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1.
Rev Invest Clin ; 76(1): 45-59, 2024.
Artículo en Inglés | MEDLINE | ID: mdl-38442372

RESUMEN

Background: Triple-negative breast cancer (TNBC) is a subtype of breast cancer (BC) that lacks receptors for targeted therapy. Deeper insight into the molecular mechanisms regulating TNBC metastasis is urgently needed. The epithelial-mesenchymal transition process facilitates the metastasis of neighboring epithelial tumor cells. Protein kinase, membrane-associated tyrosine/threonine 1 (PKMYT1), a member of the Wee family of protein kinases, is upregulated in BC, and its high expression predicts poor prognosis in BC patients. Notch signaling activation is a pathognomonic feature of TNBC. PKMYT1 has been found to induce EMT in non-small cell lung cancer by activating Notch signaling. However, whether PKMYT1 exerts effects on TNBC progression by regulating Notch signaling remains unknown. Objectives: The objective of this study was to investigate whether PKMYT1 exerts effects on TNBC progression by regulating Notch signaling. Methods: Fifty cases of surgically resected BC samples (tumor and adjacent non-tumor tissue samples) were collected from patients diagnosed with BC. We measured the expression of PKMYT1 in clinical samples with real-time quantitative polymerase chain reaction (RT-qPCR). For in vitro analysis, RT-qPCR and Western blotting were conducted to evaluate PKMYT1 expression in TNBC cells. Then, the viability, migration, and invasion of TNBC cells were detected by cell counting kit-8 assays, wound healing assays, and Transwell assays. The EMT event was examined by evaluating the levels of EMT-associated proteins. For in vivo analysis, xenograft models in nude mice were established to explore PKMYT1 roles. E-cadherin and Ki67 expression in xenograft models were estimated by immunohistochemistry staining. Hematoxylin and eosin staining was performed to assess tumor metastasis. The underlying mechanisms by which PKMYT1 affected the malignant phenotypes of TNBC cells were explored by Western blotting measuring the pathway-associated proteins. Results: PKMYT1 was upregulated in BC tissues and cells, and its knockdown prevented cell proliferation, migration, invasion, and EMT event in TNBC. Mechanistically, Notch signaling was inactivated by PKMYT1 depletion, and Notch activation abolished the PKMYT1 silencing-induced inhibition in the malignant phenotypes of TNBC cells. For in vivo analysis, PKMYT1 knockdown inhibited tumorigenesis and metastasis of TNBC. Conclusion: PKMYT1 promotes EMT, proliferation, migration, and invasion of TNBC cells and facilitates tumor growth and metastasis by activating Notch signaling.


Asunto(s)
Transición Epitelial-Mesenquimal , Proteínas Serina-Treonina Quinasas , Proteínas Tirosina Quinasas , Neoplasias de la Mama Triple Negativas , Animales , Humanos , Ratones , Proteínas de la Membrana/metabolismo , Ratones Desnudos , Proteínas Serina-Treonina Quinasas/metabolismo , Proteínas Tirosina Quinasas/metabolismo , Neoplasias de la Mama Triple Negativas/metabolismo , Neoplasias de la Mama Triple Negativas/patología
2.
Rev Invest Clin ; 76(1): 6-17, 2024 03 01.
Artículo en Inglés | MEDLINE | ID: mdl-38253021

RESUMEN

Background: Adriamycin resistance remains an obstacle to gastric cancer chemotherapy treatment. Objective: The objective of this study was to study the role and mechanism of transcription factor E2F7 in sensitivity to ADM chemotherapeutic agents in gastric cancer. Methods: Cell viability and cell sensitivity were assessed by CCK-8 and IC50 values of ADM were calculated. The impact of ADM on cellular proliferative capacity was assessed through colony formation assay. The binding relationship between E2F7 and PKMYT1 was then verified by dual luciferase assay and chromatin immunoprecipitation assay. ERK1/ERK2 and p-ERK1/p-ERK2 protein expression levels were detected by western blot. Results: In both gastric cancer tissue and ADM-resistant cells, a conspicuous upregulation of E2F7 and PKMYT1 was observed. Upregulated PKMYT1 was notably enriched in the MAPK signaling pathway. Enhanced levels of E2F7 were shown to not only drive gastric cancer cell proliferation but also engender a reduction in the sensitivity of these cells to ADM. Furthermore, PKMYT1 emerged as a downstream target of E2F7. Activation of E2F7 culminated in the transcriptional upregulation of PKMYT1, and silencing E2F7 reversed the inhibitory impact of PKMYT1 overexpression on ADM sensitivity in gastric cancer cells. Conclusion: E2F7/PKMYT1 axis might promote the proliferation and partially inhibit ADM sensitivity of gastric cancer cells by activating the MAPK pathway.


