title: Distribution of carboxypeptidase M on lymphoid and myeloid cells parallels the other zinc-dependent proteases CD10 and CD13.
abstract: Monoclonal antibody (MoAb) M27 was generated after immunization of mice with the human B-lineage acute lymphoblastic leukemia cell line Pre-ALP. Under reducing conditions, MoAb M27 precipitated a 60-kD surface-membrane molecule from Pre-ALP cells. Expression cloning of Pre-ALP cDNA showed that M27 recognizes carboxypeptidase M (CPM), a cell-surface, zinc-dependent protease known to cleave off basic C-terminal amino acids from peptide hormones. Using M27 antibody, CPM was detected only at discrete B lymphocyte developmental stages, namely on committed precursors and on germinal center cells. CPM was also expressed on mature T cells, mainly after activation. These results provide the first description of a carboxy-peptidase on lymphoid cells. In addition, CPM was found on granulocytes and monocytes, but not on their progenitors. Strikingly, CPM was present only on CD38+ cells, irrespective of lineage affiliation. Of interest, CPM displayed a largely overlapping distribution with the CD10 and CD13 peptidases, with which it shares common substrates (enkephalins, bradykinin). Collectively, the present data show a previously unrecognized distribution pattern of CPM on lymphoid and myeloid cells and suggest that CPM may cooperate with CD10 and CD13 to regulate biologic activity of peptide hormones on leukocytes.
authors.affiliation: Laboratory for Immunological Research, Schering-Plough, Dardilly, France.
authors.forename: B
authors.initials: B
authors.lastname: de Saint-Vis
authors.forename: L
authors.initials: L
authors.lastname: Cupillard
authors.forename: D
authors.initials: D
authors.lastname: Pandrau-Garcia
authors.forename: S
authors.initials: S
authors.lastname: Ho
authors.forename: N
authors.initials: N
authors.lastname: Renard
authors.forename: G
authors.initials: G
authors.lastname: Grouard
authors.forename: V
authors.initials: V
authors.lastname: Duvert
authors.forename: X
authors.initials: X
authors.lastname: Thomas
authors.forename: J P
authors.initials: JP
authors.lastname: Galizzi
authors.forename: J
authors.initials: J
authors.lastname: Banchereau
mesh_terms: D036541:ADP-ribosyl Cyclase; D051997:ADP-ribosyl Cyclase 1; D000328:Adult; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D015703:Antigens, CD; D000943:Antigens, Differentiation / Q000032:analysis; D001402:B-Lymphocytes / Q000166:cytology / Q000201:enzymology; D001853:Bone Marrow / Q000196:embryology / Q000201:enzymology*; D001854:Bone Marrow Cells; D018826:CD13 Antigens / Q000378:metabolism*; D002454:Cell Differentiation; D002648:Child; D058851:GPI-Linked Proteins; D006801:Humans; D016130:Immunophenotyping; D008213:Lymphocyte Activation; D008214:Lymphocytes / Q000201:enzymology*; D008562:Membrane Glycoproteins; D008666:Metalloendopeptidases / Q000378:metabolism*; D051379:Mice; D008807:Mice, Inbred BALB C; D009699:N-Glycosyl Hydrolases / Q000032:analysis; D015260:Neprilysin / Q000378:metabolism*; D013601:T-Lymphocytes / Q000201:enzymology; D015032:Zinc / Q000502:physiology
chemical_list: D000911:Antibodies, Monoclonal; D015703:Antigens, CD; D000943:Antigens, Differentiation; D058851:GPI-Linked Proteins; D008562:Membrane Glycoproteins; D009699:N-Glycosyl Hydrolases; D036541:ADP-ribosyl Cyclase; C498154:CD38 protein, human; C498155:Cd38 protein, mouse; D051997:ADP-ribosyl Cyclase 1; D018826:CD13 Antigens; C058479:carboxypeptidase M; D008666:Metalloendopeptidases; D015260:Neprilysin; D015032:Zinc