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21 results on '"Urrutia, Mariela"'

4. Dissection of binding interactions in the complex between the anti-lysozyme antibody HyHEL-63 and its antigen

Author

Li, Yili, Urrutia, Mariela, Smith-Gill, Sandra J., and Mariuzza, Roy A.

Subjects
Biochemistry -- Research, Alanine -- Physiological aspects, Mutagenesis -- Analysis, X-ray crystallography -- Usage, Antigens -- Physiological aspects, Antibodies -- Genetic aspects, Lysozyme -- Genetic aspects, Lysozyme -- Physiological aspects, Viral antibodies, Biological sciences, Chemistry
Abstract

Research has been conducted on interface between anti-hen egg white lysozyme antibody HyHEL-63 and HEL. The use of X-ray crystallography, alanine-scanning mutagenesis and double mutant cycles in characterizing this interface is described.

Published
2003

5. Estimation of the hydrophobic effect inan antigen-antibody protein-protein interface

Author

Sundberg, Eric J., Urrutia, Mariela, Braden, Bradford C., Isern, Jordi, Tsuchiya, Daisuke, Fields, Barry A., Malchiodi, Emilio L., Tormo, Jose, Schwarz, Frederick P., and Mariuzza, Roy A.

Subjects
Immune complexes -- Analysis, Protein binding -- Analysis, Proteins -- Structure, Lipids -- Physiological aspects, Biological sciences, Chemistry
Abstract

Research points out that in a protein-protein interface, the hydrophobic effect is dependent on surrounding environment prevailing at different sites. The hydrophobic effect at the interface between egg white lysozyme antibody and the enzyme is the same as that expected of hydrocrbon solubility models.

Published
2000

6. Hormonal Regulation of Follicle-Stimulating Hormone Glycosylation in Males

Author

Campo, Stella Maris, Andreone, Luz, Ambao, Veronica Ana, Urrutia, Mariela, Calandra, Ricardo Saul, and Rulli, Susana Beatriz

Subjects
0301 basic medicine, hormonal regulation, medicine.medical_specialty, endocrine system, Glycosylation, medicine.drug_class, Mini Review, Endocrinology, Diabetes and Metabolism, SERTOLI CELL, 030209 endocrinology & metabolism, Biology, Gonadotropic cell, lcsh:Diseases of the endocrine glands. Clinical endocrinology, 03 medical and health sciences, chemistry.chemical_compound, Follicle-stimulating hormone, Endocrinology, 0302 clinical medicine, Internal medicine, HORMONAL REGULATION, purl.org/becyt/ford/3.2 [https], medicine, Endocrine system, inhibin, Follicle-stimulating hormone glycosylation, FOLLICLE STIMULATING HORMONE, Gametogenesis, male gonad, lcsh:RC648-665, GLYCOSYLATION, Androgen, Sertoli cell, 030104 developmental biology, medicine.anatomical_structure, chemistry, INHIBIN, purl.org/becyt/ford/3 [https], MALE GONAD, Hormone
Abstract