Asunto(s)
MicroARNs , Neoplasias Gástricas , Humanos , Doxorrubicina/farmacología , Neoplasias Gástricas/tratamiento farmacológico , Neoplasias Gástricas/genética , Factores de Transcripción/metabolismo , Línea Celular Tumoral , Transducción de Señal , MicroARNs/metabolismo , Regulación Neoplásica de la Expresión Génica , Factor de Transcripción E2F7/genética , Factor de Transcripción E2F7/metabolismo , Proteínas de la Membrana/genética , Proteínas Tirosina Quinasas/metabolismo , Proteínas Serina-Treonina Quinasas/metabolismo
3.
J Phys Chem B ; 126(50): 10587-10596, 2022 12 22.
Artículo en Inglés | MEDLINE | ID: mdl-36512419

RESUMEN

Conformational changes are an essential feature for the function of some dynamic proteins. Understanding the mechanism of such motions may allow us to identify important properties, which may be directly related to the regulatory function of a protein. Also, this knowledge may be employed for a rational design of drugs that can shift the balance between active and inactive conformations, as well as affect the kinetics of the activation process. Here, the conformational changes in carboxyl-terminal Src kinase, the major catalytic repressor to the Src family of kinases, was investigated, and it was proposed as a functionally related hypothesis. A Cα Structure-Based Model (Cα-SBM) was applied to provide a description of the overall conformational landscape and further analysis complemented by detailed molecular dynamics simulations. As a first approach to Cα-SBM simulations, reversible transitions between active (closed) and inactive (open) forms were modeled as fluctuations between these two energetic basins. It was found that, in addition to the interdomain Carboxyl-terminal SRC Kinase (Csk) correlated motions, a conformational change in the αC helix is required for a complete conformational transition. The result reveals this as an important region of transition control and domain coordination. Restrictions in the αC helix region of the Csk protein were performed, and the analyses showed a direct correlation with the global conformational changes, with this location being propitious for future studies of ligands. Also, the Src Homology 3 (SH3) and SH3 plus Src Homology 2 (SH2) domains were excluded for a direct comparison with experimental results previously published. Simulations where the SH3 was deleted presented a reduction of the transitions during the simulations, while the SH3-SH2 deletion vanishes the Csk transitions, corroborating the experimental results mentioned and linking the conformational changes with the catalytic functionality of Csk. The study was complemented by the introduction of a known kinase inhibitor close to the Csk αC helix region where its consequences for the kinetic behavior and domain displacement of Csk were verified through detailed molecular dynamics. The findings describe the mechanisms involving the Csk αC helix for the transitions and also support the dynamic correlation between SH3 and SH2 domains against the Csk lobes and how local energetic restrictions or interactions in the Csk αC helix can play an important role for long-range motions. The results also allow speculation if the Csk activity is restricted to one specific conformation or a consequence of a state transition, this point being a target for future studies. However, the αC helix is revealed as a potential region for rational drug design.


Asunto(s)
Proteínas Tirosina Quinasas , Familia-src Quinasas , Proteínas Tirosina Quinasas/metabolismo , Proteína Tirosina Quinasa CSK/metabolismo , Familia-src Quinasas/química , Dominios Homologos src , Fosfotransferasas/metabolismo
4.
Cells ; 11(12)2022 06 18.
Artículo en Inglés | MEDLINE | ID: mdl-35741094

RESUMEN

The nuclear progesterone receptor (PR) is mainly known for its role as a ligand-regulated transcription factor. However, in the last ten years, this receptor's extranuclear or rapid actions have gained importance in the context of physiological and pathophysiological conditions such as cancer. The PR's polyproline (PXPP) motif allows protein-protein interaction through SH3 domains of several cytoplasmatic proteins, including the Src family kinases (SFKs). Among members of this family, cSrc is the most well-characterized protein in the scenario of rapid actions of the PR in cancer. Studies in breast cancer have provided the most detailed information on the signaling and effects triggered by the cSrc-PR interaction. Nevertheless, the study of this phenomenon and its consequences has been underestimated in other types of malignancies, especially those not associated with the reproductive system, such as glioblastomas (GBs). This review will provide a detailed analysis of the impact of the PR-cSrc interplay in the progression of some non-reproductive cancers, particularly, in GBs.


Asunto(s)
Neoplasias de la Mama , Receptores de Progesterona , Neoplasias de la Mama/metabolismo , Femenino , Humanos , Progesterona , Proteínas Tirosina Quinasas/metabolismo , Receptores de Progesterona/metabolismo , Familia-src Quinasas/metabolismo
5.
Bioorg Med Chem Lett ; 68: 128764, 2022 07 15.
Artículo en Inglés | MEDLINE | ID: mdl-35504513

RESUMEN

The discovery of potent and selective inhibitors for understudied kinases can provide relevant pharmacological tools to illuminate their biological functions. DYRK1A and DYRK1B are protein kinases linked to chronic human diseases. Current DYRK1A/DYRK1B inhibitors also antagonize the function of related protein kinases, such as CDC2-like kinases (CLK1, CLK2, CLK4) and DYRK2. Here, we reveal narrow spectrum dual inhibitors of DYRK1A and DYRK1B based on a benzothiophene scaffold. Compound optimization exploited structural differences in the ATP-binding sites of the DYRK1 kinases and resulted in the discovery of 3n, a potent and cell-permeable DYRK1A/DYRK1B inhibitor. This compound has a different scaffold and a narrower off-target profile compared to current DYRK1A/DYRK1B inhibitors. We expect the benzothiophene derivatives described here to aid establishing DYRK1A/DYRK1B cellular functions and their role in human pathologies.


