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1.
Rev Med Chil ; 140(1): 93-7, 2012 Jan.
Article in Spanish | MEDLINE | ID: mdl-22552562

ABSTRACT

Male accessory sexual glands arising in ovarian cystic teratoma are exceedingly rare. We report a 56-year-old female subjected to an ovariohysterectomy due to a left ovarian mass. The pathological study of the surgical piece revealed a tumor composed of different mature tissue elements and well defined nodules of benign prostatic tissue.


Subject(s)
Dermoid Cyst/pathology , Ovarian Neoplasms/pathology , Prostate/pathology , Teratoma/pathology , Acid Phosphatase , Dermoid Cyst/chemistry , Female , Humans , Male , Middle Aged , Ovarian Neoplasms/chemistry , Prostate/chemistry , Prostate-Specific Antigen/analysis , Protein Tyrosine Phosphatases/analysis , Teratoma/chemistry
2.
Rev. méd. Chile ; 140(1): 93-97, ene. 2012. ilus
Article in Spanish | LILACS | ID: lil-627614

ABSTRACT

Male accessory sexual glands arising in ovarian cystic teratoma are exceedingly rare. We report a 56-year-old female subjected to an ovariohysterectomy due to a left ovarian mass. The pathological study of the surgical piece revealed a tumor composed of different mature tissue elements and well defined nodules of benign prostatic tissue.


Subject(s)
Female , Humans , Male , Middle Aged , Dermoid Cyst/pathology , Ovarian Neoplasms/pathology , Prostate/pathology , Teratoma/pathology , Dermoid Cyst/chemistry , Ovarian Neoplasms/chemistry , Prostate-Specific Antigen/analysis , Prostate/chemistry , Protein Tyrosine Phosphatases/analysis , Teratoma/chemistry
3.
Mem Inst Oswaldo Cruz ; 106(5): 546-52, 2011 Aug.
Article in English | MEDLINE | ID: mdl-21894374

ABSTRACT

Phosphorylation and dephosphorylation of protein tyrosine residues constitutes a major biochemical regulatory mechanism for the cell. We report a transient increase in the total tyrosine phosphorylation of the Aedes aegypti head during the first days after emergence from the pupal stage. This correlates with an initial reduction in total head protein tyrosine phosphatase (PTP) activity. Similarly, phosphotyrosine (pTyr)-containing bands are seen in extracts prepared from both male and female heads and are spread among a variety of structures including the antennae, proboscis and the maxillary palps combined with the proboscis. Also, mosquitoes treated with sodium orthovanadate, a classical PTP inhibitor, show reduced blood-feeding activity and higher head tyrosine phosphorylation levels. These results suggest that pTyr-mediated signalling pathways may play a role in the initial days following the emergence of the adult mosquito from the pupal stage.


Subject(s)
Aedes/enzymology , Protein Tyrosine Phosphatases/analysis , Aedes/growth & development , Animals , Female , Head , Male , Protein Tyrosine Phosphatases/metabolism , Pupa/enzymology
4.
Forensic Sci Int ; 206(1-3): 111-8, 2011 Mar 20.
Article in English | MEDLINE | ID: mdl-20692115

