Biochemical and antigenic characterization of CD45 polypeptides expressed on plasma membrane and internal granules of human neutrophils

Pulido, Rafael; Lacal, Pedro Miguel; Mollinedo, Faustino; Sánchez-Madrid, Francisco

doi:10.1016/0014-5793(89)80654-4

Cited by 18 publications

(17 citation statements)

References 35 publications

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“…A member of the transmembrane class of tyrosine phosphatases, CD45 has been found on secretory granules and the plasma membranes of neutrophils (23). Stimulation with a variety of agents has been shown to enhance the expression of CD45 on the plasma membrane (24), a phenomenon thought to contribute to the desensitization of neutrophils following further stimulation with fMLP (25).…”

Section: Polymorphonuclear (Pmn)mentioning

confidence: 99%

Regulation of Src Homology 2-containing Tyrosine Phosphatase 1 during Activation of Human Neutrophils

Brumell

Chan²,

Butler

et al. 1997

Journal of Biological Chemistry

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The tyrosine phosphorylation of several proteins induced in neutrophils by soluble and particulate stimuli is thought to be crucial for initiating antimicrobial responses. Although activation of tyrosine kinases is thought to mediate this event, the role of tyrosine phosphatases in the initiation and modulation of neutrophil responses remains largely undefined. We investigated the role of Src homology 2-containing tyrosine phosphatase 1 (SHP-1; also known as protein tyrosine phosphatase 1C (PTP1C), hematopoetic cell phosphatase, PTP-N6, and SHPTP-1), a phosphatase expressed primarily in hemopoietic cells, in the activation of human neutrophils. SHP-1 mRNA and protein were detected in these cells, and the enzyme was found to be predominantly localized to the cytosol in unstimulated cells. Following stimulation with neutrophil agonists such as phorbol ester, chemotactic peptide, or opsonized zymosan, a fraction of the phosphatase redistributed to the cytoskeleton. Agonist treatment also induced significant decreases (30 -60%) in SHP-1 activity, which correlated temporally with increases in the cellular phosphotyrosine content. Phosphorylation of SHP-1 on serine residues was associated with the inhibition of its enzymatic activity, suggesting a causal relationship. Accordingly, both the agonist-evoked phosphorylation of SHP-1 and the inhibition of its catalytic activity were blocked by treatment with bisindolylmaleimide I, a potent and specific inhibitor of protein kinase C (PKC) activity. Immunoprecipitated SHP-1 was found to be phosphorylated efficiently by purified PKC in vitro. Such phosphorylation also caused a decrease in the phosphatase activity of SHP-1. Together, these data suggest that inhibition of SHP-1 by PKC-mediated serine phosphorylation plays a role in facilitating the accumulation of tyrosine-phosphorylated proteins following neutrophil stimulation.These findings provide a new link between the PKC and tyrosine phosphorylation branches of the signaling cascade that triggers antimicrobial responses in human neutrophils.

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Section: Polymorphonuclear (Pmn)mentioning

confidence: 99%

Regulation of Src Homology 2-containing Tyrosine Phosphatase 1 during Activation of Human Neutrophils

Brumell

Chan²,

Butler

et al. 1997

Journal of Biological Chemistry

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“…This recovery could be due either to the release of immature neutrophils from bone marrow or to recirculation of neutrophiis expressing lower CD45 ieveis from lung capillaries [25]. We have previously demonstrated that CD45 molecules arc stored in resting neutrophils on membranes from the readily translocatabie tertiary secretory granuies, as weli as in that from specific granules [9], and it is known that intraceilular compartmcntaiization of these organelles is regulated during neutrophil activation [26].…”

Section: Discussionmentioning

confidence: 99%

“…Spain. branes [9]. However, the biochemical relation between these 180-and I30-l50-kD polypeptides was not established in such studies.…”

Section: Introductionmentioning

confidence: 98%

Biochemical and functional characterization of the leucocyte tyrosine phosphatase CD4S (CD4SRO, 180 kD) from human neutrophils. In vivo upregulation of CD45RO plasma membrane expression on patients undergoing haemodialysis