Asunto(s)
Proteínas Serina-Treonina Quinasas , Proteínas Tirosina Quinasas , Humanos , Inhibidores de Proteínas Quinasas/química , Inhibidores de Proteínas Quinasas/farmacología , Proteínas Quinasas , Proteínas Tirosina Quinasas/metabolismo , Tiofenos
6.
J Cell Biochem ; 123(7): 1197-1206, 2022 07.
Artículo en Inglés | MEDLINE | ID: mdl-35538691

RESUMEN

A reduction in extracellular pH (pHe) is a characteristic of most malignant tumors. The aryl hydrocarbon receptor (AhR) is a transcription factor localized in a cytosolic complex with c-Src, which allows it to trigger nongenomic effects through c-Src. Considering that the slightly acidic tumor microenvironment promotes breast cancer progression in a similar way to the AhR/c-Src axis, our aim was to evaluate whether this pathway could be activated by low pHe. We examined the effect of pHe 6.5 on AhR/c-Src axis using two breast cancer cell lines (MDA-MB-231 and LM3) and mammary epithelial cells (NMuMG) and found that acidosis increased c-Src phosphorylation only in tumor cells. Moreover, the presence of AhR inhibitors prevented c-Src activation. Low pHe reduced intracellular pH (pHi), while amiloride treatment, which is known to reduce pHi, induced c-Src phosphorylation through AhR. Analyses were conducted on cell migration and metalloproteases (MMP)-2 and -9 activities, with results showing an acidosis-induced increase in MDA-MB-231 and LM3 cell migration and MMP-9 activity, but no changes in NMuMG cells. Moreover, all these effects were blocked by AhR and c-Src inhibitors. In conclusion, acidosis stimulates the AhR/c-Src axis only in breast cancer cells, increasing cell migration and MMP-9 activity. Although the AhR activation mechanism still remains elusive, a reduction in pHi may be thought to be involved. These findings suggest a critical role for the AhR/c-Src axis in breast tumor progression stimulated by an acidic microenvironment.


Asunto(s)
Acidosis , Neoplasias de la Mama , Neoplasias de la Mama/metabolismo , Proteína Tirosina Quinasa CSK , Línea Celular Tumoral , Movimiento Celular , Femenino , Humanos , Metaloproteinasa 9 de la Matriz/metabolismo , Proteínas Tirosina Quinasas/metabolismo , Receptores de Hidrocarburo de Aril/metabolismo , Transducción de Señal , Microambiente Tumoral
7.
Mol Pharmacol ; 101(6): 381-389, 2022 06.
Artículo en Inglés | MEDLINE | ID: mdl-35383108

RESUMEN

The organic anion transporting polypeptide family member (OATP) 1B3 is a hepatic uptake transporter that has a broad substrate recognition and plays a significant role in regulating elimination of endogenous biomolecules or xenobiotics. OATP1B3 works in tandem with OATP1B1, with which it shares approximately 80% sequence homology and a high degree of substrate overlap. Despite some substrates being recognized solely by OATP1B3, its ability to compensate for loss of OATP1B1-mediated elimination and recognition by regulatory agencies, little is known about OATP1B3 regulatory factors and how they are involved with drug-drug interaction. It was recently discovered that OATP1B1 function is mediated by the activity of a particular tyrosine kinase that is sensitive to a variety of tyrosine kinase inhibitors (TKIs). This study reports that OATP1B3 is similarly regulated, as at least 50% of its activity is reduced by 20 US Food and Drug Administration -approved TKIs. Nilotinib was assessed as the most potent OATP1B3 inhibitor among the investigated TKIs, which can occur at clinically relevant concentrations and acted predominantly through noncompetitive inhibition without impacting membrane expression. Finally, OATP1B3 function was determined to be sensitive to the knockdown of the Lck/Yes novel tyrosine kinase that is sensitive to nilotinib and has been previously implicated in mediating OATP1B1 activity. Collectively, our findings identify tyrosine kinase activity as a major regulator of OATP1B3 function which is sensitive to kinase inhibition. Given that OATP1B1 is similarly regulated, simultaneous disruption of these transporters can have drastic effects on systemic drug concentrations, which would promote adverse events. SIGNIFICANCE STATEMENT: The organic anion transporting polypeptide family member (OATP) 1B3 is a facilitator of hepatic drug elimination, although much is unknown of how OATP1B3 activity is mediated, or how such regulators contribute to drug-drug interactions. This study reports that OATP1B3 activity is dependent on the Lck/Yes novel tyrosine kinase, which is sensitive to numerous tyrosine kinase inhibitors. These findings provide insight into the occurrence of many clinical drug-drug interactions, and a rationale for future study of tyrosine kinases regulating drug disposition.


Asunto(s)
Transportadores de Anión Orgánico , Proteínas Tirosina Quinasas , Interacciones Farmacológicas , Transportador 1 de Anión Orgánico Específico del Hígado/metabolismo , Proteínas de Transporte de Membrana/metabolismo , Transportadores de Anión Orgánico/metabolismo , Transportadores de Anión Orgánico Sodio-Independiente/metabolismo , Inhibidores de Proteínas Quinasas/farmacología , Proteínas Tirosina Quinasas/metabolismo , Miembro 1B3 de la Familia de los Transportadores de Solutos de Aniones Orgánicos/metabolismo
8.
Front Endocrinol (Lausanne) ; 12: 640298, 2021.
Artículo en Inglés | MEDLINE | ID: mdl-33841333

