Immunodetection of phosphotyrosine-containing proteins in the integument, fat body and haemocytes of the mediterranean fruit-fly Ceratitis capitata: Possible involvement in pupariation

Katsoris, Panagiotis; Tsakas, Sotiris; Bournazos, Stavros N.; Marmaras, Vassilis J.

doi:10.1016/0020-1790(91)90088-v

Cited by 5 publications

(1 citation statement)

References 18 publications

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“…7). By contrast, immunoblotting analysis using antibodies against phosphotyrosine (Katsoris et al, 1991) did not reveal any phosphorylated band co-migrating with enzyme activity (data not shown). Both results are in accordance with data for the granular tyrosinase from the epidermis of Manduca sexta (Hiruma and Riddiford, 1988).…”

Section: Resultsmentioning

confidence: 80%

Glycosylation and adhesiveness differentiate larval Ceratitis capitata tyrosinases

Charalambidis

Bournazos

Zervas

et al. 1994

Arch Insect Biochem Physiol

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Larval Ceratitrs capitata phenoloxidases (POs) from hemocytes, serum, integument, and fat body were analyzed. Two types of PO were recorded: the tyrosinase type found in hemocytes, serum, integument, and fat body and the laccase type found in integument. Tyrosinase from all larval tissues and integumental laccase as well, showed similarity in molecular weight (93 KDa), activation by Ocherichia coli at 5 m M Ca2+, and reactivity to antibodies raised against serum tyrosinase. However, the enzymes differed with respect to their glycosylation and adhesiveness. The serum and integumental enzyme forms contain concanavalin A reacting material, whereas hemocyte and integumental tyrosrnase(s) are adhesive. These differences in enzyme forms, although not influencing their substrate specificity, seem to give advantages to performing their function, i.e., the adhesive enzyme form facilitates the adherence to f. colicell wall and hemocyte surface (unpublished data) while the glycosylated form facilitated the secretion into serum. o

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Section: Resultsmentioning

confidence: 80%

Glycosylation and adhesiveness differentiate larval Ceratitis capitata tyrosinases

Charalambidis

Bournazos

Zervas

et al. 1994

Arch Insect Biochem Physiol

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Changes of protein tyrosine phosphorylation in third instar larval integument of the Mediterranean fruit fly, Ceratitis capitata

Zervas

Katsoris

Marmaras

2002

Arch Insect Biochem Physiol

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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.

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Expression of the major tyrosyl phosphoprotein of 54 KDa in the integument of the medfly Ceratitis capitata

Zervas

Katsoris

Marmaras

1994

Roux's Arch Dev Biol

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Immunodetection of phosphotyrosine-containing proteins in the integument, fat body and haemocytes of the mediterranean fruit-fly Ceratitis capitata: Possible involvement in pupariation

Cited by 5 publications

References 18 publications

Glycosylation and adhesiveness differentiate larval Ceratitis capitata tyrosinases

Glycosylation and adhesiveness differentiate larval Ceratitis capitata tyrosinases

Changes of protein tyrosine phosphorylation in third instar larval integument of the Mediterranean fruit fly, Ceratitis capitata

Expression of the major tyrosyl phosphoprotein of 54 KDa in the integument of the medfly Ceratitis capitata

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