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M Venegas

Publications and source records attributed to M Venegas.

At least 19 recordsLinked to original sources
PubMed2003

Thyrotropin-releasing hormone as a mediator of the central autonomic pathway controlling ovarian function.

We studied the effect of thyrotropin-releasing hormone (TRH) applied centrally on the sympathetic activity of the ovary in female rats. Intracerebroventricular (i.c.v.) administration of a dose of 25 ng/kg weight produced an increase in noradrenaline (NA) content at the ovary after 5 days of hormone administration. However, higher doses in a range up to 500 ng/kg weight decreased NA content at the ovary. At the celiac ganglia (where the cell bodies of sympathetic neurons projecting to the ovary originate) there was an accumulation of NA in spite of a decrease in tyrosine hydroxylase activity (T-OH). After cold exposure, opposite effects on T-OH activity and no effects on NA in ganglia and in ovary were obtained. Besides, i.v. injection of TRH only induced a decrease in ovarian NA. In contrast to the increase in T(3) plasma levels obtained after the cold-stress procedure, none of the i.c.v. doses of TRH used produced changes in T(3) plasma levels, strongly suggesting that the effect on sympathetic activity is mediated by a central effect of TRH acting as a putative activator of ovarian sympathetic nerves.

Adrenal Glands↗
PubMed2002

Changes in sympathetic nerve activity of the mammalian ovary during a normal estrous cycle and in polycystic ovary syndrome: Studies on norepinephrine release.

Although it has been known for many years that the ovary is innervated by catecholaminergic nerve fibers and much experimental evidence has strengthened the notion that catecholamines are physiologically involved in the control of ovarian function, scarce evidence has been presented as to the role of sympathetic activity in ovarian pathologies that affect reproductive function. The purpose of this article is to provide a succinct overview of the findings in this area and discuss them relative to the pathology of polycystic ovary syndrome, the most common ovarian pathology in women during their reproductive years.

Animals↗
PubMed2001

Long-Term treatment with cisapride and antibiotics in liver cirrhosis: effect on small intestinal motility, bacterial overgrowth, and liver function.

OBJECTIVES: Altered small-bowel motility, lengthening of the orocecal transit time, and small-intestinal bacterial overgrowth have been described in patients with liver cirrhosis. These changes might be related to the progressive course and poor prognosis of the disease. We investigated the effect of a long-term treatment with cisapride and an antibiotic regimen on small-intestinal motor activity, orocecal transit time, bacterial overgrowth, and some parameters of liver function. METHODS: Thirty-four patients with liver cirrhosis of different etiology entered in the study. They were randomly allocated to receive cisapride (12), an alternating regimen of norfloxacin and neomycin (12), or placebo (10) during a period of 6 months. At entry and at 3 and 6 months, a stationary small-intestinal manometry was performed, and orocecal transit time and small-intestinal bacterial overgrowth were also investigated using the H2 breath test. Liver function was estimated with clinical and laboratory measurements (Child-Pugh score). RESULTS: After 6 months, both cisapride and antibiotics significantly improved fasting cyclic activity, reduced the duration of orocecal transit time, and decreased small-intestinal bacterial overgrowth. Cisapride administration was followed also by an increase in the amplitude of contractions. No statistically significant variations in these parameters were observed with placebo. An improvement of liver function was observed at 3 and 6 months with both cisapride and antibiotics. CONCLUSIONS: Long-term treatment with cisapride or antibiotics reversed altered small-intestinal motility and bacterial overgrowth in patients with liver cirrhosis. These findings suggest a possible role for prokinetics and antibiotics as a modality of treatment in selected cases of decompensated cirrhosis.

Adult↗
PubMed1999

Effects of adrenalectomy on the stress-induced changes in ovarian sympathetic tone in the rat.

A 3-wk period of stress promotes the development of ovarian cysts in rats apparently mediated by increased sympathetic nerve activity and ovarian steroid secretion. After 11 wk of stress, these parameters are indistinguishable from nonstressed control rats. To study adrenal contribution, we adrenalectomized rats and studied the effect of 3-wk of cold/restraint stress (1.5 h/d) on them compared to intact animals. Adrenalectomy (ADX) increased ovarian norepinephrine (NE) release, the content of beta-adrenergic receptors (betaAR) and basal, but not isoproterenol (Iso)-induced, androgen secretion. Stress to intact animals increased NE release, decreased betaAR content, and Iso-induced, but not basal, androgen secretion from the ovary. ADX did not modify the response to stress. We propose a tonic inhibition by the adrenal gland on nerve activity of ovarian nerves. Stress overrides this inhibitory effect, and nerve activity downregulates betaAR, decreasing ovarian steroid secretion.

Adrenal Glands↗
PubMed1998

[Cholestatic hepatitis associated with piroxicam use. Case report].

Most nonsteroidal antiinflammatory drugs can produce hepatotoxicity. We report a 22 years old female who presented with an acute cholestatic hepatitis after a prolonged period of piroxicam use. Hepatitis was attributed to this drug since all markers for hepatitis virus (A, B, C, E, Epstein Barr, Cytomegalovirus and Herpex Simplex) were negative, autoimmune markers were negative, serum iron and ceruloplasmin were normal, there was a temporal relationship between the administration of piroxicam and the hepatitis, the histological picture was compatible with this etiology and the patient had a favorable evolution after the discontinuance of the drug. This type of hepatotoxicity is not common but it must be born in mind when patients must receive nonsteroidal antiinflammatory drugs for prolonged periods.

