Fifteen years of prothymosin alpha: contradictory past and new horizons

Citation
A. Pineiro et al., Fifteen years of prothymosin alpha: contradictory past and new horizons, PEPTIDES, 21(9), 2000, pp. 1433-1446
Citations number
127
Categorie Soggetti
Biochemistry & Biophysics
Journal title
PEPTIDES
ISSN journal
01969781 → ACNP
Volume
21
Issue
9
Year of publication
2000
Pages
1433 - 1446
Database
ISI
SICI code
0196-9781(200009)21:9<1433:FYOPAC>2.0.ZU;2-U
Abstract
Prothymosin alpha (ProT alpha) is a highly acidic and small protein of only 111 amino acids with an unusual primary structure. One would expected it t o play an essential role in the organism, as it has a wide distribution and is high conserved among mammals, yet its exact function remains elusive. D espite the number of effects described for ProT alpha, intracellular and ex tracellular, none are accepted as its physiological role. Furthermore, many other aspects of its biology still remain obscure. In this review, we disc uss the structural properties, location, gene family, functions and immunom odulatory activities of and cellular receptors for ProT alpha. These topics are addressed in an attempt to reconcile opposing outlooks while emphasizi ng those points where scant investigations do exist. We have also re-evalua ted some previous results in light of the structural properties of ProT alp ha and have found that molecular mimetism could be the underlying basis. Th is molecular mimicry hypothesis provides a clue that must nor be overlooked for a realistic appraisal of future results. (C) 2000 Elsevier Science Inc . All rights reserved.