Pulido

Álvarez

Mollinedo

et al. 1992

Clinical and Experimental Immunology

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SUMMARYThe biochemical and functional characterization, and the regulation of plasma membrane expression of the leucocyte tyrosine phosphatase CD45. have been investigated in neutrophils from healthy donors and patients undergoing haemodialysis. CD45 proteins of 180 kD and 130-150 kD were precipitated from neutrophils from both healthy subjects and haemodialysed patients. Prolonged storing, as well as trypsin treatment of satnples containing the 180-kD CD45 protein, generated the 130-150-kD polypeptides. The 130-150-kD CD45 polypeptides carried extracellular CD45 epitopes. including the sialic acid-related UCHLI epitope (CD45RO). Furthermore, these trypsin-generated CD45 polypeptides did not possess phosphatase activity, which could be detected on the 180-kD protein. A remarkable quantitative increase o^ cell surface expression of the neutrophil CD45 components was detected both afler in vitro neutrophil activation and after dialysis treatment with neutropenic membranes. The CD45 biochemical pattern did not qualitatively ehange upon either in vitro or in vivo dialysis-induced neutrophil activation. The upreguiated expression of CD45 on neutrophils from dialysed patients correlated with the neutropenic effect induced by the different dialyser membranes. Maximal upregulation ofC045 expression was observed alter ISminofdialysis with neutropenic membranes, and norrnal expression levels were restored after 1 h. By contrast, increase of CD45 plasma mernbrane expression induced in vitro by treatment of normal neutrophils with thedegranulatory agents fMLPor Ca-^ ionophore was maintained. These results demonstrate that neutrophil cell surface expression ofthe 180-kD CD45 protein is upregulated during the in vivo haemodialysis process, and suggest that a proteotytic activity could regulate the enzymatic activity of CD45 by degranulation of its cytoplasmic phosphatase domains.

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“…With respect to phosphatases, a membrane-associated phosphotyrosine phosphatase activity has been observed in human neutrophils [5]. CD45, a phosphotyrosine phosphatase, is mobilized from specific and/or tertiary granules to the plasma-membrane fraction when neutrophils are stimulated by fMet-Leu-Phe or CB [35]. In vitro, the specific activities of phosphotyrosine phosphatases are much higher than those of tyrosine kinases [36].…”

Section: Discussionmentioning

confidence: 99%

“…5 and Table 1). This may be due to that CB pretreatment inducing mobilization of CD45 from granules to the membrane fraction [35] and thus increasing the phosphatase activity in the membrane. This hypothesis should be tested.…”

Section: Discussionmentioning

confidence: 99%

Protein tyrosine phosphorylation in rabbit peritoneal neutrophils

Huang

Bonak

Laramee

et al. 1990

Biochemical Journal

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Protein tyrosine phosphorylation in rabbit peritoneal neutrophils was examined by immunoblotting with antibodies specific for phosphotyrosine. Stimulation of the neutrophils with chemotactic factor fMet-Leu-Phe (10 nM) caused rapid increases of tyrosine phosphorylation of several proteins with apparent molecular masses of (Group A) 54-58 kDa and 100-125 kDa and (Group B) 36-41 kDa. Stimulation of Group A proteins was observed by fMet-Leu-Phe (10 nM, maximum at 20 s) and A23187 (1 microM, 1 min). Stimulation of Group B proteins was observed by fMet-Leu-Phe (ED50 0.15 nM, 1 min), leukotriene B4 (ED50 0.15 nM, 1 min), phorbol 12-myristate 13-acetate (PMA) (ED50 25 ng/ml, 10 min) and partially by ionophore A23187 (1 microM, 1 min). Pretreatment of the cell with the protein kinase inhibitor H-7 (25 microM, 5 min) and PMA (0.1 microgram/ml, 3 min) partially inhibited the fMet-Leu-Phe effect. However, pretreatment of the cells with quin 2/AM (20 microM, 10 min) completely inhibited the fMet-Leu-Phe effect. The results indicate that rapid regulation of tyrosine phosphorylation is an early event occurring in stimulated neutrophils. Furthermore the effect of fMet-Leu-Phe on tyrosine phosphorylation may require Ca2+ mobilization and may partially require the activity of H-7-sensitive protein kinases.

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Biochemical and antigenic characterization of CD45 polypeptides expressed on plasma membrane and internal granules of human neutrophils

Cited by 18 publications

References 35 publications

Regulation of Src Homology 2-containing Tyrosine Phosphatase 1 during Activation of Human Neutrophils

Regulation of Src Homology 2-containing Tyrosine Phosphatase 1 during Activation of Human Neutrophils

Biochemical and functional characterization of the leucocyte tyrosine phosphatase CD4S (CD4SRO, 180 kD) from human neutrophils. In vivo upregulation of CD45RO plasma membrane expression on patients undergoing haemodialysis

Protein tyrosine phosphorylation in rabbit peritoneal neutrophils

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