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Changes of protein tyrosine phosphorylation in third instar larval integument of the Mediterranean fruit fly, Ceratitis capitata
Author(s) -
Zervas Christos G.,
Katsoris Panagiotis G.,
Marmaras Vassilis J.
Publication year - 2002
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.10025
Subject(s) - ceratitis capitata , biology , integument , tyrosine phosphorylation , tyrosine , phosphorylation , capitata , larva , metamorphosis , instar , biochemistry , botany , microbiology and biotechnology , pest analysis , tephritidae , brassica oleracea
Developmental analysis of the tyrosine protein phosphorylation levels in larval integument and partial characterization of the endogenous protein tyrosine kinase activity (PTK) in Ceratitis capitata are described in this study. Larval integument contains high levels of PTK activity at the early stages of the third instar, which progressively declines to low levels in the white pupal stage. An integumental 90‐kDa polypeptide was identified to have prominent endogenous PTK activity and follow a similar developmental pattern. The major integumental phosphotyrosine‐containing polypeptides have apparent molecular weights of 30, 41, 44, 46, and 54 kDa, respectively. Polypeptides with molecular weights of 62 and 73 kDa were identified as Ser/Thr‐containing phosphoproteins and were shown to exhibit high levels of phosphorylation at the middle stage of larval development. These differences are likely to be due to the higher activation state of the protein tyrosine kinase(s) at the early stages of larval development. Arch. Insect Biochem. Physiol. 50:9–20, 2002. © 2002 Wiley‐Liss, Inc.