RESUMEN

Glioblastomas are the most common and aggressive primary brain tumors in adults, and patients with glioblastoma have a median survival of 15 months. Some alternative therapies, such as Src family kinase inhibitors, have failed presumably because other signaling pathways compensate for their effects. In the last ten years, it has been proven that sex hormones such as progesterone (P4) can induce growth, migration, and invasion of glioblastoma cells through its intracellular progesterone receptor (PR), which is mostly known for its role as a transcription factor, but it can also induce non-genomic actions. These non-classic actions are, in part, a consequence of its interaction with cSrc, which plays a significant role in the progression of glioblastomas. We studied the relation between PR and cSrc, and its effects in human glioblastoma cells. Our results showed that P4 and R5020 (specific PR agonist) activated cSrc protein since both progestins increased the p-cSrc (Y416)/cSrc ratio in U251 and U87 human glioblastoma derived cell lines. When siRNA against the PR gene was used, the activation of cSrc by P4 was abolished. The co-immunoprecipitation assay showed that cSrc and PR interact in U251 cells. P4 treatment also promoted the increase in the p-Fak (Y397) (Y576/577)/Fak and the decrease in p-Paxillin (Y118)/Paxillin ratio, which are significant components of the focal adhesion complex and essential for migration and invasion processes. A siRNA against cSrc gene blocked the increase in the p-Fak (Y576/Y577)/Fak ratio and the migration induced by P4, but not the decrease in p-Paxillin (Y118)/Paxillin ratio. We analyzed the potential role of cSrc over PR phosphorylation in three databases, and one putative tyrosine residue in the amino acid 87 of PR was found. Our results showed that P4 induces the activation of cSrc protein through its PR. The latter and cSrc could interact in a bidirectional mode for regulating the activity of proteins involved in migration and invasion of glioblastomas.


Asunto(s)
Neoplasias Encefálicas/metabolismo , Proteína Tirosina Quinasa CSK/metabolismo , Glioblastoma/metabolismo , Receptores de Progesterona/metabolismo , Línea Celular Tumoral , Movimiento Celular , Proliferación Celular/efectos de los fármacos , Proteína-Tirosina Quinasas de Adhesión Focal/metabolismo , Adhesiones Focales/metabolismo , Humanos , Invasividad Neoplásica , Paxillin/metabolismo , Fosforilación , Progesterona/metabolismo , Proteínas Tirosina Quinasas/metabolismo , ARN Interferente Pequeño/metabolismo , Transducción de Señal/efectos de los fármacos , Tirosina/química
9.
Med Princ Pract ; 30(3): 253-261, 2021.
Artículo en Inglés | MEDLINE | ID: mdl-33601387

RESUMEN

OBJECTIVES: The aim of the study was to study the Janus kinase/tyrosine kinase-activated transduction factor (JAK/STAT) signaling pathway and myogenesis on the masseter muscle after sleep deprivation and to investigate the role of stress in this scenario. SUBJECTS AND METHODS: A total of 18 male Wistar rats were divided into the following groups: control (n = 6): animals were not submitted to any procedures, and paradoxical sleep deprivation and vehicle (PSD + V; n = 6): animals were subjected to PSD for 96 h and (PSD + MET; n = 6): animals were subjected to PSD for 96 h with administration of metyrapone. Paradoxical sleep deprivation was performed by the modified multiple platforms method. Histopathological analysis, histomorphometry, and immunohistochemistry were performed. RESULTS: The results showed the presence of inflammatory infiltrate in the PSD + V and PSD + MET groups and atrophy. Histomorphometry showed that the cellular profile area decreased, while cellular density increased in both experimental groups. Expression of p-STAT 3, MyoD, and MyoG increased in the PSD + V group, while the PSD + MET group showed increased expression of IL-6 and p-STAT 3. CONCLUSION: Our results suggest that sleep deprivation induces an inflammatory response and atrophy in the masseter muscle of rats.


Asunto(s)
Atrofia/etiología , Quinasas Janus/metabolismo , Músculo Masetero , Desarrollo de Músculos , Atrofia Muscular/etiología , Proteínas Tirosina Quinasas/metabolismo , Privación de Sueño/complicaciones , Animales , Masculino , Metirapona/efectos adversos , Ratas , Ratas Wistar , Transducción de Señal/efectos de los fármacos , Privación de Sueño/inducido químicamente , Privación de Sueño/metabolismo
10.
Hematol Oncol Stem Cell Ther ; 14(3): 192-198, 2021 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-33290717

RESUMEN

ROS proto-oncogene 1 (ROS1) encodes a type I integral membrane protein with tyrosine kinase activity and whose activating alterations are involved in the aggressiveness of several tumor types. Fusions involving ROS1 gene are present in 1-2% of lung adenocarcinomas and other solid tumors. Entrectinib, also known as RXDX-101, is a potent second-generation, multitarget oral inhibitor against NTRK1, NTRK2, NTRK3, ALK, and ROS1 with the ability to cross the blood-brain barrier. Results of Phase I and II trials have led the Food and Drug Administration to grant approval to entrectinib for the treatment of patients with metastatic, ROS1-positive non-small cell lung cancer (NSCLC). In this review, we will describe the biology of ROS1, as well as results of the efficacy and safety of different clinical trials evaluating entrectinib in ROS1-positive NSCLC.


Asunto(s)
Benzamidas/uso terapéutico , Carcinoma de Pulmón de Células no Pequeñas , Indazoles/uso terapéutico , Neoplasias Pulmonares , Proteínas Tirosina Quinasas/metabolismo , Proteínas Proto-Oncogénicas/metabolismo , Carcinoma de Pulmón de Células no Pequeñas/tratamiento farmacológico , Carcinoma de Pulmón de Células no Pequeñas/metabolismo , Carcinoma de Pulmón de Células no Pequeñas/patología , Ensayos Clínicos Fase I como Asunto , Ensayos Clínicos Fase II como Asunto , Humanos , Neoplasias Pulmonares/tratamiento farmacológico , Neoplasias Pulmonares/metabolismo , Neoplasias Pulmonares/patología , Proto-Oncogenes Mas
11.
Toxicol In Vitro ; 66: 104871, 2020 Aug.
Artículo en Inglés | MEDLINE | ID: mdl-32325111