The Follicle-Stimulating Hormone plays an important role in the regulation of gametogenesis. It is synthesized and secreted as a family of glycoforms with differing oligosaccharide structure, biological action, and half-life. The presence of these oligosaccharides is absolutely necessary for the full expression of hormone bioactivity at the level of the target cell. The endocrine milieu modulates the glycosylation of this hormone. During male sexual development a progressive increase in FSH sialylation and in the proportion of glycoforms bearing complex oligosaccharides are the main features in this physiological condition. In late puberty, FSH oligosaccharides are largely processed in the medial- and trans-Golgi cisternae of the gonadotrope and remain without changes throughout adult life. In experimental models, the absence of gonads severely affects FSH sialylation; androgen administration is able to restore the characteristics observed under physiological conditions. The expression of ST6 beta-galactoside alpha-2,6-sialyltransferase 1 is hormonally regulated in the male rat; it decreases after short periods of castration but increases markedly at longer periods of androgen deprivation. Although ST3 beta-galactoside alpha-2,3-sialyltransferase 3 is expressed in the male rat pituitary it is not influenced by changes in the endocrine milieu. The oligosaccharide structure of FSH has an impact on the Sertoli cell endocrine activity. In more advanced stages of Sertoli cell maturation, both sialylation and complexity of the oligosaccharides are involved in the regulation of inhibin B production; moreover, FSH glycoforms bearing incomplete oligosaccharides may enhance the stimulatory effect exerted by gonadal growth factors. In this review, we discuss available information on variation of FSH glycosylation and its hormonal regulation under different physiological and experimental conditions, as well as the effect on Sertoli cell endocrine activity. The Follicle-Stimulating Hormone plays an important role in the regulation of gametogenesis. It is synthesized and secreted as a family of glycoforms with differing oligosaccharide structure, biological action, and half-life. The presence of these oligosaccharides is absolutely necessary for the full expression of hormone bioactivity at the level of the target cell. The endocrine milieu modulates the glycosylation of this hormone. During male sexual development a progressive increase in FSH sialylation and in the proportion of glycoforms bearing complex oligosaccharides are the main features in this physiological condition. In late puberty, FSH oligosaccharides are largely processed in the medial- and trans-Golgi cisternae of the gonadotrope and remain without changes throughout adult life. In experimental models, the absence of gonads severely affects FSH sialylation; androgen administration is able to restore the characteristics observed under physiological conditions. The expression of ST6 beta-galactoside alpha-2,6-sialyltransferase 1 is hormonally regulated in the male rat; it decreases after short periods of castration but increases markedly at longer periods of androgen deprivation. Although ST3 beta-galactoside alpha-2,3-sialyltransferase 3 is expressed in the male rat pituitary it is not influenced by changes in the endocrine milieu. The oligosaccharide structure of FSH has an impact on the Sertoli cell endocrine activity. In more advanced stages of Sertoli cell maturation, both sialylation and complexity of the oligosaccharides are involved in the regulation of inhibin B production; moreover, FSH glycoforms bearing incomplete oligosaccharides may enhance the stimulatory effect exerted by gonadal growth factors. In this review, we discuss available information on variation of FSH glycosylation and its hormonal regulation under different physiological and experimental conditions, as well as the effect on Sertoli cell endocrine activity. Fil: Campo, Stella Maris. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones Endocrinológicas "Dr. César Bergada". Gobierno de la Ciudad de Buenos Aires. Centro de Investigaciones Endocrinológicas "Dr. César Bergada". Fundación de Endocrinología Infantil. Centro de Investigaciones Endocrinológicas "Dr. César Bergada"; Argentina Fil: Campo, Stella Maris. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones Endocrinológicas "Dr. César Bergada". Gobierno de la Ciudad de Buenos Aires. Centro de Investigaciones Endocrinológicas "Dr. César Bergada". Fundación de Endocrinología Infantil. Centro de Investigaciones Endocrinológicas "Dr. César Bergada"; Argentina Fil: Andreone, Luz. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones Endocrinológicas "Dr. César Bergada". Gobierno de la Ciudad de Buenos Aires. Centro de Investigaciones Endocrinológicas "Dr. César Bergada". Fundación de Endocrinología Infantil. Centro de Investigaciones Endocrinológicas "Dr. César Bergada"; Argentina Fil: Andreone, Luz. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones Endocrinológicas "Dr. César Bergada". Gobierno de la Ciudad de Buenos Aires. Centro de Investigaciones Endocrinológicas "Dr. César Bergada". Fundación de Endocrinología Infantil. Centro de Investigaciones Endocrinológicas "Dr. César Bergada"; Argentina Fil: Ambao, Veronica Ana. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones Endocrinológicas "Dr. César Bergada". Gobierno de la Ciudad de Buenos Aires. Centro de Investigaciones Endocrinológicas "Dr. César Bergada". Fundación de Endocrinología Infantil. Centro de Investigaciones Endocrinológicas "Dr. César Bergada"; Argentina Fil: Ambao, Veronica Ana. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones Endocrinológicas "Dr. César Bergada". Gobierno de la Ciudad de Buenos Aires. Centro de Investigaciones Endocrinológicas "Dr. César Bergada". Fundación de Endocrinología Infantil. Centro de Investigaciones Endocrinológicas "Dr. César Bergada"; Argentina Fil: Urrutia, Mariela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones Endocrinológicas "Dr. César Bergada". Gobierno de la Ciudad de Buenos Aires. Centro de Investigaciones Endocrinológicas "Dr. César Bergada". Fundación de Endocrinología Infantil. Centro de Investigaciones Endocrinológicas "Dr. César Bergada"; Argentina Fil: Urrutia, Mariela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones Endocrinológicas "Dr. César Bergada". Gobierno de la Ciudad de Buenos Aires. Centro de Investigaciones Endocrinológicas "Dr. César Bergada". Fundación de Endocrinología Infantil. Centro de Investigaciones Endocrinológicas "Dr. César Bergada"; Argentina Fil: Calandra, Ricardo Saul. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina Fil: Calandra, Ricardo Saul. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina Fil: Rulli, Susana Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina Fil: Rulli, Susana Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina

