Contribution to Study the Glycoprotein Ligands of the Cerebellar Soluble Lectin in Human K562 Tumour Cells

نویسنده

  • H. Rechreche
چکیده

Many cancer cells over-express significantly the glycoproteins specific to the endogenous cerebellar soluble lectin or CSL. These ligands may present the same electrophoretic profiles regardless of the specie or tissue. We purified a large amount of the active CSL using an immuno-affinity chromatography, which was used to isolate the CSL ligands from human tumour K562 cell lines. After protease digestion of these ligands, we analyzed the obtained peptides using reverse phase chromatography and isolated an overrepresented group that carried N-glycans and was relatively hydrophobic. Thus, we suggested that the CSL ligands have a common pepetide sequence specifically recognized by the CSL, who could direct the production of these CSL-recognized N-glycans. Moreover, we speculated that the expression deregulation of a specific exon encoding this peptide sequence alters the glycosylation in K562 tumour cells.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

An endogenous lectin and one of its neuronal glycoprotein ligands are involved in contact guidance of neuron migration.

In the central nervous system, postmitotic neurons migrate along astrocytic processes to reach their adult position. The molecular mechanisms of this guided migration are not clearly defined, although some steps have been shown to involve proteases and cell adhesion molecules. We report that monovalent antibodies (Fab fragments) raised against an endogenous cerebellar soluble lectin (CSL) compl...

متن کامل

تأثیر آدنوزین ´5تری فسفات در القای آپوپتوز و مهار بیان ژن Survivin و واریانت پیرایشی ضد آپوپتوزی SUR-3B آن در سلول های K562

Introduction: Leukemia is a heterogeneous malignant disease in which progression at the level of CD34+ cells has a major impact in drug resistance and relapse. The multi-drug resistance gene product, P-glycoprotein is an inhibitor of apoptosis proteins (IAPs), such as Survivin that are expressed simultaneously with several putative drug resistance parameters in CD34+ leukemia cells. In fact, IA...

متن کامل

Review of NKG2D function and its related ligands: review article

The natural killer group 2D (NKG2D) is a transmembrane protein and a member of the CD94/NKG2 family of C-type lectin-like receptors. NKG2D is encoded by the KLRK1 gene, which is located in the NK-gene complex (NKC) placed on chromosomes 6 and 12 in mice and humans, respectively. NKG2D forms a homodimer structure and binds through ectodomains with its related ligands. Each of its monomers consis...

متن کامل

Contribution of Somatic and Dendritic SK Channels in the Firing Rate of Deep Cerebellar Nuclei: Implication in Cerebellar Ataxia

Introduction: Loss of inhibitory output from Purkinje cells leads to hyperexcitability of the Deep Cerebellar Nuclei (DCN), which results in cerebellar ataxia. Also, inhibition of small-conductancecalcium-activated potassium (SK) channel increases firing rate  f DCN, which could cause cerebellar ataxia. Therefore, SK channel activators can be effective in reducing the symptoms of this disease, ...

متن کامل

Evaluation of the Effect of Curcumin and Imatinib on BCR-ABL Expression Gene in Chronic Human k562 Cells

Background and Aims: Detection of overexpression in tumor-inhibiting genes provides valuable information for leukemia diagnosis and prognosis. Chronic myeloid leukemia (CML) is a stem cell disorder determined by a well-defined genetic anomaly involving BCR-ABL translocation in the Philadelphia chromosome. Curcumin is a chemo-preventive agent for the primary cancer targets, such as the breast, p...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2016