RESUMEN

Bisphenol A (BPA) is an industrial synthetic chemical used in the production of polycarbonate plastics and epoxy resins. Human exposition to BPA is primarily through eating food, and drinking liquids, because BPA can leach from polycarbonate plastic containers, beverage cans and epoxy resins. BPA induces proliferation and migration in human breast cancer cells. The G protein-coupled estrogen receptor (GPER) is a G protein-coupled receptor coupled with Gs proteins that is activated by estrogen and estrogenic compounds and it is the receptor for BPA. However, the signal transduction pathways that mediate migration via BPA/GPER in triple negative breast cancer (TNBC) cells has not been studied in detail. Here, we demonstrate that BPA induces an increase of GPER expression and activation of FAK, Src and ERK2, and an increase of focal adhesion assembly via GPER in TNBC MDA-MB-231 cells. Moreover, BPA induces FAK and ERK2 activation, focal adhesion assembly and migration via epidermal growth factor receptor (EGFR) transactivation. Collectively our data showed that BPA via GPER and/or EGFR transactivation induces activation of signal transduction pathways that mediate migration in TNBC MDA-MB-231 cells.


Asunto(s)
Compuestos de Bencidrilo/toxicidad , Adhesiones Focales/efectos de los fármacos , Fenoles/toxicidad , Plastificantes/toxicidad , Proteínas Tirosina Quinasas/metabolismo , Receptores de Estrógenos/metabolismo , Receptores Acoplados a Proteínas G/metabolismo , Neoplasias de la Mama Triple Negativas/metabolismo , Línea Celular Tumoral , Movimiento Celular/efectos de los fármacos , Humanos , Receptores de Estrógenos/genética , Receptores Acoplados a Proteínas G/genética
12.
Theriogenology ; 148: 174-179, 2020 May.
Artículo en Inglés | MEDLINE | ID: mdl-32182525

RESUMEN

Heparin is the most commonly used in vitro capacitation inducer in the bovine. However, hyaluronic acid (HA) has been recently used for capacitation induction as well as for other reproductive biotechnologies, such as sperm selection and in vitro fertilization (IVF). Our aim was to induce sperm capacitation with heparin or HA in order to study mAC and TK intracellular signals and their relation with cleavage and blastocyst rates after IVF as well as with the oxidative status of the potential bovine embryos. 2,5-dideoxyadenosine and genistein were used as mAC and TK inhibitors, respectively. Sperm capacitation was analyzed using CTC technique, sperm plasma membrane and acrosome integrity were determined using trypan blue stain and differential interference contrast, and mitochondrial activity was evaluated using fluorochrome JC-1. Cleavage rate was analyzed 48h and blastocyst production 7-8 days after IVF, while cytosolic oxidative activity was determined using RedoxSensor Red CC-1 fluorochrome 7h after IVF. When mAC and TK inhibitors were added to sperm samples, only capacitation decreased significantly both in HA and heparin treated samples (P < 0.05), but plasma membrane and acrosome integrity percentages were not affected in any of these groups (P > 0.05). Sperm mitochondrial membrane potential only decreased in heparin treated samples in the presence of both inhibitors (P < 0.05). Oocytes activated with HA sperm treated samples with the addition of 2,5-dideoxyadenosine and genistein presented a lower cytosolic oxidative status than those activated with sperm treated with HA alone (P < 0.05). On the other hand, oocytes activated with heparin treated sperm samples presented a lower cytosolic oxidative status only in the presence of 2,5-dideoxyadenosine (P < 0.05). Therefore, mAC and TK present a differential participation in heparin and HA sperm induced capacitation and mitochondrial function as well as in IVF.


Asunto(s)
Adenilil Ciclasas/metabolismo , Fertilización In Vitro/veterinaria , Ácido Hialurónico/farmacología , Proteínas Tirosina Quinasas/metabolismo , Capacitación Espermática/efectos de los fármacos , Animales , Bovinos , Membrana Celular/efectos de los fármacos , Membrana Celular/enzimología , Criopreservación/veterinaria , Didesoxiadenosina/administración & dosificación , Didesoxiadenosina/farmacología , Quimioterapia Combinada , Genisteína/administración & dosificación , Genisteína/farmacología , Heparina/administración & dosificación , Heparina/farmacología , Masculino
13.
Curr Top Med Chem ; 20(3): 227-243, 2020.
Artículo en Inglés | MEDLINE | ID: mdl-31976834

RESUMEN

The phenylamino-pyrimidine (PAP) nucleus has been demonstrated to be useful for the development of new drugs and is present in a wide variety of antiretroviral agents and tyrosine kinase inhibitors (TKIs). This review aims to evaluate the application of PAP derivatives in drugs and other bioactive compounds. It was concluded that PAP derivatives are still worth exploring, as they may provide highly competitive ATP TKI's with nano/picomolar activity.


Asunto(s)
Antirretrovirales/farmacología , VIH-1/efectos de los fármacos , Inhibidores de Proteínas Quinasas/farmacología , Proteínas Tirosina Quinasas/antagonistas & inhibidores , Compuestos de Anilina , Antirretrovirales/química , Humanos , Estructura Molecular , Inhibidores de Proteínas Quinasas/química , Proteínas Tirosina Quinasas/metabolismo , Pirimidinas
14.
Future Med Chem ; 11(17): 2273-2285, 2019 09.
Artículo en Inglés | MEDLINE | ID: mdl-31581913

RESUMEN

Background: Carboranylanilinoquinazoline-hybrids, developed for boron neutron capture therapy, have demonstrated cytotoxicity against murine-glioma cells with EGFR-inhibition ability. In addition, their adequate aqueous/metabolic stabilities and ability to cross blood-brain barrier make them good leads as to become antiglioma drugs. Aim: Analyze drug-like properties of representative carboranylanilinoquinazolines. Materials & methods: To expand carboranylanilinoquinazolines therapeutic spectrum, we studied their ability to act against glioma-mammal cells, U-87 MG and other tyrosine kinase-overexpress cells, HT-29. Additionally, we predicted theoretically and studied experimentally drug-like properties, in other words, organization for economic cooperation and development-recommended toxicity-studies and, due to some aqueous-solubility problems, and vehicularization for oral and intravenous administrations. Conclusion: We have identified a promising drug-candidate with broad activity spectrum, appropriate drug-like properties, adequate toxicological behavior and able ability to be loaded in suitable vehicles.


