The leukocyte common antigen, CD45 and other protein tyrosine phosphatases in hematopoietic cells

1993 ◽  
Vol 4 (6) ◽  
pp. 409-418 ◽  
Author(s):  
T. Woodford-Thomas ◽  
M.L. Thomas
Keyword(s):  
Hematopoietic Cells ◽  
Protein Tyrosine Phosphatases ◽  
Common Antigen ◽  
Tyrosine Phosphatases ◽  
Leukocyte Common Antigen ◽  
Protein Tyrosine

scholarly journals Protein tyrosine phosphatase containing SH2 domains: characterization, preferential expression in hematopoietic cells, and localization to human chromosome 12p12-p13.

1992 ◽  
Vol 12 (2) ◽  
pp. 836-846 ◽  
Author(s):  
T L Yi ◽  
J L Cleveland ◽  
J N Ihle
Keyword(s):  
Tyrosine Phosphorylation ◽  
Protein Tyrosine Phosphatase ◽  
Human Gene ◽  
Tyrosine Phosphatase ◽  
Hematopoietic Cells ◽  
Protein Tyrosine Phosphatases ◽  
Hematopoietic Cell ◽  
Protein Tyrosine Phosphorylation ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine

Protein tyrosine phosphorylation has been implicated in the growth and functional responses of hematopoietic cells. Recently, approaches have been developed to characterize the protein tyrosine phosphatases that may contribute to regulation of protein tyrosine phosphorylation. One novel protein tyrosine phosphatase was expressed predominantly in hematopoietic cells. Hematopoietic cell phosphatase encodes a 68-kDa protein that contains a single phosphatase conserved domain. Unlike other known protein tyrosine phosphatases, hematopoietic cell phosphatase contains two src homology 2 domains. We also cloned the human homolog, which has 95% amino acid sequence identity. Both the murine and human gene products have tyrosine-specific phosphatase activity, and both are expressed predominantly in hematopoietic cells. Importantly, the human gene maps to chromosome 12 region p12-p13. This region is associated with rearrangements in approximately 10% of cases of acute lymphocytic leukemia in children.

scholarly journals Identification of novel protein tyrosine phosphatases of hematopoietic cells by polymerase chain reaction amplification

Blood ◽  
1991 ◽  
Vol 78 (9) ◽  
pp. 2222-2228 ◽  
Author(s):  
T Yi ◽  
JL Cleveland ◽  
JN Ihle
Keyword(s):  
Polymerase Chain Reaction ◽  
Polymerase Chain Reaction Amplification ◽  
Hematopoietic Cells ◽  
Protein Tyrosine Phosphatases ◽  
Cdna Clones ◽  
Tyrosine Phosphatases ◽  
Chain Reaction ◽  
Protein Tyrosine ◽  
Cdna Sequences ◽  
Polymerase Chain

Polymerase chain reaction (PCR) conditions were used to amplify cDNAs that encode putative protein tyrosine phosphatases (PTPs) from a murine interleukin-3-dependent myeloid cell line. Primers for the reactions were based on conserved sequences of the catalytic domain that are shared among all known PTPs. Sequencing of 100 PCR-amplified cDNA clones identified seven different cDNA sequences. Two of these sequences were identical to the murine PTP genes Ly5/CD45/LCA and LRP/R- PTP-alpha. Two of the cDNA sequences were 95% identical to human PTP epsilon (HPTP epsilon) and rat brain PTP (PTP1B), respectively, and are likely to represent their murine homologs. Three of the cDNA sequences encoded novel potential PTPs. One of the putative PTPs was ubiquitously expressed while a second was predominantly expressed in brain, kidney, and liver and at much lower levels in a variety of other cell tkpes and tissues. The third novel putative phosphatase was expressed primarily in hematopoietic cells and tissues in a pattern that was comparable with Ly5/CD45/LCA. Further characterization of these novel PTPs will provide insights into the growth regulation of hematopoietic cells.

Protein tyrosine phosphatase containing SH2 domains: characterization, preferential expression in hematopoietic cells, and localization to human chromosome 12p12-p13

1992 ◽  
Vol 12 (2) ◽  
pp. 836-846
Author(s):  
T L Yi ◽  
J L Cleveland ◽  
J N Ihle
Keyword(s):  
Tyrosine Phosphorylation ◽  
Protein Tyrosine Phosphatase ◽  
Human Gene ◽  
Tyrosine Phosphatase ◽  
Hematopoietic Cells ◽  
Protein Tyrosine Phosphatases ◽  
Hematopoietic Cell ◽  
Protein Tyrosine Phosphorylation ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine

