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1.
Expert Opin Drug Metab Toxicol ; 9(8): 943-54, 2013 Aug.
Article in English | MEDLINE | ID: mdl-23621565

ABSTRACT

INTRODUCTION: Albumin and α1-acid glycoprotein (AGP) are two of the most abundant proteins found in plasma. Their effect on the pharmacokinetic profile of exogenous compounds has major implications to clinical practice. Recent exploration into their possible role as diagnostic markers underlines their significance, and provides highlights their potential in medicinal applications. AREAS COVERED: This review summarizes the current understanding behind albumin and AGP. Specifically, the review focuses on their structure, physiological function, and their potential use in diagnostics as biomarkers. The article lists and describes the most common methods, with a specific focus on their use in drug design and clinical practice. EXPERT OPINION: Human serum albumin and AGP play a significant role in clinical practice. Research on human serum albumin and AGP, as potential diagnostic biomarkers, has been so far successful, with the development of novel diagnostic methods for detecting ischemia-modified albumin in cardiac ischemia patients. While research into this particular aspect is still in its infancy, future research should make things somewhat clearer and provide a better insight into the true potential of plasma proteins as a whole.


Subject(s)
Orosomucoid/metabolism , Serum Albumin/metabolism , Biomarkers/blood , Biomarkers/metabolism , Humans , Myocardial Ischemia/diagnosis , Protein Binding/drug effects , Serum Albumin, Human
2.
Ceska Slov Farm ; 61(3): 93-100, 2012 Jun.
Article in Slovak | MEDLINE | ID: mdl-22913824

ABSTRACT

Neuritic plaques, which are situated in the brain of Alzheimer's disease (AD) patients, are composed mainly of peptides containing 40 or 42 amino acid residues known as ß-amyloid plaques (Aß). The Aß peptide is the result of the enzymatic cleavage of the amyloid precursor protein (APP). In the so-called amyloidogenic pathway, the ß-secretase enzyme releases a protein fragment (C99), which is subsequently metabolized by the enzyme γ-secretase. Monomer forms of Aß are turned into oligomer forms, which are the main cause of cellular neuronal death in AD patients. The following study is focused on γ-secretase inhibitors that can slow down the production or accumulation of pathologic Aß deposits. γ secretase inhibitors that reached different phases of clinical trials are particularly reported as well as other promising groups of these analogues.


Subject(s)
Alzheimer Disease/drug therapy , Amyloid Precursor Protein Secretases/antagonists & inhibitors , Alzheimer Disease/metabolism , Amyloid beta-Peptides/chemistry , Amyloid beta-Peptides/metabolism , Humans , Plaque, Amyloid/metabolism
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