ABSTRACT

In the forensic laboratory the biological analyses for rape investigation commonly include vaginal swabs as sample material combined to biochemical tests including sperm cytology (SC) and detection of acid phosphatase activity (AP) and prostate-specific antigen (PSA, p30) for the conclusive identification of semen components. Most reports comparing these tests relied on analysis of semen samples or donor swabs taken under controlled conditions; however their individual or combined efficacy under real live sampling conditions in different laboratories is largely unknown. We carried out SC, APA and PSA analyses in vaginal swabs collected from casework rapes submitted to Mexican Forensic Laboratories at Texcoco and Toluca. On the basis of positive and negative results from each assay and sample, data were classified into eight categories (I-VIII) and compared with those obtained in the two only similar studies reported in Toronto, Canada and Hong Kong, China. SC and APA assays had the higher overall positivity in Toluca and Texcoco samples respectively and otherwise PSA had a lower but very similar positivity between these two laboratories. When compared to the previous studies some similarities were found, namely similar frequencies (at a ratio of approximately 1 out of 3) of samples being positive or negative by all techniques (Categories I and VI respectively) and a comparable overall positivity of APA and SC but higher than that of PSA. Indeed the combined results of using SC, APA and PSA tests was considered as conclusive for semen detection from approximately 1 out of 3 cases (Category I) to approximately 1 out of 2 cases in a scenario where at least SC is positive, strongly presumptive in 2 out of 3 cases (with at least one test positive) and the remainder 1 out of 3 cases (Category VI) suggested absence of semen. By determining Y-STR polymorphisms (12-loci) in additional samples obtained at Toluca laboratory, complete DNA profiles were determined from all Category I samples, none marker was detected from all Category VI samples and mostly partial profiles were obtained from samples of other categories. These observations give an overview on the variability in efficacy of each test performed at different laboratories and provide a general notion about the in praxis contribution of SC, APA and PSA tests for further DNA typing in the forensic analysis of rape.


Subject(s)
DNA Fingerprinting/methods , Prostate-Specific Antigen/analysis , Protein Tyrosine Phosphatases/analysis , Rape , Spermatozoa/cytology , Acid Phosphatase , Chromosomes, Human, Y , Female , Humans , Male , Polymerase Chain Reaction , Polymorphism, Genetic , Semen , Sensitivity and Specificity , Tandem Repeat Sequences , Vagina/chemistry , Vagina/cytology
5.
Arch Oral Biol ; 54(7): 642-50, 2009 Jul.
Article in English | MEDLINE | ID: mdl-19414171

ABSTRACT

OBJECTIVE: Low molecular weight protein tyrosine phosphatases (LMW-PTPs) are a family of enzymes strongly involved in the regulation of cell growth and differentiation. Since there is no information concerning the relationship between osteoblastic differentiation and LMW-PTP expression/activity, we investigated its involvement during human osteoblast-like cells (hFOB 1.19) differentiation. It is known that LMW-PTP is regulated by an elegant redox mechanism, so we also observed how the osteoblastic differentiation affected the reduced glutathione levels. DESIGN: hFOB 1.19 cells were cultured in DMEM/F12 up to 35 days. The osteoblast phenotype acquisition was monitored by measuring alkaline phosphatase activity and mineralized nodule formation by Von Kossa staining. LMW-PTP activity and expression were measured using the p-nitrophenylphosphate as substrate and Western blotting respectively. Crystal violet assay determined the cell number in each experimental point. Glutathione level was determined by both HPLC and DNTB assays. RESULTS: LMW-PTP modulation was coincident with the osteoblastic differentiation biomarkers, such as alkaline phosphatase activity and presence of nodules of mineralization in vitro. Likewise LMW-PTP, the reduced glutathione-dependent microenvironment was modulated during osteoblastic differentiation. During this process, LMW-PTP expression/activity, as well as alkaline phosphatase and glutathione increased progressively up to the 21st day (p < 0.001) of culturing, decreasing thereafter. CONCLUSIONS: Our results clearly suggest that LMW-PTP expression/activity was rigorously modulated during osteoblastic differentiation, possibly in response to the redox status of the cells, since it seems to depend on suitable levels of reduced glutathione. In this way, we pointed out LMW-PTP as an important signaling molecule in osteoblast biology and bone formation.


Subject(s)
Glutathione/metabolism , Osteoblasts/physiology , Protein Tyrosine Phosphatases/metabolism , Proto-Oncogene Proteins/metabolism , Alkaline Phosphatase/analysis , Biomarkers/analysis , Blotting, Western , Calcification, Physiologic/physiology , Calcium Phosphates/analysis , Cell Count , Cell Differentiation/physiology , Cell Line , Cell Proliferation , Chromatography, High Pressure Liquid , Dinitrobenzenes , Glutathione/analysis , Haptens , Humans , Nitrophenols , Organophosphorus Compounds , Oxidation-Reduction , Oxidative Stress/physiology , Phenotype , Protein Tyrosine Phosphatases/analysis , Proto-Oncogene Proteins/analysis , Time Factors
6.
Biochem Biophys Res Commun ; 342(4): 1014-21, 2006 Apr 21.
Article in English | MEDLINE | ID: mdl-16513090

