Last update 01 Nov 2024

LGALS3BP x Tubulin

Last update 01 Nov 2024

Basic Info

Related Targets

LGALS3BPTubulin

Drugs associated with LGALS3BP x Tubulin

1959-sss-DM3

Target

LGALS3BP x Tubulin

Mechanism

LGALS3BP inhibitors [+1]

Active Org.

Universita Degli Studi Di L'Aquila [+1]

Originator Org.

MediaPharma Srl

Active Indication

Neuroblastoma [+1]

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with LGALS3BP x Tubulin

100 Translational Medicine associated with LGALS3BP x Tubulin

0 Patents (Medical) associated with LGALS3BP x Tubulin

Literatures (Medical) associated with LGALS3BP x Tubulin

01 Aug 2007·Journal of Proteome ResearchQ2 · BIOLOGY

Identification of Differentially Secreted Biomarkers Using LC-MS/MS in Isogenic Cell Lines Representing a Progression of Breast Cancer

Q2 · BIOLOGY

Article

Author: Shevde, Lalita A. ; Mbeunkui, Flaubert ; Pannell, Lewis K. ; Metge, Brandon J.

Proteins secreted (the secretome) from cancer cells are potentially useful as biomarkers of the disease. Using LC-MS/MS, the secreted proteomes from a series of isogenic breast cancer cell lines varying in aggressiveness were analyzed by mass spectrometry: nontumorigenic MCF10A, premalignant/tumorigenic MCF10AT, tumorigenic/locally invasive MCF10 DCIS.com, and tumorigenic/metastatic MCF 10CA cl. D. Proteomes were obtained from conditioned serum-free media, partially fractionated using a small reverse phase C2 column, and digested with trypsin for analysis by LC-MS/MS, using a method previously shown to give highly enriched secreted proteomes (Mbeunkui et al. J. Proteome Res. 2006, 5, 899-906). The search files produced from five analyses (three separate preparations) were combined for database searching (Mascot) which produced a list of over 250 proteins from each cell line. The aim was to discover highly secreted proteins which changed significantly in abundance corresponding with aggressiveness. The most apparent changes were observed for alpha-1-antichymotrypsin and galectin-3-binding protein which were highly secreted proteins from MCF10 DCIS.com and MCF10CA cl. D, yet undetected in the MCF10A and MCF10AT cell lines. Other proteins showing increasing abundance in the more aggressive cell lines included alpha-1-antitrypsin, cathepsin D, and lysyl oxidase. The S100 proteins, often associated with metastasis, showed variable changes in abundance. While the cytosolic proteins were low (e.g., actin and tubulin), there was significant secretion of proteins often associated with the cytoplasm. These proteins were all predicted as products of nonclassical secretion (SecretomeP, Center for Biological Sequence Analysis). The LC-MS/MS results were verified for five selected proteins by western blot analysis, and the relevance of other significant proteins is discussed. Comparisons with two other aggressive breast cancer cell lines are included. The protein with consistent association with aggressiveness in all lines, and in unrelated cancer cells, was the galectin-3-binding protein which has been associated with breast, prostate, and colon cancer earlier, supporting the approach and findings. This analysis of an isogenic series of cell lines suggests the potential usefulness of the secretome for identifying prospective markers for the early detection and aggressiveness/progression of cancer.

01 Dec 1993·Molecular and Cellular EndocrinologyQ2 · MEDICINE

Tissue-specific expression of heat shock proteins 70 and 90: potential implication for differential sensitivity of tissues to glucocorticoids

Q2 · MEDICINE

Article

Author: Vamvakopoulos, N O

Heat shock proteins (hsps) and glucocorticoids are key elements of the organism's adaptive response to adverse physiological conditions. Glucocorticoids are pleiotropic hormones acting through receptor-mediated processes and eliciting tissue-specific biologic effects. The inactive form of the glucocorticoid receptor (GR) in the cytoplasm appears to be bound to hsps of the 90K family (hsp90 alpha and hsp90 beta). This interaction facilitates binding of glucocorticoid to its receptor, and depends on the relative amounts of the interacting components, GR and hsp90. To gain insight into the mechanisms of glucocorticoid regulation in a physiological context, the level of the hsp70/90 system in a panel of tissues, including testis, spleen, liver, thymus, pituitary, hypothalamus, hippocampus, brain cortex, pineal and adrenal, was examined by Western blotting. The hsp90 component showed greater variation (up to about forty-fold) relative to the less variable (up to about three-fold) hsp70 component of the system. The relative distribution of the hsp90 alpha and beta forms in the various tissues was also examined by a combination of Western and Northern blotting techniques. It was found that the alpha form predominated in the brain and the testis and the beta form predominated in the other peripheral organs. There was no relation between tissue hsp90 content and differential expression of either form. These findings suggest that tissue hsp90 content, an important physiological parameter of cellular homeostasis, may confer tissue specificity and sensitivity to glucocorticoids.

01 Jun 1992·SteroidsQ4 · MEDICINE

Lack of dexamethasone modulation of mRNAs involved in the glucocorticoid signal transduction pathway in two cell systems

Q4 · MEDICINE

Article

Author: Margioris, Andrew N. ; Chrousos, George P. ; Mayol, Vanessa ; Vamvakopoulos, Nikos C.

Glucocorticoids are final effectors of the stress response. These hormones exert negative feedback action at multiple levels of the hypothalamic-pituitary-adrenal axis and regulate a large number of central nervous system and peripheral target genes. The inactive form of the glucocorticoid receptor in the cytoplasm appears to be bound to heat shock proteins of the 90K family (hsp90 alpha and hsp90 beta). This interaction facilitates binding of glucocorticoid to its receptor and, therefore, its activation. The chicken ovalbumin upstream promoter transcription factor (COUP-TF) binds on a negative glucocorticoid response element in the 5' regulatory region of the proopiomelanocortin gene and prevents the repressive effect of glucocorticoids on this gene. The aim of this study was to examine the effect of glucocorticoids on the steady-state mRNAs of their own receptor, the two hsp90s, and COUP-TF. Quantitative Northern blot analysis in primary leukocytes and Epstein-Barr virus-transformed human lymphocytes (EBV-THL) basally and after a 24-hour exposure to 50 nM dexamethasone was performed. Treatment of primary leukocytes or normally growing EBV-THL with dexamethasone had no effect on the mRNA level of glucocorticoid receptor, hsp90 alpha, hsp90 beta, or COUP-TF. Similar treatment of EBV-THL grown in charcoal-stripped media, resulted in minimal changes in the mRNAs of these factors. Our findings suggest that glucocorticoids do not regulate the steady-state mRNA levels of these core components of the mammalian stress response in human primary and Epstein-Barr virus-transformed lymphocytes.

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