Chemotaxis of macrophages by a peritoneal fluid protein in women with endometriosis. 1997

S J Weil, and S Wang, and M C Perez, and C R Lyttle
University of Pennsylvania, Division of Reproductive Biology, Philadelphia, USA.

OBJECTIVE To expand on a preliminary study comparing the chemotactic potential of peritoneal fluid (PF) from women with and without endometriosis and to characterize this activity via immunosuppressants and a protease. METHODS Case control study. METHODS University center. METHODS Fifty-nine women with endometriosis and 44 without, undergoing laparoscopy. METHODS Collection of PF, endometriotic, ovarian, and endometrial biopsies at laparoscopy. METHODS Chemotactic activity of PF was tested via an in vitro assay alone and in the presence of immunosuppressants cyclosporin A (CSA), FK506, rapamycin, and type XVII-b(S-V8) protease and in media incubated with endometriotic, ovarian, or endometrial biopsy specimens. RESULTS The PF from women with endometriosis had significantly greater chemotactic activity (cells per well, mean +/- SD) than without endometriosis (142 +/- 39 versus 48 +/- 17). Cyclosporin A significantly inhibited the chemotactic activity of the endometriotic PF; FK506 and rapamycin did not. Incubation of media with endometriotic tissue, but not ovarian or endometrial, for > or = 7 hours displayed chemotactic activity. Protease type XVII-b(S-V8) added to endometriotic PF inhibited this chemotactic activity. CONCLUSIONS Peritoneal fluid from patients with endometriosis contains a protein chemotactic factor attracting inflammatory cells into the peritoneal cavity, possibly secreted by endometriotic implants. This chemotactic factor may be a member of the immunophilin family because of its inhibition profile.

UI MeSH Term Description Entries
D007166 Immunosuppressive Agents Agents that suppress immune function by one of several mechanisms of action. Classical cytotoxic immunosuppressants act by inhibiting DNA synthesis. Others may act through activation of T-CELLS or by inhibiting the activation of HELPER CELLS. While immunosuppression has been brought about in the past primarily to prevent rejection of transplanted organs, new applications involving mediation of the effects of INTERLEUKINS and other CYTOKINES are emerging. Immunosuppressant,Immunosuppressive Agent,Immunosuppressants,Agent, Immunosuppressive,Agents, Immunosuppressive
D008264 Macrophages The relatively long-lived phagocytic cell of mammalian tissues that are derived from blood MONOCYTES. Main types are PERITONEAL MACROPHAGES; ALVEOLAR MACROPHAGES; HISTIOCYTES; KUPFFER CELLS of the liver; and OSTEOCLASTS. They may further differentiate within chronic inflammatory lesions to EPITHELIOID CELLS or may fuse to form FOREIGN BODY GIANT CELLS or LANGHANS GIANT CELLS. (from The Dictionary of Cell Biology, Lackie and Dow, 3rd ed.) Bone Marrow-Derived Macrophages,Monocyte-Derived Macrophages,Macrophage,Macrophages, Monocyte-Derived,Bone Marrow Derived Macrophages,Bone Marrow-Derived Macrophage,Macrophage, Bone Marrow-Derived,Macrophage, Monocyte-Derived,Macrophages, Bone Marrow-Derived,Macrophages, Monocyte Derived,Monocyte Derived Macrophages,Monocyte-Derived Macrophage
D009240 N-Formylmethionine Leucyl-Phenylalanine A formylated tripeptide originally isolated from bacterial filtrates that is positively chemotactic to polymorphonuclear leucocytes, and causes them to release lysosomal enzymes and become metabolically activated. F-Met-Leu-Phe,N-Formyl-Methionyl-Leucyl-Phenylalanine,Formylmet-Leu-Phe,Formylmethionyl Peptide,Formylmethionyl-Leucyl-Phenylalanine,Formylmethionylleucylphenylalanine,N-Formylated Peptide,N-formylmethionyl-leucyl-phenylalanine,fMet-Leu-Phe,F Met Leu Phe,Formylmet Leu Phe,Formylmethionyl Leucyl Phenylalanine,Leucyl-Phenylalanine, N-Formylmethionine,N Formyl Methionyl Leucyl Phenylalanine,N Formylated Peptide,N Formylmethionine Leucyl Phenylalanine,N formylmethionyl leucyl phenylalanine,Peptide, Formylmethionyl,Peptide, N-Formylated,fMet Leu Phe
D011090 Polyenes Hydrocarbons with more than one double bond. They are a reduced form of POLYYNES. Cumulenes
D011506 Proteins Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein. Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D002633 Chemotaxis The movement of cells or organisms toward or away from a substance in response to its concentration gradient. Haptotaxis
D004715 Endometriosis A condition in which functional endometrial tissue is present outside the UTERUS. It is often confined to the PELVIS involving the OVARY, the ligaments, cul-de-sac, and the uterovesical peritoneum. Endometrioma,Endometriomas,Endometrioses
D005260 Female Females
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D001202 Ascitic Fluid The serous fluid of ASCITES, the accumulation of fluids in the PERITONEAL CAVITY. Peritoneal Effusion,Peritoneal Fluid,Ascitic Fluids,Effusion, Peritoneal,Fluid, Ascitic,Fluid, Peritoneal,Peritoneal Effusions,Peritoneal Fluids

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