ABSTRACT

Reversible protein tyrosine phosphorylation is an essential signal transduction mechanism that regulates cell growth, differentiation, mobility, metabolism, and survival. Two genes coding for protein tyrosine phophatases, designed EhPTPA and EhPTPB, were cloned from Entamoeba histolytica. EhPTPA and EhPTPB proteins showed amino acid sequence identity of 37%, both EhPTPases showed similarity with Dictyostelium discoideum and vertebrate trasmembranal PTPases. mRNA levels of EhPTPA gene are up-regulated in trophozoites recovered after 96h of liver abscess development in the hamster model. EhPTPA protein expressed as a glutathione S-transferase fusion protein (GST::EhPTPA) showed enzymatic activity with p-nitrophenylphosphate as a substrate and was inhibited by PTPase inhibitors vanadate and molybdate. GST::EhPTPA protein selectively dephosphorylates a 130kDa phosphotyrosine-containing protein in trophozoite cell lysates. EhPTPA gene codifies for a 43kDa native protein. Up-regulation of EhPTPA expression suggests that EhPTPA may play an important role in the adaptive response of trophozoites during amoebic liver abscess development.


Subject(s)
Dysentery, Amebic/parasitology , Entamoeba histolytica/enzymology , Liver/parasitology , Protein Tyrosine Phosphatases/chemistry , Protein Tyrosine Phosphatases/metabolism , Amino Acid Sequence , Animals , Cloning, Molecular , Cricetinae , Enzyme Activation , Molecular Sequence Data , Protein Tyrosine Phosphatases/analysis , Sequence Homology, Amino Acid , Species Specificity
7.
Arch Androl ; 49(5): 343-9, 2003.
Article in English | MEDLINE | ID: mdl-12893510

ABSTRACT

Spermatozoa travel a long distance to meet and fertilize the oocyte, so sperm motility is a requisite for normal fertilization. Asthenozoospermia, or low sperm motility, is a common cause of human male infertility. This is a retrospective study (1992-1999) to document the prevalence of this pathology in infertile men and to clarify the probable factors associated to its etiology. The prevalence was 18.71% for asthenozoospermia and 63.13% for asthenozoospermia associated with oligo- and/or teratozoo-spermia; thus, 81.84% of the studied samples had altered motility. Leukocytospermia, the ratio of germ cells/sperm, anti-sperm antibodies, consistency, biochemical markers of accessory sex glands, and sperm response after swim-up were studied in normospermic (N), asthenozoospermic (A), and combined asthenozoospermic (C) samples. No significant difference was found in the frequency of leukocytospermia among groups. The rate of germ cells/(spermatozoa + germ cells) between C and N (p < .01) and C and A (p < .01) was statistically different, while no difference was found on comparing N and A. MAR-test over 40% was found in 6% of the A samples and 7.6% of the C, while no positive values were observed in the N group. The percentage of hyperviscous samples was higher in the low sperm motility samples than in the normal group. Data on concentration of the biochemical markers seem to be decreased in asthenozoospermia. Pure and combined asthenozoo-spermia showed different behavior in sperm recovery after swim-up. Two different asthenozoospermias could be defined: the pure one where sperm environment is involved (immunological factor, hyperviscosity, and secretory gland function) and the combined, where the testis is comprised.


Subject(s)
Oligospermia , Sperm Maturation/physiology , Sperm Motility/physiology , Spermatozoa/pathology , Acid Phosphatase , Antibodies/immunology , Argentina/epidemiology , Citric Acid/analysis , Fructose/analysis , Humans , Leukocyte Count , Leukocytosis/complications , Leukocytosis/physiopathology , Male , Oligospermia/epidemiology , Oligospermia/etiology , Oligospermia/physiopathology , Protein Tyrosine Phosphatases/analysis , Retrospective Studies , Semen/chemistry , Spermatozoa/immunology
8.
FEMS Microbiol Lett ; 220(2): 197-206, 2003 Mar 28.
Article in English | MEDLINE | ID: mdl-12670681