Published
2019

10. Vaccine potential of antigen cocktails composed of recombinant Toxoplasma gondii TgPI-1, ROP2 and GRA4 proteins against chronic toxoplasmosis in C3H mice

Author

Picchio, Mariano S., primary, Sánchez, Vanesa R., additional, Arcon, Nadia, additional, Soto, Ariadna S., additional, Perrone Sibilia, Matías, additional, Aldirico, María de los Angeles, additional, Urrutia, Mariela, additional, Moretta, Rosalía, additional, Fenoy, Ignacio M., additional, Goldman, Alejandra, additional, and Martin, Valentina, additional

Published
2018
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12. Abstract A37: Immunization of cutaneous melanoma patients with the allogeneic cell vaccine CSF-470 enhances immune infiltration of metastatic lesions and would favor subsequent response to Vemurafenib

Author

Aris, Mariana, primary, Pampena, María Betina, additional, Levy, Estrella M., additional, Bravo, Alicia I., additional, Madorsky-Rowdo, Florencia P., additional, Mordoh, Ana, additional, Kaplan, Julio, additional, Baron, Antonela, additional, Urrutia, Mariela, additional, Blanco, Paula A., additional, Barrio, María Marcela, additional, and Mordoh, José, additional

Published
2015
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20. Single-domain llama antibodies as specific intracellular inhibitors of SpvB, the actin ADP-ribosylating toxin of Salmonella typhimurium.

Author

Alzogaray, Vanina, Danquah, Welbeck, Aguirre, Andrés, Urrutia, Mariela, Berguer, Paula, Véscovi, Eleonora García, Haag, Friedrich, Koch-Nolte, Friedrich, and Goldbaum, Fernando A.

Subjects
SALMONELLA typhimurium, MICROBIAL toxins, FOODBORNE diseases, SALMONELLA, ANTITOXINS, BORDETELLA pertussis, CORYNEBACTERIUM diseases, CELLS
Abstract

ADP-ribosylation of host cell proteins is a common mode of cell intoxication by pathogenic bacterial toxins. Antibodies induced by immunization with inactivated ADP-ribosylating toxins provide efficient protection in case of some secreted toxins, e.g., diphtheria and pertussis toxins. However, other ADP-ribosylating toxins, such as Salmonella SpvB toxin, are secreted directly from the Salmonella-containing vacuole into the cytosol of target cells via the SPI-2 encoded bacterial type III secretion system, and thus are inaccessible to conventional antibodies. Small-molecule ADP-ribosylation inhibitors are fraught with potential side effects caused by inhibition of endogenous ADP-ribosyltransferases. Here, we report the development of a single-domain antibody from an immunized llama that blocks the capacity of SpvB to ADP-ribosylate actin at a molar ratio of 1:1. The single-domain antibody, when expressed as an intrabody, effectively protected cells from the cytotoxic activity of a translocation-competent chimeric C2IN-C/SpvB toxin. Transfected cells were also protected against cytoskeletal alterations induced by wild-type SpvB-expressing strains of Salmonella. This proof of principle paves the way for developing new antidotes against intracellular toxins. [ABSTRACT FROM AUTHOR]

Published
2011
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21. Estimation of the Hydrophobic Effect in an Antigen-Antibody Protein-Protein Interface.

Author

Sundberg, Eric J. and Urrutia, Mariela

Subjects
*HYDROPHOBIC surfaces, *LYSOZYMES, *IMMUNOGLOBULINS, *CHEMICAL reactions, *REACTIVITY (Chemistry)
Abstract

Investigates the role of hydrophobic interactions in stabilizing the complex between the Fv fragment of the anti-hen egg white lysozyme (HEL) antibody D1.3 and HEL. Structures of wild-type and mutant FvD1.3-HEL complexes; Thermodynamic properties of association in the wild-type and mutant complexes; Hydrophobic effect in the D1.3-HEL interface.

Published
2000
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