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Lysine adducts between methyltetrahydrophthalic anhydride and collagen in guinea pig lung

Jönsson, Bo A LU ; Wishnok, J S; Skipper, P L; Stillwell, W G and Tannenbaum, S R (1995) In Toxicology and Applied Pharmacology 135(1). p.156-162
Abstract
The formation of adducts between methyltetrahydrophthalic anhydride (MTHPA), an important industrial chemical and potent allergen, and collagen from guinea pig lung tissue was investigated. Collagen peptides were obtained from the lung tissue by homogenization, defatting, washing, and digestion with collagenase. In experiments in vitro, lung tissue was exposed to 8.4 mumol (50 microCi) of 14C MTHPA. The amount of adducts was 97 nmol MTHPA/g of wet tissue as determined from the bound radioactivity. In a study in vivo, four guinea pigs were injected intratracheally with 8.4 mumol of 14C MTHPA each. The amount of adducts was 0-1.2 nmol MTHPA/g of wet tissue (determined by bound radioactivity). N epsilon-methyltetrahydrophthaloyl-L-lysine... (More)
The formation of adducts between methyltetrahydrophthalic anhydride (MTHPA), an important industrial chemical and potent allergen, and collagen from guinea pig lung tissue was investigated. Collagen peptides were obtained from the lung tissue by homogenization, defatting, washing, and digestion with collagenase. In experiments in vitro, lung tissue was exposed to 8.4 mumol (50 microCi) of 14C MTHPA. The amount of adducts was 97 nmol MTHPA/g of wet tissue as determined from the bound radioactivity. In a study in vivo, four guinea pigs were injected intratracheally with 8.4 mumol of 14C MTHPA each. The amount of adducts was 0-1.2 nmol MTHPA/g of wet tissue (determined by bound radioactivity). N epsilon-methyltetrahydrophthaloyl-L-lysine (MTHPL) was synthesized and characterized by NMR, UV, and mass spectrometry (MS). A method to analyze MTHPL, after derivatization with methanol and pentafluorobenzoyl chloride, using gas chromatography-MS was developed. Analysis of Pronase-digested MTHPA-exposed lung tissue showed a concentration of 19 nmol MTHPL/g wet lung in vitro and between 0 and 0.15 nmol MTHPL/g wet lung in vivo. Thus, 20% in vitro and 12-15% in vivo of the bound radioactivity was found as adducts with lysine. These results are a first step toward studies of allergenic epitopes in proteins and methods for biological monitoring of exposure to acid anhydrides. (Less)
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author
publishing date
type
Contribution to journal
publication status
published
subject
in
Toxicology and Applied Pharmacology
volume
135
issue
1
pages
156 - 162
publisher
Academic Press
external identifiers
  • pmid:7482535
  • scopus:0028838750
ISSN
1096-0333
DOI
10.1006/taap.1995.1218
language
English
LU publication?
no
id
853e03e0-4270-49ae-979f-bbcbe00489c0 (old id 1108980)
date added to LUP
2008-07-25 11:38:34
date last changed
2017-01-01 07:04:12
@article{853e03e0-4270-49ae-979f-bbcbe00489c0,
  abstract     = {The formation of adducts between methyltetrahydrophthalic anhydride (MTHPA), an important industrial chemical and potent allergen, and collagen from guinea pig lung tissue was investigated. Collagen peptides were obtained from the lung tissue by homogenization, defatting, washing, and digestion with collagenase. In experiments in vitro, lung tissue was exposed to 8.4 mumol (50 microCi) of 14C MTHPA. The amount of adducts was 97 nmol MTHPA/g of wet tissue as determined from the bound radioactivity. In a study in vivo, four guinea pigs were injected intratracheally with 8.4 mumol of 14C MTHPA each. The amount of adducts was 0-1.2 nmol MTHPA/g of wet tissue (determined by bound radioactivity). N epsilon-methyltetrahydrophthaloyl-L-lysine (MTHPL) was synthesized and characterized by NMR, UV, and mass spectrometry (MS). A method to analyze MTHPL, after derivatization with methanol and pentafluorobenzoyl chloride, using gas chromatography-MS was developed. Analysis of Pronase-digested MTHPA-exposed lung tissue showed a concentration of 19 nmol MTHPL/g wet lung in vitro and between 0 and 0.15 nmol MTHPL/g wet lung in vivo. Thus, 20% in vitro and 12-15% in vivo of the bound radioactivity was found as adducts with lysine. These results are a first step toward studies of allergenic epitopes in proteins and methods for biological monitoring of exposure to acid anhydrides.},
  author       = {Jönsson, Bo A and Wishnok, J S and Skipper, P L and Stillwell, W G and Tannenbaum, S R},
  issn         = {1096-0333},
  language     = {eng},
  number       = {1},
  pages        = {156--162},
  publisher    = {Academic Press},
  series       = {Toxicology and Applied Pharmacology},
  title        = {Lysine adducts between methyltetrahydrophthalic anhydride and collagen in guinea pig lung},
  url          = {http://dx.doi.org/10.1006/taap.1995.1218},
  volume       = {135},
  year         = {1995},
}