No Association Between Transmembrane Protein-Tyrosine Phosphatase Receptor Type C (CD45) Exon A Point Mutation (77C>G) and Idiopathic Dilated Cardiomyopathy

The leucocyte common antigen, protein tyrosine phosphatase receptor type C (PTPRC), also known as CD45, is a transmembrane glycoprotein, expressed on almost all haematopoietic cells except for mature erythrocytes, and is an essential regulator of T and B cell antigen receptor-mediated activation. Disruption of the equilibrium between protein tyrosine kinase and phosphatase activity (from CD45 and others) can result in immunodeficiency, autoimmunity, or malignancy. CD45 is normally present on the cell surface, therefore it works upstream of a large signalling network which differs between cell types, and thus the effects of CD45 on these cells are also different. However, it is becoming clear that CD45 plays an essential role in the innate immune system and this is likely to be a key area for future research. In this review of PTPRC (CD45), its structure and biological activities as well as abnormal expression of CD45 in leukaemia and lymphoma will be discussed.

Download Full-text

A transmembrane protein-tyrosine phosphatase receptor type C (CD45) exon A point mutation (77 C to G) is not associated with the development of type 1 diabetes mellitus in a German population

European Journal of Immunogenetics ◽

10.1111/j.1365-2370.2004.00479.x ◽

2004 ◽

Vol 31 (6) ◽

pp. 245-247 ◽

Cited By ~ 10

Author(s):

H. Thude ◽

S. Rosenhahn ◽

W. Hunger-Dathe ◽

U.-A. Muller ◽

D. Barz

Keyword(s):

Diabetes Mellitus ◽

Type 1 Diabetes ◽

Type 1 Diabetes Mellitus ◽

Point Mutation ◽

Protein Tyrosine Phosphatase ◽

Transmembrane Protein ◽

Tyrosine Phosphatase ◽

German Population ◽

Type C

Download Full-text

Protein Tyrosine Phosphatase Receptor Type C

Encyclopedia of Signaling Molecules ◽

10.1007/978-1-4419-0461-4_101106 ◽

2012 ◽

pp. 1488-1488

Author(s):

Dominique M. Donato ◽

Steven K. Hanks ◽

Kenneth A. Jacobson ◽

M. P. Suresh Jayasekara ◽

Zhan-Guo Gao ◽

...

Keyword(s):

Protein Tyrosine Phosphatase ◽

Tyrosine Phosphatase ◽

Receptor Type ◽

Protein Tyrosine ◽

Type C

Download Full-text

Protein Tyrosine Phosphatase Receptor Type C

Encyclopedia of Signaling Molecules ◽

10.1007/978-3-319-67199-4_103115 ◽

2018 ◽

pp. 4244-4244

Keyword(s):

Protein Tyrosine Phosphatase ◽

Tyrosine Phosphatase ◽

Receptor Type ◽

Protein Tyrosine ◽

Type C

Download Full-text

An investigation of the C77G and C772T variations within the human protein tyrosine phosphatase receptor type C gene for association with multiple sclerosis in an Australian population

Brain Research ◽

10.1016/j.brainres.2008.12.017 ◽

2009 ◽

Vol 1255 ◽

pp. 148-152 ◽

Cited By ~ 8

Author(s):

Attila L. Szvetko ◽

Ashleigh Jones ◽

Jason Mackenzie ◽

Lotti Tajouri ◽

Peter A. Csurhes ◽

...

Keyword(s):

Multiple Sclerosis ◽

Protein Tyrosine Phosphatase ◽

Tyrosine Phosphatase ◽

Human Protein ◽

Receptor Type ◽

Australian Population ◽

Protein Tyrosine ◽

Type C

Download Full-text

Receptor Type Protein Tyrosine Phosphatase ζ-Pleiotrophin Signaling Controls Endocytic Trafficking of DNER That Regulates Neuritogenesis

Molecular and Cellular Biology ◽

10.1128/mcb.00074-08 ◽

2008 ◽

Vol 28 (14) ◽

pp. 4494-4506 ◽

Cited By ~ 27

Author(s):

Nobuna Fukazawa ◽

Seisuke Yokoyama ◽

Mototsugu Eiraku ◽

Mineko Kengaku ◽

Nobuaki Maeda

Keyword(s):

Plasma Membrane ◽

Tyrosine Phosphorylation ◽

Purkinje Cells ◽

Protein Tyrosine Phosphatase ◽

Transmembrane Protein ◽

Tyrosine Phosphatase ◽

Receptor Type ◽

Protein Tyrosine ◽

Tyrosine Residues ◽

Type Protein

ABSTRACT Protein tyrosine phosphatase ζ (PTPζ) is a receptor type protein tyrosine phosphatase that uses pleiotrophin as a ligand. Pleiotrophin inactivates the phosphatase activity of PTPζ, resulting in the increase of tyrosine phosphorylation levels of its substrates. We studied the functional interaction between PTPζ and DNER, a Notch-related transmembrane protein highly expressed in cerebellar Purkinje cells. PTPζ and DNER displayed patchy colocalization in the dendrites of Purkinje cells, and immunoprecipitation experiments indicated that these proteins formed complexes. Several tyrosine residues in and adjacent to the tyrosine-based and the second C-terminal sorting motifs of DNER were phosphorylated and were dephosphorylated by PTPζ, and phosphorylation of these tyrosine residues resulted in the accumulation of DNER on the plasma membrane. DNER mutants lacking sorting motifs accumulated on the plasma membrane of Purkinje cells and Neuro-2A cells and induced their process extension. While normal DNER was actively endocytosed and inhibited the retinoic-acid-induced neurite outgrowth of Neuro-2A cells, pleiotrophin stimulation increased the tyrosine phosphorylation level of DNER and suppressed the endocytosis of this protein, which led to the reversal of this inhibition, thus allowing neurite extension. These observations suggest that pleiotrophin-PTPζ signaling controls subcellular localization of DNER and thereby regulates neuritogenesis.

Download Full-text