Abstract |
Studies in our laboratory have shown that polymorphonuclear leucocytes (PMNL) from chronic myeloid leukemia (CML) patients are defective in chemotaxis towards a synthetic peptide, n-formyl-methionyl-leucyl-phenylalanine (FMLP), during the active phases of the disease and in remission. Actin plays a major role in cellular movements and binding of chemo-attractant to cells induces polymerization of G-actin to F-actin. We have, therefore, compared polymerization of actin in FMLP stimulated PMNL from CML patients with those from normal subjects by fluorescence microscopy and flow cytometry, using F-actin specific probe, NBD- phallacidin. Our results show that binding of FMLP to normal PMNL induces rapid conversion of G-actin to F-actin followed by depolymerization to some extent. In CML PMNL, such a biphasic response is not seen. Conversion of G-actin to F-actin is slower and F-actin content is significantly lower than that in normal PMNL. Moreover, organization of F-actin is different in CML PMNL as compared to that in normal PMNL.
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Authors | N R Naik, A N Bhisey, S H Advani |
Journal | Leukemia research
(Leuk Res)
Vol. 14
Issue 10
Pg. 921-30
( 1990)
ISSN: 0145-2126 [Print] England |
PMID | 2259229
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Actins
- Amanitins
- Polymers
- N-Formylmethionine Leucyl-Phenylalanine
- 7-nitrobenz-2-oxa-1,3-diazole-phallacidin
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Topics |
- Actins
(metabolism)
- Amanitins
- Flow Cytometry
- Humans
- Leukemia, Myelogenous, Chronic, BCR-ABL Positive
(blood)
- Microscopy, Fluorescence
- N-Formylmethionine Leucyl-Phenylalanine
(metabolism, pharmacology)
- Neutrophils
(metabolism)
- Polymers
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