Adult↗
PubMed1989

Purification and immunochemical characterization of ascitic fluid glycoproteins containing certain tumor-associated and blood group antigen markers.

Ascitic fluids from patients with various types of cancer were screened for the CA 19-9 and CA 125 tumor-associated antigenic activities. Two fluids exhibiting the highest activities were tested for their binding to various lectin-Sepharose columns resulting in both being bound best to wheat germ agglutinin (WGA) Sepharose. The WGA column eluate of one fluid was further chromatographed by HPLC and three peaks were obtained with approximate molecular weights of 3.65 MDa, 664 kDa and 330 kDa, of which only the largest fraction contained the CA 19-9 activity. The fluids were also fractionated on a Sephacryl S-400 column with most of the activity being present in or near the void volume. Monoclonal antibodies were used to demonstrate that the purified glycoproteins also contained the blood group A determinant, the four Lewis determinants Le(a), Le(b), Le(x) and Le(y), and the sialylated-Le(x) determinant, while other antibody analyses failed to detect other blood group and/or carbohydrate sequence determinants. Some of the blood group expressions could be separated from the CA 19-9 and CA 125 active glycoproteins by adsorption with various lectins other than the WGA.

Antibodies, Monoclonal↗
PubMed1988

Tumor-associated blood group antigen expressions and immunoglobulins associated with tumors.

As outlined in Figures 1 and 2, the biosynthetic pathways for the expression of the A, B and H, and the Lewis determinant carbohydrate sequence structures, as well as sialylated structures, involves both type 1 and type 2 precursor chains (which may be present as glycolipids and N- or O-linked glycoproteins), and many glycosyltransferases. For tumor cells, there appears to be increased expressions of fucosyl- and sialyltransferases yielding such structures as the Le(x), sialyl-Le(a), and many other similar determinants, which are not found on the normal cell progenitor of the tumor. The types of structures expressed on tumor cells is dependent on the particular fucosyl-, sialyl- and other glycosyltransferase genes activated in the transformation and tumor progression events, the availability of the substrates for the glycosyltransferases (both the precursor sequences and the nucleotide-sugar substrates) which is partly dependent on metabolites available to the tumor mass, and on the genotype of the individual regarding particular glycosyltransferases. Both the loss of A, B and/or H blood group antigen expressions of tumor cells and the relative expressions of the Lewis and sialylated-oligosaccharide determinants may be a consequence of the competing biosynthetic pathways and the glycosyltransferases for common substrate sequences, as well as due to the loss of particular glycosyltransferases concomitant with transformation. All of these factors probably account for the variable expressions of the complex of carbohydrate sequence determinants when comparing tumor sections of different individuals as well as the heterogeneity of expression of particular determinants within a single tumor tissue section. As described above, the A, B and/or H determinants, and the precursor sequences, are also expressed to differing extents on epithelial cells depending on the tissue type and cellular location in the tissue. Thus, the differentiation state of the particular epithelial cell also determines the quantity and types of carbohydrate sequences expressed. However, because of the complex nature of the competing biosynthetic pathways for the carbohydrate sequences of glycolipids and glycoproteins, and the relative activations of fucosyl- and sialyltransferases of tumor cells, it would seem that simple deductions as to the state of differentiation of particular tumors with A, B, H and precursor sequence expressions is not warranted.(ABSTRACT TRUNCATED AT 400 WORDS)

Antibodies, Neoplasm↗
PubMed1988

Evidence that serum amyloid P component binds to mannose-terminated sequences of polysaccharides and glycoproteins.

Serum amyloid P component (SAP) is a normal human serum protein with pentraxin structure that has morphological and immunochemical identity to the amyloid P component found in normal tissue and amyloid deposits. In the presence of calcium, SAP binds to certain complex polysaccharides, including agarose and zymosan. While the binding of SAP to agarose involves interaction with a galactose pyruvate acetal, the ligand in zymosan has not been defined. In the present study we determined that SAP binds to ligand(s) in a soluble extract of zymosan prepared by alkaline hydrolysis, which contains the mannose oligosaccharide sequences alpha DMan1----3DMan and alpha DMan1----6DMan. SAP did not bind to the alkali-insoluble fraction of zymosan, which is predominantly a glucan polymer, and its binding to zymosan extract which had been absorbed with concanavalin A was markedly reduced, suggesting that mannose residues are involved in the binding of SAP to zymosan. We also demonstrated that SAP binds to the glycoproteins ovalbumin, thyroglobulin, beta-glucuronidase and C3bi, which contain mannose-terminated sequences, while it did not bind to native and desialized preparations of ovomucoid, alpha 1-acid glycoprotein and glycophorin, which lack terminal mannose residues. SAP did not bind to pneumococcal C polysaccharide or to N-acetylglucosamine oligosaccharides covalently linked to a protein carrier. The binding of SAP to ligand(s) in zymosan extract or ovalbumin was inhibited by the preincubation of SAP with either zymosan extract or ovalbumin glycopeptides, both of which share similar mannose oligosaccharide sequences. All of the SAP binding reactions required calcium, were maximal at approximately 1 mM calcium, and gave similar results whether purified SAP or SAP in serum was used. These findings indicate that mannose-terminated oligosaccharides of polysaccharides and glycoproteins represent a new class of ligands for SAP and suggest that SAP may function as a mannose-binding protein.

Calcium↗