Role of Dietary Fibre from Bengal Gram (Cicer Arietinum) as Hypocholesterolaemic Agent- Effect on Erythrocyte Membrane-Bound Enzymes and Haemotological Parameters

1987 ◽  
Vol 41 (3-4) ◽  
pp. 193-201 ◽  
Author(s):  
Ann Thomas ◽  
Giridhari L. Soni ◽  
Rattan Singh
Keyword(s):  
Cicer Arietinum ◽  
Erythrocyte Membrane ◽  
Dietary Fibre ◽  
Bengal Gram ◽  
Membrane Bound ◽  
Membrane Bound Enzymes

Alterations in rat erythrocyte membrane due to hexachlorocyclohexane (technical) exposure

1998 ◽  
Vol 17 (11) ◽  
pp. 638-642 ◽  
Author(s):  
Pankaj Bhalla ◽  
Deepa Agrawal
Keyword(s):  
Membrane Fluidity ◽  
Erythrocyte Membrane ◽  
Osmotic Fragility ◽  
Structure And Function ◽  
Membrane Structure And Function ◽  
Hydrophobic Molecule ◽  
Erythrocyte Membrane Fluidity ◽  
Membrane Bound ◽  
And Function ◽  
Membrane Bound Enzymes

1 Hexachlorocyclohexane (HCH), an organochlorine pesticide having hydrophobic molecule is known to act on membranes. HCH mediated alterations in erythrocyte membrane occur through disorganization of the lipid bilayer. Therefore the changes in erythrocyte membrane fluidity, osmotic fragility and certain membrane bound enzymes were studied. Administration of HCH (technical) to rats at 5 mg/kg, orally, 5 days a week for 1, 2 and 3 months caused marked increase in erythrocyte membrane fluidity, osmotic fragility anddecreaseinlevelsofNa+, K+-ATPase, acetylcholinesterase in erythrocytes and glutathione in blood. 2 These changes indicate that HCH adversely affects membrane structure and function.

scholarly journals (2-Aminobenzothiazole)-Methyl-1,1-Bisphosphonic Acids: Targeting Matrix Metalloproteinase 13 Inhibition to the Bone

2021 ◽  
Vol 14 (2) ◽  
pp. 85
Author(s):  
Antonio Laghezza ◽  
Luca Piemontese ◽  
Leonardo Brunetti ◽  
Alessia Caradonna ◽  
Mariangela Agamennone ◽  
...  
Keyword(s):  
Acid Group ◽  
Biological Evaluation ◽  
Matrix Metalloproteinase 13 ◽  
In Silico Studies ◽  
Long Time ◽  
Membrane Bound ◽  
Bisphosphonic Acids ◽  
Membrane Bound Enzymes

Matrix Metalloproteinases (MMPs) are a family of secreted and membrane-bound enzymes, of which 24 isoforms are known in humans. These enzymes degrade the proteins of the extracellular matrix and play a role of utmost importance in the physiological remodeling of all tissues. However, certain MMPs, such as MMP-2, -9, and -13, can be overexpressed in pathological states, including cancer and metastasis. Consequently, the development of MMP inhibitors (MMPIs) has been explored for a long time as a strategy to prevent and hinder metastatic growth, but the important side effects linked to promiscuous inhibition of MMPs prevented the clinical use of MMPIs. Therefore, several strategies were proposed to improve the therapeutic profile of this pharmaceutical class, including improved selectivity toward specific MMP isoforms and targeting of specific organs and tissues. Combining both approaches, we conducted the synthesis and preliminary biological evaluation of a series of (2-aminobenzothiazole)-methyl-1,1-bisphosphonic acids active as selective inhibitors of MMP-13 via in vitro and in silico studies, which could prove useful for the treatment of bone metastases thanks to the bone-targeting capabilities granted by the bisphosphonic acid group.

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