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Biochemical evidence for a low molecular weight protein (profilin‐like protein) in hog thyroid gland and its involvement in actin polymerisation
Author(s) -
Fattoum Abdellatif,
Roustan Claude,
Feinberg Jeanne,
Pradel Louise-Anne
Publication year - 1980
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(80)80227-4
Subject(s) - research centre , humanities , art , chemistry , library science , computer science
Actin was characterized ubiquitously in muscle fibers and in non-muscle cells from the most primitive to the most advanced organisms. However, in nonmuscle cells, this protein is found together in microtilamentous and monomeric states (Fand G-actin, respectively). It has been suggested that cell constituents in non-muscle cells interact with G-actin to maintain it in non-polymerized form. In this context, it has been shown that a low molecular weight protein named profilin prevents the actin polymerisation [ 11. In thyroid cells actin microfilaments appear to be involved in the endocytotic process [2]. The organization of these microfilaments depends on the physiological state of the gland. The bundles of actin filaments in the resting gland are transformed into a net-. work in response to thyrotropin stimulation; concomitantly, an increase of the ratio G/F actin is observed [ 31. Here, we have initiated a search for effecters which may have an influence on the state of actin polymerisation in hog thyroid cells.