Asunto(s)
Compuestos de Anilina/química , Antineoplásicos/química , Neoplasias Encefálicas/radioterapia , Receptores ErbB/antagonistas & inhibidores , Glioma/radioterapia , Inhibidores de Proteínas Quinasas/química , Quinazolinas/química , Compuestos de Anilina/farmacología , Animales , Antineoplásicos/farmacología , Barrera Hematoencefálica/metabolismo , Terapia por Captura de Neutrón de Boro/métodos , Línea Celular Tumoral , Supervivencia Celular , Colesterol/química , Composición de Medicamentos/métodos , Desarrollo de Medicamentos , Liberación de Fármacos , Femenino , Humanos , Liposomas/química , Ratones , Ratones Endogámicos BALB C , Modelos Moleculares , Fosfatidilcolinas/química , Poliaminas/química , Polietilenos/química , Polipropilenos/química , Inhibidores de Proteínas Quinasas/farmacología , Proteínas Tirosina Quinasas/metabolismo , Quinazolinas/farmacología , Solubilidad , Agua
15.
Biochem Biophys Res Commun ; 519(3): 597-604, 2019 11 12.
Artículo en Inglés | MEDLINE | ID: mdl-31540690

RESUMEN

INTRODUCTION: Multiple myeloma (MM) remains incurable due to high rates of relapse after various treatment regimens. WEE1 is a cell cycle related gene that regulates the G2/M checkpoint and promotes cell cycle suspension for consequent DNA repair. To date, there are clinical studies for the evaluation of WEE1 inhibitors in the treatment of solid tumors and studies on cell lines of non-MM hematological tumors. OBJECTIVES: To perform in vitro functional studies to verify the effect of the inhibition of WEE1 on MM cell lines viability and its potential as therapeutic target. MATERIAL AND METHODS: WEE1 expression was evaluated in 22 newly diagnosed MM patients and in four MM cell lines, RPMI-8226, U266 and SKO-007 and SK-MM2, by quantitative real-time PCR (qPCR). After treatment with the WEE1 inhibitor (MK-1775), with or without proteasome inhibitor (bortezomib) pretreatment, we assessed cell viability through Prestoblue functional test, microspheres formation in soft agar, and induction of apoptosis and cell cycle alterations by flow cytometry. RESULTS: All MM cell lines showed WEE1 expression by qPCR. RPMI-8226 and U266 showed a 50% reduction in cell viability after 24 h of incubation with MK-1775, at concentrations of 5 µM and 20 µM, respectively. SKO-007 showed dose and time dependence to this drug. Combination therapy with bortezomib and MK-1775 abolished the formation of soft agar microspheres in the RPMI-8226 cell line (also responsive to the use of both drugs) and U266, but SKO-007 was resistant to all drugs, isolated and combined. However, treatment of bortezomib followed by MK-1775 (sequential treatment) versus bortezomib alone showed statistically significant impact on cell lines total apoptosis: 88.8% vs 74.1% in RPMI-8222 (confirmed by cell cycle experiments); 92.5% vs 86.6% in U266; and 60.2% 30.9% on SKO-007 (p < 0.05). CONCLUSION: The sequential combination of bortezomib and WEE1 inhibitor, MK-1775, induced apoptosis in RPMI-8226, U266, and especially SKO-007 cell lines, more efficiently than the use of the same isolated drugs, highlighting its effect in inhibition of proliferation of tumor cells in MM cell lines. Our data suggest that WEE1 can figure as a MM target and that the sequential combination of bortezomib and MK-1775 may be explored in future clinical trials.


Asunto(s)
Antineoplásicos/farmacología , Apoptosis/efectos de los fármacos , Bortezomib/farmacología , Proteínas de Ciclo Celular/antagonistas & inhibidores , Mieloma Múltiple/tratamiento farmacológico , Inhibidores de Proteínas Quinasas/farmacología , Proteínas Tirosina Quinasas/antagonistas & inhibidores , Pirazoles/farmacología , Pirimidinonas/farmacología , Proteínas de Ciclo Celular/genética , Proteínas de Ciclo Celular/metabolismo , Proliferación Celular/efectos de los fármacos , Supervivencia Celular/efectos de los fármacos , Relación Dosis-Respuesta a Droga , Combinación de Medicamentos , Ensayos de Selección de Medicamentos Antitumorales , Femenino , Humanos , Masculino , Persona de Mediana Edad , Mieloma Múltiple/patología , Proteínas Tirosina Quinasas/genética , Proteínas Tirosina Quinasas/metabolismo , Relación Estructura-Actividad , Células Tumorales Cultivadas
16.
Behav Brain Res ; 359: 66-72, 2019 02 01.
Artículo en Inglés | MEDLINE | ID: mdl-30347225

