using the specific mAb 4H10. Using FACS
and Western blotting analysis we compared the expression of Gzm M with
that of other granzymes (Gzm A and Gzm B) and the lytic protein
perforin. Human Gzm M was constitutively highly expressed in NK cells
as was perforin and Gzm A. Surprisingly, freshly isolated NK cells had
very low (sometimes undetectable) levels of Gzm B. In contrast to Gzm B
and perforin, Gzm M was not detected in highly purified
CD4+ and CD8+ T cells either constitutively or
after short term activation in vitro. However, low levels of Gzm M were
observed in some T cell clones on prolonged passage in vitro. Gzm M was
not detected in highly purified neutrophils, monocytes, or tumor cells
of the myelomonocytic lineage. Examination of minor T cell subsets from
human peripheral blood showed detectable Gzm M in CD3+,
CD56+ T cells and 
T cells. A histological staining
procedure was developed that demonstrated a granular staining pattern
for Gzm M and a cellular distribution similar to that observed by
Western blotting. These data indicate that the expression of Gzm M does
not always correlate with the lytic activity of cytotoxic cells.
However, expression of Gzm M in NK cells, CD3+,
CD56+ T cells, and T cells suggests that this enzyme
may play some role in innate immune responses.
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