ABSTRACT

Procyclic forms of Trypanosoma brucei possess a phosphatase activity on their external cell surface. This activity, while it dephosphorylates [(32)P]phosphocasein, is inhibited weakly by NaF and tartrate but strongly by vanadate. In this work, we describe the presence of an external phosphatase activity in intact bloodstream forms of T. brucei. With p-nitrophenyl phosphate (pNPP) as substrate, these intact cells produced 3-5 nmol pNP min(-1) mg(-1), linearly for up to at least 30 min. The activity was not significantly increased by Mg(2+), Mn(2+), Ca(2+) and Co(2+), but was inhibited by vanadate, NaF, p-chloromercuribenzoate and Zn(2+) and was insensitive to okadaic acid. Membrane-enriched fractions of parasites contained an acid phosphatase activity, with a pH optimum in the range of 4.5-5.5. This activity hydrolyzed phosphotyrosine (40 nmol phosphate min(-1) mg(-1)) better than phosphothreonine or phosphoserine. Partial purification of this phosphatase yielded a single activity band following gel electrophoresis, a K(m) value of 0.29 mM with pNPP and was insensitive to the Fe(2+)/H(2)O(2)/ascorbate system.


Subject(s)
Protein Tyrosine Phosphatases/metabolism , Trypanosoma brucei brucei/enzymology , Animals , Cations, Divalent/metabolism , Cell Membrane/enzymology , Hydrogen-Ion Concentration , Life Cycle Stages , Nitrophenols/metabolism , Organophosphorus Compounds/metabolism , Oxidative Stress , Parasitemia/parasitology , Phosphotyrosine/metabolism , Protein Tyrosine Phosphatases/analysis , Protein Tyrosine Phosphatases/antagonists & inhibitors , Substrate Specificity , Trypanosoma brucei brucei/growth & development
9.
Endocrine ; 16(3): 227-34, 2001 Dec.
Article in English | MEDLINE | ID: mdl-11954667

ABSTRACT

Insulin resistance is known to play a pivotal role in type 2 diabetes. Senile individuals, besides being prone to insulin resistance and, consequently, to type 2 diabetes, manifest diseases of the central nervous system (CNS) that may be influenced by disturbances of insulin signaling in the brain, such as memory impairment, Parkinson disease, and Alzheimer disease. We investigated the expression and response to insulin of elements involved in the insulin-signaling pathway in the forebrain cortex and cerebellum of rats ages 1 d to 60 wk. The protein content of insulin receptors and SRC homology adaptor protein (SHC) did not change significantly along the time frame analyzed. However, insulin-induced tyrosine phosphorylation of the insulin receptor and SHC, and the association of SHC/growth factor receptor binding protein-2 (GRB2) decreased significantly from d 1 to wk 60 of life in both types of tissues. Moreover, the expression of SH protein tyrosine phosphatase-2 (SHP2), a tyrosine phosphatase involved in insulin signal transduction and regulation of the insulin signal, decreased significantly with age progression, in both the forebrain cortex and the cerebellum of rats. Thus, elements involved in the insulin-signaling pathway are regulated at the expression and/or functional level in the CNS, and this regulation may play a role in insulin resistance in the brain.


Subject(s)
Adaptor Proteins, Signal Transducing , Aging , Brain/metabolism , Insulin/metabolism , Signal Transduction , Animals , Cerebellum/metabolism , GRB2 Adaptor Protein , Insulin/blood , Insulin/pharmacology , Intracellular Signaling Peptides and Proteins , Male , Phosphorylation , Phosphotyrosine/metabolism , Prosencephalon/metabolism , Protein Phosphatase 2 , Protein Tyrosine Phosphatase, Non-Receptor Type 11 , Protein Tyrosine Phosphatase, Non-Receptor Type 6 , Protein Tyrosine Phosphatases/analysis , Proteins/analysis , Proteins/metabolism , Rats , Rats, Wistar , Receptor, Insulin/analysis , Receptor, Insulin/metabolism , SH2 Domain-Containing Protein Tyrosine Phosphatases , src Homology Domains
10.
Brain Res Bull ; 50(4): 229-39, 1999 Nov 01.
Article in English | MEDLINE | ID: mdl-10582521

