https://search.dev.ndltd.org/etd/milano/oai:air.unimi.it:2434/153542
type: CreativeWork
name: MORPHOLOGICAL FEATURES OF THE REPRODUCTIVE ORGANS IN DOMESTIC SPECIES IN RELATION TO WATER MOVEMENT CONTROL, HYPONUTRITION AND ENVIRONMENTAL INFLUENCES IN FETAL AND PREPUBERTAL LIFE, AND METABOLISM REGULATOR FACTORS.
description: AQPs are a class of small, hydrophobic, integral membrane proteins that are able to make the cell membrane 10 to 100 fold more permeable than the membranes lacking such channels. Based on studies with AQP1, it appears that AQPs exist in the plasma membrane as homotetramers. Each AQP monomer contains 2 hemi-pores, which fold together to form a water channel. Different aqps have different patterns of glycosylation. In the case of AQP1 the peptide backbone is roughly 28 kDa and the glycosylated forms range from 40 to 60 kDa in mass. Water transport activity of AQP1 is inhibited by mercurial ion, and the site of mercurial inhibition is the cysteine in the E loop. I have personally verified that using the bovine ovary granulosa cell swelling and shrinkage as a model for mercurial inhibition. The shortest pathway for water to reach the follicle antral cavity is the transcellular pathway directly through the cytoplasm of granulosa cells. In this first experiment we have considered the functional presence of Hg2+-sensitive Aqps in isolated granulosa cells assessing changes in cell volume in presence or absence of HgCl2. Each of the AQPs has an essentially unique pattern of expression among tissues and during development. In humans 13 AQPs have been identified to date although this number pales in comparison to the greater than 100 related proteins found in plants and bacteria. The landmark discovery of AQPs starts the era of molecular water channels, which has permeated virtually every branch of biology and medicine. A number of recent studies have revealed the importance of mammalian AQPs in both physiology and pathophysiology and have suggested that pharmacological modulation of aquaporin expression and activity may provide new tools for the treatment of variety of human disorders, such as brain edema, glaucoma, tumour growth, fertility and obesity in which water and small solute transport may be involved. Since multiple isoforms of AQPs are differentially expressed in ce…
abstract: AQPs are a class of small, hydrophobic, integral membrane proteins that are able to make the cell membrane 10 to 100 fold more permeable than the membranes lacking such channels. Based on studies with AQP1, it appears that AQPs exist in the plasma membrane as homotetramers. Each AQP monomer contains 2 hemi-pores, which fold together to form a water channel. Different aqps have different patterns of glycosylation. In the case of AQP1 the peptide backbone is roughly 28 kDa and the glycosylated forms range from 40 to 60 kDa in mass. Water transport activity of AQP1 is inhibited by mercurial ion, and the site of mercurial inhibition is the cysteine in the E loop. I have personally verified that using the bovine ovary granulosa cell swelling and shrinkage as a model for mercurial inhibition. The shortest pathway for water to reach the follicle antral cavity is the transcellular pathway directly through the cytoplasm of granulosa cells. In this first experiment we have considered the functional presence of Hg2+-sensitive Aqps in isolated granulosa cells assessing changes in cell volume in presence or absence of HgCl2. Each of the AQPs has an essentially unique pattern of expression among tissues and during development. In humans 13 AQPs have been identified to date although this number pales in comparison to the greater than 100 related proteins found in plants and bacteria. The landmark discovery of AQPs starts the era of molecular water channels, which has permeated virtually every branch of biology and medicine. A number of recent studies have revealed the importance of mammalian AQPs in both physiology and pathophysiology and have suggested that pharmacological modulation of aquaporin expression and activity may provide new tools for the treatment of variety of human disorders, such as brain edema, glaucoma, tumour growth, fertility and obesity in which water and small solute transport may be involved. Since multiple isoforms of AQPs are differentially expressed in ce…
author: M. Aralla
language: eng
keywords: aquaporins, fertility, metabolism, nutrition, Settore VET/01 - Anatomia degli Animali Domestici
date published: 2011-02-08
date modified: 2026-07-27T20:19:17Z
provider: Università degli Studi di Milano
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: Università degli Studi di Milano

PropertyValue
property ID: Handle
value: http://hdl.handle.net/2434/153542

PropertyValue
property ID: DOI
value: 10.13130/aralla-marina_phd2011-02-08