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Tyrosine‐rich acidic matrix protein (TRAMP) is a tyrosine‐sulphated and widely distributed protein of the extracellular matrix
Author(s) -
Forbes Euan G.,
Cronshaw Andrew D.,
MacBeath Jonathan R.E.,
Hulmes David J.S.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00907-4
Subject(s) - tramp , tyrosine , extracellular matrix , immunoprecipitation , biochemistry , lysyl oxidase , polyclonal antibodies , chemistry , matrix (chemical analysis) , viral matrix protein , microbiology and biotechnology , biology , antibody , immunology , gene , transgene , chromatography
Tyrosine‐rich acidic matrix protein (TRAMP; 22 kDa extracellular matrix protein; dermatopontin) is a protein that co‐purifies with lysyl oxidase and with dermatan sulphate proteoglycans, with possible functions in cell—matrix interactions and matrix assembly. Using a rabbit polyclonal antiserum raised against porcine TRAMP, which cross‐reacts with both the human and murine forms of the protein, we show by immunoblotting that TRAMP has a widespread tissue distribution, including skin, skeletal muscle, heart, lung, kidney, cartilage and bone. In cultures of human skin fibroblasts, TRAMP incorporates both [ 35 S]sulphate and [ 3 H]tyrosine and is secreted into the medium, as shown by immunoprecipitation. Amino acid analysis of immunoprecipitated TRAMP demonstrates that many of the tyrosine residues in TRAMP are sulphated.