ABSTRACT

Proteoglycans and glycosaminoglycans are elements of matrix. In the nervous system, glycosaminoglycans modulate neurite outgrowth and are co-receptors for growth factors playing a crucial role in cell differentiation and synaptogenesis. The receptor of protein tyrosine phosphatase beta (RPTPbeta) is a chondroitin sulphate proteoglycan which plays an important role in neural morphogenesis and axon guidance mechanisms. Pilocarpine-treated rats present status epilepticus, which is followed by a seizure-free period (silent), by a period of spontaneous recurrent seizures (chronic), and the hippocampus of these animals exhibits cell loss and mossy fiber sprouting. Thus, the synthesis of heparan sulphate and chondroitin sulphate and the time course of RPTPbeta immunoreactivity were studied in the hippocampus and cerebral cortex during these phases of pilocarpine-induced epilepsy. The results showed decreased synthesis of heparan sulphate during the acute phase and an increased synthesis of chondroitin sulphate during the silent period in the cortex and hippocampus. In control rats RPTPbeta immunoreactivity was detected only in glial cells. After 6 h of status epilepticus the RPTPbeta immunoreactivity was no longer detectable in the glial cells in both tissues and intense staining became evident in the matrix, surrounding CA3 and dentate gyrus and piriform cortex neurones. In the silent and chronic periods RPTPbeta immunoreactivity was mainly detected in neuronal somata and fibers of neurones of hippocampus and cortex. These changes show a selective variation of synthesis and expression of glycosaminoglycans and RPTPbeta in relation to epilepsy suggesting a molecular interplay between glia and neurones during seizures.


Subject(s)
Cerebral Cortex/metabolism , Epilepsy/metabolism , Glycosaminoglycans/biosynthesis , Hippocampus/metabolism , Pilocarpine/toxicity , Proteoglycans/biosynthesis , Animals , Chondroitin Sulfates/biosynthesis , Epilepsy/chemically induced , Heparitin Sulfate/biosynthesis , Male , Nerve Tissue Proteins/analysis , Protein Tyrosine Phosphatases/analysis , Rats , Rats, Wistar , Reaction Time/physiology , Receptor-Like Protein Tyrosine Phosphatases, Class 5 , Status Epilepticus/metabolism
11.
Rev. Fac. Odontol. Bauru ; 7(3/4): 85-93, jul.-dez. 1999. ilus, tab
Article in Portuguese | LILACS, BBO - Dentistry | ID: lil-298412

ABSTRACT

Nosso propósito foi avaliar a biocompatibilidade de dois materiais preparados com osso cortical bovino, um desproteinizado a 100ºC (Gen-Ox(R), Baumer S.A.) e outro a 1000ºC (preparado no laboratório de Bioquímica, FOB-USP). Esses materiais foram implantados em subcutâneo de ratos e, após 10, 20, 30 e 60 dias, os animais foram sacrificados e as peças histológicas removidas. As análises microscópicas mostraram uma reaçäo granulomatosa tipo corpo estranho de baixa renovaçäo contendo macrófagos e células gigantes multinucleadas em contato com o material, semelhante à implantaçäo subcutânea de osso autógeno ou alógeno mineralizado. Ao final do período experimental näo houve diferença significativa nos níveis das fosfatases ácidas nos grupos que receberam o osso cortical desproteinizado a 100 ou 1000ºC, mostrando que näo há diferença significativa entre os materiais testados. Podemos concluir que o osso cortical bovino, quer desproteinizado a 100ºC (Gen-Ox(R), Baumer S.A.) ou a 1000ºC (preparado em nosso laboratório) podem ser usados como material de preenchimento osteo-substituto e como potenciais carreadores das proteínas morfogenéticas do osso


Subject(s)
Animals , Male , Female , Rats , Biocompatible Materials/classification , Biocompatible Materials/chemical synthesis , Cattle , Acid Phosphatase/analysis , Implants, Experimental/standards , Biocompatible Materials/chemistry , Protein Tyrosine Phosphatases/analysis , Bone Transplantation/methods
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