Protein tyrosine phosphorylation has been implicated in the growth and functional responses of hematopoietic cells. Recently, approaches have been developed to characterize the protein tyrosine phosphatases that may contribute to regulation of protein tyrosine phosphorylation. One novel protein tyrosine phosphatase was expressed predominantly in hematopoietic cells. Hematopoietic cell phosphatase encodes a 68-kDa protein that contains a single phosphatase conserved domain. Unlike other known protein tyrosine phosphatases, hematopoietic cell phosphatase contains two src homology 2 domains. We also cloned the human homolog, which has 95% amino acid sequence identity. Both the murine and human gene products have tyrosine-specific phosphatase activity, and both are expressed predominantly in hematopoietic cells. Importantly, the human gene maps to chromosome 12 region p12-p13. This region is associated with rearrangements in approximately 10% of cases of acute lymphocytic leukemia in children.

scholarly journals Identification of novel protein tyrosine phosphatases of hematopoietic cells by polymerase chain reaction amplification

Blood ◽  
1991 ◽  
Vol 78 (9) ◽  
pp. 2222-2228 ◽  
Author(s):  
T Yi ◽  
JL Cleveland ◽  
JN Ihle
Keyword(s):  
Polymerase Chain Reaction ◽  
Polymerase Chain Reaction Amplification ◽  
Hematopoietic Cells ◽  
Protein Tyrosine Phosphatases ◽  
Cdna Clones ◽  
Tyrosine Phosphatases ◽  
Chain Reaction ◽  
Protein Tyrosine ◽  
Cdna Sequences ◽  
Polymerase Chain

Abstract Polymerase chain reaction (PCR) conditions were used to amplify cDNAs that encode putative protein tyrosine phosphatases (PTPs) from a murine interleukin-3-dependent myeloid cell line. Primers for the reactions were based on conserved sequences of the catalytic domain that are shared among all known PTPs. Sequencing of 100 PCR-amplified cDNA clones identified seven different cDNA sequences. Two of these sequences were identical to the murine PTP genes Ly5/CD45/LCA and LRP/R- PTP-alpha. Two of the cDNA sequences were 95% identical to human PTP epsilon (HPTP epsilon) and rat brain PTP (PTP1B), respectively, and are likely to represent their murine homologs. Three of the cDNA sequences encoded novel potential PTPs. One of the putative PTPs was ubiquitously expressed while a second was predominantly expressed in brain, kidney, and liver and at much lower levels in a variety of other cell tkpes and tissues. The third novel putative phosphatase was expressed primarily in hematopoietic cells and tissues in a pattern that was comparable with Ly5/CD45/LCA. Further characterization of these novel PTPs will provide insights into the growth regulation of hematopoietic cells.

scholarly journals 3,6-Fluorescein Diphosphate: A Sensitive Fluorogenic and Chromogenic Substrate for Protein Tyrosine Phosphatases

1999 ◽  
Vol 4 (6) ◽  
pp. 327-334 ◽  
Author(s):  
Zheng Huang ◽  
Qingping Wang ◽  
Hoa D. Ly ◽  
Arvind Gorvindarajan ◽  
John Scheigetz ◽  
...  
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine Phosphatases ◽  
Wavelength Region ◽  
Catalytic Efficiency ◽  
Common Antigen ◽  
Peptide Substrates ◽  
Leukocyte Common Antigen ◽  
Protein Tyrosine ◽  
Highly Sensitive

A highly sensitive and continuous protein tyrosine phosphatase (PTPase) assay using 3,6-fluorescein diphosphate (FDP) is described. Leukocyte phosphatase CD45 (leukocyte common antigen), protein tyrosine phosphatase-lB, and leukocyte common antigen-related protein LAR preferentially hydrolyze FDP to fluorescein monophosphate (FMP) with Vmax and Km values comparable with those of phosphotyrosine peptide substrates. Further hydrolysis of FMP to fluorescein was less efficient because of increased Km values compared with those of FDP. FMP absorbs strongly at 445 nm and fluoresces intensely near 515 nm, both of which are insensitive to pH perturbations above pH 6. Its high catalytic efficiency, coupled with the highly sensitive dual detection in the visible wavelength region and wider pH operating range, make FDP the substrate of choice for PTPase inhibitor screening in HTS format and assay miniaturization.

scholarly journals Fullerene derivatives act as inhibitors of leukocyte common antigen based on molecular dynamics simulations

RSC Advances ◽  
2018 ◽  
Vol 8 (25) ◽  
pp. 13997-14008 ◽  
Author(s):  
Yi Yu ◽  
Huiyong Sun ◽  
Tingjun Hou ◽  
Suidong Wang ◽  
Youyong Li
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Protein Tyrosine Phosphatases ◽  
Common Antigen ◽  
Tyrosine Phosphatases ◽  
Leukocyte Common Antigen ◽  
Fullerene Derivatives ◽  
Low Toxicity ◽  
Dynamics Simulations ◽  
Potential Inhibitors

Fullerene-based molecules are being studied as potential inhibitors of protein tyrosine phosphatases due to their unique properties and low toxicity.

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