Applications of Monoclonal Antibodies in Clinical Chemistry

SynopsisImmunoassays have markedly enlarged the armamentarium of the clinical chemist during the last twenty years. Radioimmunoassays and their variants, in particular, now provide evidence which is central to diagnosis and patient management in endocrinology and certain other disorders. Currently used methods employ labelled antigens in the radioimmunoassay (RIA) method first described for insulin by Yalow and Berson. The advent of monoclonal antibodies seems to remove the one major barrier to the use of methods based upon labelled antibodies–the immunoradiometric (IRMA) method as proposed by Miles and Hales. These procedures offer advantages of speed, sensitivity, working range, specificity and robustness which strongly suggest that they will replace RIA for the microdetermination of specific proteins. Nevertheless, their specificity is based upon the recognition of a single epitope on the antigen and thorough testing on varied patient material will be required before they can safely be adopted for routine use.

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Ultrastructural analysis of unique glycoconjugates in the rat olfactory system

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100124859 ◽

1992 ◽

Vol 50 (1) ◽

pp. 890-891

Author(s):

James E. Crandall ◽

Linda C. Hassinger ◽

Gerald A. Schwarting

Keyword(s):

Central Nervous System ◽

Nervous System ◽

Monoclonal Antibodies ◽

Olfactory System ◽

Olfactory Bulbs ◽

Temporal And Spatial Patterns ◽

Carbohydrate Epitopes ◽

Olfactory Systems ◽

Temporal And Spatial ◽

Cell Surface Glycoconjugates

Cell surface glycoconjugates are considered to play important roles in cell-cell interactions in the developing central nervous system. We have previously described a group of monoclonal antibodies that recognize defined carbohydrate epitopes and reveal unique temporal and spatial patterns of immunoreactivity in the developing main and accessory olfactory systems in rats. Antibody CC2 reacts with complex α-galactosyl and α-fucosyl glycoproteins and glycolipids. Antibody CC1 reacts with terminal N-acetyl galactosamine residues of globoside-like glycolipids. Antibody 1B2 reacts with β-galactosyl glycolipids and glycoproteins. Our light microscopic data suggest that these antigens may be located on the surfaces of axons of the vomeronasal and olfactory nerves as well as on some of their target neurons in the main and accessory olfactory bulbs.

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Structural and Chemical Studies of Pathological Fibers in Human Neurofibrillary Degeneration

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s042482010012031x ◽

1985 ◽

Vol 43 ◽

pp. 726-729

Author(s):

K.S. Kosik ◽

L.K. Duffy ◽

S. Bakalis ◽

C. Abraham ◽

D.J. Selkoe

Keyword(s):

Monoclonal Antibodies ◽

Alzheimer Disease ◽

Human Brain ◽

Neurofibrillary Tangles ◽

Morphological Analysis ◽

High Specificity ◽

Cytoskeletal Proteins ◽

Neuritic Plaque ◽

Protein Chemistry ◽

Chemical Studies

The major structural lesions of the human brain during aging and in Alzheimer disease (AD) are the neurofibrillary tangles (NFT) and the senile (neuritic) plaque. Although these fibrous alterations have been recognized by light microscopists for almost a century, detailed biochemical and morphological analysis of the lesions has been undertaken only recently. Because the intraneuronal deposits in the NFT and the plaque neurites and the extraneuronal amyloid cores of the plaques have a filamentous ultrastructure, the neuronal cytoskeleton has played a prominent role in most pathogenetic hypotheses.The approach of our laboratory toward elucidating the origin of plaques and tangles in AD has been two-fold: the use of analytical protein chemistry to purify and then characterize the pathological fibers comprising the tangles and plaques, and the use of certain monoclonal antibodies to neuronal cytoskeletal proteins that, despite high specificity, cross-react with NFT and thus implicate epitopes of these proteins as constituents of the tangles.

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