Human eosinophil granule major basic protein and its novel homolog.
Human MBP is associated with an array of in vitro cytotoxic and cytostimulatory activities, mediated in part by its strong basicity. It is most prominently found in the eosinophil, but is also present in placental X cells and placental-site giant cells during pregnancy. Pathologically, its pattern of tissue deposition and its ability to induce characteristic pathophysiologic changes, such as bronchial hyperreactivity and vasopermeability, strongly suggest a role for MBP in allergic and eosinophilic diseases. The role of MBP in protection from helminthic disease is also evident. Here, we present information on a novel homolog of eosinophil granule MBP with biologic activities similar to that of MBP. However, results from experiments on eosinophil granules suggest that the quantity of the homolog present in the eosinophil granule is significantly less than that of MBP itself. Further, preliminary experiments indicate that the two proteins are not synergistic in terms of their cytotoxic and cytostimulatory biologic activities. Future experiments must determine whether the MBP homolog is deposited at sites of tissue damage and can be detected in biologic fluids at concentrations required for biologic activity.
Plager
D A
DA
Department of Immunology, Mayo Clinic and Foundation, Rochester, MN 55905, USA.
Stuart
S
S
Gleich
G J
GJ
D000818:Animals; D001249:Asthma / Q000503:physiopathology; D001798:Blood Proteins / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology / Q000502:physiology*; D047091:Eosinophil Granule Proteins; D004804:Eosinophils / Q000378:metabolism; D005260:Female; D006373:Helminthiasis / Q000276:immunology / Q000503:physiopathology; D006801:Humans; D018836:Inflammation Mediators / Q000502:physiology*; D010920:Placenta / Q000378:metabolism; D011247:Pregnancy; D012260:Ribonucleases; D017385:Sequence Homology
D001798:Blood Proteins; D047091:Eosinophil Granule Proteins; D018836:Inflammation Mediators; D012260:Ribonucleases