RESUMEN

Introduction Evidence suggests early life stress impairs development, quality of life and increases vulnerability to disease. One important aspect of the stress experience is its impact on cognitive-motor performance, which includes the ability to adapt walking according to the environmental conditions. This study aimed to investigate how early-life stress affects walking adaptability of mice, while investigating BDNF/TrkB and Drd1/Drd2 expression in different brain regions. Methods Briefly, we exposed male C56BL/6 to the limited bedding protocol (LB) from post-natal day (PND) 2 to PND9 and then tested animals in the ladder walking task at PND60. RT-qPCR was used to investigate gene expression in the mPFC, hippocampus, motor cortex and cerebellum 2 h after the task Results LB induced a wide range of variability and therefore two distinct subgroups of animals within the LB group were established: a) superior performance (LB-SP); and b) inferior performance (LB-IP), compared to controls. Additionally, Drd1 gene expression was increased in the mPFC of LB-IP animals and in the cerebellum of LB-SP animals, while Drd2 expression was reduced in the hippocampus of the LB-IP group. BDNF exon IV gene expression in the mPFC and motor cortex was increased in both the LB-IP and LB-SP subgroups. TrkB gene expression in the hippocampus was reduced in the LB-IP group. A strong negative correlation was found between walking adaptability performance and BDNF exon IV gene expression in the motor cortex. Conversely, a positive correlation was found between walking adaptability performance and TrkB expression in the mPFC and a negative correlation in the hippocampus. Both Drd1 and Drd2 gene expression were negatively correlated with the ability to adapt walking. Conclusions Overall, our findings suggest exposure to early life stress leads to distinct walking adaptability phenotypes, which may be related to Drd1, Drd2, Bdnf exon IV and TrkB gene expression in brain regions that influence walking adaptability.


Asunto(s)
Encéfalo/metabolismo , Estrés Psicológico/fisiopatología , Caminata , Adaptación Fisiológica/fisiología , Adaptación Psicológica/fisiología , Animales , Ansiedad/fisiopatología , Encéfalo/crecimiento & desarrollo , Factor Neurotrófico Derivado del Encéfalo/metabolismo , Regulación de la Expresión Génica , Masculino , Glicoproteínas de Membrana/metabolismo , Ratones Endogámicos C57BL , Modelos Animales , Fenotipo , Proteínas Tirosina Quinasas/metabolismo , Receptores de Dopamina D1/metabolismo , Receptores de Dopamina D2/metabolismo , Caminata/fisiología
17.
Theriogenology ; 122: 68-73, 2018 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-30243136

RESUMEN

Hyaluronic acid is a glycosaminoglycan present in uterine and oviductal fluids in female ruminants, which has been used as a sperm capacitation inducer prior to in vitro fertilization in several species. CD44 is a specific hyaluronic acid receptor, present in the sperm plasma membrane, but its signaling transduction system has not been elucidated yet. Our aim was to study protein kinase C and tyrosine kinase participation in intracellular signaling and oxidative metabolism in hyaluronic acid-induced capacitation of cryopreserved bull spermatozoa. Sperm capacitation was induced with hyaluronic acid or heparin. GF-109203× and genistein were used as protein kinase C and tyrosine kinase inhibitors, respectively. Capacitation, sperm plasma membrane and acrosome integrity were studied using CTC and trypan blue - DIC, while variations in enzymatic activities were determined by spectrophotometry. The inhibition of protein kinase C and tyrosine kinase blocked hyaluronic acid and heparin induced capacitation. Metabolic enzymes such as NADP-dependent isocitrate and malate dehydrogenases participate in hyaluronic acid capacitation, in coincidence with a lower mitochondrial metabolism compared with heparin. On the other hand, NAD-dependent isocitrate and malate dehydrogenase were not modified by hyaluronic acid induction. These dehydrogenases were also modulated by protein kinase C and tyrosine kinase in the capacitation induced by heparin or hyaluronic acid. In conclusion, hyaluronic acid intracellular signal system involves protein kinase C and tyrosine kinase activities, which may modulate capacitation in cryopreserved bull sperm with a lower oxidative metabolism than heparin.


Asunto(s)
Bovinos/metabolismo , Ácido Hialurónico/farmacología , Proteína Quinasa C/metabolismo , Proteínas Tirosina Quinasas/metabolismo , Capacitación Espermática/efectos de los fármacos , Animales , Criopreservación/veterinaria , Oxidación-Reducción , Preservación de Semen/veterinaria , Transducción de Señal , Capacitación Espermática/fisiología
18.
J Neurochem ; 146(6): 686-702, 2018 09.
Artículo en Inglés | MEDLINE | ID: mdl-29851427

RESUMEN

Astrocytes are glial cells that help maintain brain homeostasis and become reactive in neurodegenerative processes releasing both harmful and beneficial factors. We have demonstrated that brain-derived neurotrophic factor (BDNF) expression is induced by melanocortins in astrocytes but BDNF actions in astrocytes are largely unknown. We hypothesize that BDNF may prevent astrocyte death resulting in neuroprotection. We found that BDNF increased astrocyte viability, preventing apoptosis induced by serum deprivation by decreasing active caspase 3 and p53 expression. The anti-apoptotic action of BDNF was abolished by ANA-12 (a specific TrkB antagonist) and by K252a (a general Trk antagonist). Astrocytes only express the BDNF receptor TrkB-truncated isoform 1, TrkB-T1. BDNF induced ERK, Akt, and Src (a non-receptor tyrosine kinase) activation in astrocytes. Blocking ERK and Akt pathways abolished BDNF protection in serum deprivation-induced cell death. Moreover, BDNF protected astrocytes from death by 3-nitropropionic acid (3-NP), an effect also blocked by ANA-12, K252a, and inhibitors of ERK, calcium, and Src. BDNF reduced reactive oxygen species levels induced in astrocytes by 3-NP and increased xCT expression and glutathione levels. Astrocyte-conditioned medium (ACM) from untreated astrocytes partially protected PC12 neurons, whereas ACM from BDNF-treated astrocytes completely protected PC12 neurons from 3-NP-induced apoptosis. Both ACM from control and BDNF-treated astrocytes markedly reduced reactive oxygen species levels induced by 3-NP in PC12 cells. Our results demonstrate that BDNF protects astrocytes from cell death through TrkB-T1 signaling, exerts an antioxidant action, and induces release of neuroprotective factors from astrocytes. OPEN PRACTICES: Open Science: This manuscript was awarded with the Open Materials Badge. For more information see: https://cos.io/our-services/open-science-badges/.


Asunto(s)
Apoptosis/efectos de los fármacos , Astrocitos/efectos de los fármacos , Astrocitos/metabolismo , Factor Neurotrófico Derivado del Encéfalo/farmacología , Glicoproteínas de Membrana/metabolismo , Fármacos Neuroprotectores/farmacología , Receptor trkB/metabolismo , Transducción de Señal/efectos de los fármacos , Animales , Apoptosis/genética , Azepinas/farmacología , Benzamidas/farmacología , Carbazoles/farmacología , Ciclo Celular/efectos de los fármacos , Células Cultivadas , Medio de Cultivo Libre de Suero/toxicidad , Inhibidores Enzimáticos/farmacología , Regulación de la Expresión Génica/efectos de los fármacos , Regulación de la Expresión Génica/genética , Alcaloides Indólicos/farmacología , Glicoproteínas de Membrana/genética , Células PC12 , Proteínas Tirosina Quinasas/metabolismo , Ratas , Ratas Wistar , Especies Reactivas de Oxígeno/metabolismo , Receptor trkB/genética
19.
J Cell Biochem ; 119(7): 5885-5892, 2018 07.
Artículo en Inglés | MEDLINE | ID: mdl-29575149

RESUMEN

The accumulation of fatty acids in the liver associated with obesity condition is also known as nonalcoholic fatty liver disease (NAFLD). The impaired fat oxidation in obesity condition leads to increased hepatic fat accumulation and increased metabolic syndrome risk. On the other hand, physical exercise has been demonstrated as a potent strategy in the prevention of NAFLD. Also, these beneficial effects of exercise occur through different mechanisms. Recently, the Cdc2-like kinase (CLK2) protein was associated with the suppression of fatty acid oxidation and hepatic ketogenesis. Thus, obese animals demonstrated elevated levels of hepatic CLK2 and decreased fat acid oxidation. Here, we explored the effects of chronic physical exercise in the hepatic metabolism of obese mice. Swiss mice were distributed in Lean, Obese (fed with high-fat diet during 16 weeks) and Trained Obese group (fed with high-fat diet during 16 weeks and exercised (at 60% exhaustion velocity during 1 h/5 days/week) during 8 weeks. In our results, the obese animals showed insulin resistance, increased hepatic CLK2 content and increased hepatic fat accumulation compared to the Lean group. Otherwise, the chronic physical exercise improved insulin resistance state, prevented the increased CLK2 in the liver and attenuated hepatic fat accumulation. In summary, these data reveal a new protein involved in the prevention of hepatic fat accumulation after chronic physical exercise. More studies can evidence the negative role of CLK2 in the control of liver metabolism, contributing to the improvement of insulin resistance, obesity, and type 2 diabetes.


Asunto(s)
Resistencia a la Insulina , Lipogénesis , Hígado/enzimología , Obesidad/terapia , Condicionamiento Físico Animal , Proteínas Serina-Treonina Quinasas/metabolismo , Proteínas Tirosina Quinasas/metabolismo , Delgadez/fisiopatología , Animales , Dieta Alta en Grasa/efectos adversos , Metabolismo de los Lípidos , Ratones , Ratones Endogámicos C57BL , Ratones Obesos , Obesidad/enzimología , Obesidad/etiología , Proteínas Serina-Treonina Quinasas/genética , Proteínas Tirosina Quinasas/genética
20.
Curr Oncol Rep ; 20(1): 4, 2018 01 30.
Artículo en Inglés | MEDLINE | ID: mdl-29383451

RESUMEN

The introduction of tyrosine kinase inhibitors (TKI) has dramatically changed the outcome of chronic myeloid leukemia (CML). Over the last decade, imatinib positioned itself as the gold standard of care, until second-generation TKIs were introduced as first-line treatment. Multiple therapeutic options available today in CML make the decision of the first-line therapy a difficult choice. However, a gap still exists, in the management of CML outside academic centers. Important advances in molecular monitoring have been developed worldwide; nevertheless, monitoring in the "real world" continues to be a challenge in part because international scale (IS) standardized laboratories are not available worldwide, and also because physicians still have some resource barriers and lack of familiarity restricting guideline adoption and consider optimal molecular monitoring a challenge. This review addresses CML first-line treatment, monitoring aspects and giving practical advice, identifying prognostic factors, and guiding management of CML for non-academic centers.


Asunto(s)
Leucemia Mielógena Crónica BCR-ABL Positiva/tratamiento farmacológico , Inhibidores de Proteínas Quinasas/uso terapéutico , Proteínas Tirosina Quinasas/metabolismo , Humanos
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